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• W2075074068 abstract "Adaptor and scaffolding proteins determine the cellular targeting, the spatial, and thereby the functional association of G protein-coupled seven-transmembrane receptors with co-receptors, transducers, and downstream effectors and the adaptors determine post-signaling events such as receptor sequestration through interactions, mainly with the C-terminal intracellular tails of the receptors. A library of tails from 59 representative members of the super family of seven-transmembrane receptors was probed as glutathione S-transferase fusion proteins for interactions with four different adaptor proteins previously proposed to be involved in post-endocytotic sorting of receptors. Of the two proteins suggested to target receptors for recycling to the cell membrane, which is the route believed to be taken by a majority of receptors, ERM (ezrin-radixin-moesin)-binding phosphoprotein 50 (EBP50) bound only a single receptor tail, i.e. the β2-adrenergic receptor, whereas N-ethylmaleimide-sensitive factor bound 11 of the tail-fusion proteins. Of the two proteins proposed to target receptors for lysosomal degradation, sorting nexin 1 (SNX1) bound 10 and the C-terminal domain of G protein-coupled receptor-associated sorting protein bound 23 of the 59 tail proteins. Surface plasmon resonance analysis of the binding kinetics of selected hits from the glutathione S-transferase pull-down experiments, i.e. the tails of the virally encoded receptor US28 and the δ-opioid receptor, confirmed the expected nanomolar affinities for interaction with SNX1. Truncations of the NK1 receptor revealed that an extended binding epitope is responsible for the interaction with both SNX1 and G protein-coupled receptor-associated sorting protein as well as with N-ethylmaleimide-sensitive factor. It is concluded that the tail library provides useful information on the general importance of certain adaptor proteins, for example, in this case, ruling out EBP50 as being a broad spectrum-recycling adaptor. Adaptor and scaffolding proteins determine the cellular targeting, the spatial, and thereby the functional association of G protein-coupled seven-transmembrane receptors with co-receptors, transducers, and downstream effectors and the adaptors determine post-signaling events such as receptor sequestration through interactions, mainly with the C-terminal intracellular tails of the receptors. A library of tails from 59 representative members of the super family of seven-transmembrane receptors was probed as glutathione S-transferase fusion proteins for interactions with four different adaptor proteins previously proposed to be involved in post-endocytotic sorting of receptors. Of the two proteins suggested to target receptors for recycling to the cell membrane, which is the route believed to be taken by a majority of receptors, ERM (ezrin-radixin-moesin)-binding phosphoprotein 50 (EBP50) bound only a single receptor tail, i.e. the β2-adrenergic receptor, whereas N-ethylmaleimide-sensitive factor bound 11 of the tail-fusion proteins. Of the two proteins proposed to target receptors for lysosomal degradation, sorting nexin 1 (SNX1) bound 10 and the C-terminal domain of G protein-coupled receptor-associated sorting protein bound 23 of the 59 tail proteins. Surface plasmon resonance analysis of the binding kinetics of selected hits from the glutathione S-transferase pull-down experiments, i.e. the tails of the virally encoded receptor US28 and the δ-opioid receptor, confirmed the expected nanomolar affinities for interaction with SNX1. Truncations of the NK1 receptor revealed that an extended binding epitope is responsible for the interaction with both SNX1 and G protein-coupled receptor-associated sorting protein as well as with N-ethylmaleimide-sensitive factor. It is concluded that the tail library provides useful information on the general importance of certain adaptor proteins, for example, in this case, ruling out EBP50 as being a broad spectrum-recycling adaptor. Interaction of receptors with adaptor and scaffolding proteins is important for their biogenesis, their cellular sorting and targeting to the cell membrane, and their function at the membrane in complex with transducer molecules and down-stream effector molecules as well as the subsequent internalization and post-endocytotic sorting of the receptors (1Brady A.E. Limbird L.E. Cell. Signal. 2002; 14: 297-309Crossref PubMed Scopus (212) Google Scholar, 2Hall R.A. Lefkowitz R.J. Circ. Res. 2002; 91: 672-680Crossref PubMed Scopus (175) Google Scholar). These interactions among receptors, adaptors, and scaffolding proteins are highly regulated processes that can be controlled by phosphorylation events (3Luttrell L.M. Lefkowitz R.J. J. Cell Sci. 2002; 115: 455-465Crossref PubMed Google Scholar), expression of receptor activating, or inactivating variants of adaptor proteins (4Fagni L. Worley P.F. Ango F. Science's STKE. 2002; (http://stke.sciencemag.org/cgi/content/full/sigtrans;2002/137/RE8)PubMed Google Scholar), by competition among adaptor proteins, and by competition between adaptor proteins and effector molecules (5Feng G.J. Kellett E. Scorer C.A. Wilde J. White J.H. Milligan G. J. Biol. Chem. 2003; 278: 33400-33407Abstract Full Text Full Text PDF PubMed Scopus (48) Google Scholar). For the large family of G protein-coupled seven-transmembrane segment receptors (7TM 1The abbreviations used are: 7TM, seven-transmembrane; GST, glutathione S-transferase; EBP50, ERM-binding phosphoprotein 50; SNX1, sorting nexin 1; GASP, G protein-coupled receptor-associated sorting protein; PAR1, protease-activated receptor 1; NSF, N-ethylmaleimide-sensitive factor; SPR, surface plasmon resonance; cGASP, C-terminal fragment GASP; 5-HT, 5-hydroxytryptamine; KOP, κ-opioid; H, histamine; M, muscarinic; SST, somatostatin; V, vasopressin; OT, oxytocin; MC, melanocortin; MCH, melanin-concentrating hormone; AT1, angiotensin II receptor type 1; DOP, δ-opioid; MOP, μ-opioid; GLP, glucagon-like peptide; mGlu, metabotropic glutamate; GABA, γ-aminobutyric acid; GABAA, γ-aminobutyric acid, type A; NK, tachykinin; D, dopamine; ERM, ezrin-radixin-moesin. receptors), this field is still in its infancy and only a rather sketchy picture has emerged of relative importance of specific adaptor and scaffolding proteins for the biogenesis, function, and desensitization of these receptors. Methods such as yeast two-hybrid screening, co-immunoprecipitation, and affinity chromatography using immobilized receptor fragments as bait have been used to identify potential receptor-binding proteins. The proposed functional roles of these interacting proteins are very diverse. Examples include promotion or inhibition of agonist-induced receptor internalization (6Xia Z. Gray J.A. Compton-Toth B.A. Roth B.L. J. Biol. Chem. 2003; 278: 21901-21908Abstract Full Text Full Text PDF PubMed Scopus (124) Google Scholar, 7Xu J. Paquet M. Lau A.G. Wood J.D. Ross C.A. Hall R.A. J. Biol. Chem. 2001; 276: 41310-41317Abstract Full Text Full Text PDF PubMed Scopus (105) Google Scholar, 8Hu L.A. Tang Y. Miller W.E. Cong M. Lau A.G. Lefkowitz R.J. Hall R.A. J. Biol. Chem. 2000; 275: 38659-38666Abstract Full Text Full Text PDF PubMed Scopus (131) Google Scholar), inhibition of mitogen-activated protein kinase activation (9Hu L.A. Chen W. Martin N.P. Whalen E.J. Premont R.T. Lefkowitz R.J. J. Biol. Chem. 2003; 278: 26295-26301Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar), regulation of constitutive activity (10Ango F. Prezeau L. Muller T. Tu J.C. Xiao B. Worley P.F. Pin J.P. Bockaert J. Fagni L. Nature. 2001; 411: 962-965Crossref PubMed Scopus (327) Google Scholar), retention of receptors in the endoplasmic reticulum (11Roche K.W. Tu J.C. Petralia R.S. Xiao B. Wenthold R.J. Worley P.F. J. Biol. Chem. 1999; 274: 25953-25957Abstract Full Text Full Text PDF PubMed Scopus (176) Google Scholar, 12Bermak J.C. Li M. Bullock C. Zhou Q.Y. Nat. Cell Biol. 2001; 3: 492-498Crossref PubMed Scopus (219) Google Scholar), coupling to second messenger systems (13Perroy J. El Far O. Bertaso F. Pin J.P. Betz H. Bockaert J. Fagni L. EMBO J. 2002; 21: 2990-2999Crossref PubMed Scopus (67) Google Scholar, 14Lezcano N. Mrzljak L. Eubanks S. Levenson R. Goldman-Rakic P. Bergson C. Science. 2000; 287: 1660-1664Crossref PubMed Scopus (151) Google Scholar, 15Tu J.C. Xiao B. Yuan J.P. Lanahan A.A. Leoffert K. Li M. Linden D.J. Worley P.F. Neuron. 1998; 21: 717-726Abstract Full Text Full Text PDF PubMed Scopus (702) Google Scholar), and spatial organization of synapses (16Sheng M. Kim E. J. Cell Sci. 2000; 113: 1851-1856Crossref PubMed Google Scholar). Thus, a number of cases have been described where a specific adaptor protein has been biochemically and/or functionally linked to a single or several related receptors. However, to what degree such interactions are of general importance for 7TM receptors or for specific subsets of receptors or, in fact, only a single or a few receptors is in most cases still unclear. To address the question of the importance of specific adaptor scaf-folding proteins for the function of 7TM receptors in general, we chose a systematic biochemical approach by establishing a library of 7TM receptor tails fused to glutathione S-transferase (GST). 7TM receptors expose several intracellular loops for potential interaction with intracellular proteins. However, it is especially the C-terminal tail of the receptors that interacts with adaptor and scaffolding proteins (17Innamorati G. Sadeghi H.M. Tran N.T. Birnbaumer M. Proc. Natl. Acad. Sci. U. S. A. 1998; 95: 2222-2226Crossref PubMed Scopus (108) Google Scholar, 18Trejo J. Coughlin S.R. J. Biol. Chem. 1999; 274: 2216-2224Abstract Full Text Full Text PDF PubMed Scopus (145) Google Scholar, 19Anborgh P.H. Seachrist J.L. Dale L.B. Ferguson S.S. Mol. Endocrinol. 2000; 14: 2040-2053PubMed Google Scholar, 20Bockaert J. Marin P. Dumuis A. Fagni L. FEBS Lett. 2003; 546: 65-72Crossref PubMed Scopus (178) Google Scholar, 21Cao T.T. Deacon H.W. Reczek D. Bretscher A. von Zastrow M. Nature. 1999; 401: 286-290Crossref PubMed Scopus (545) Google Scholar, 22Cong M. Perry S.J. Hu L.A. Hanson P.I. Claing A. Lefkowitz R.J. J. Biol. Chem. 2001; 276: 45145-45152Abstract Full Text Full Text PDF PubMed Scopus (116) Google Scholar, 23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar, 24Wang Y. Zhou Y. Szabo K. Haft C.R. Trejo J. Mol. Biol. Cell. 2002; 13: 1965-1976Crossref PubMed Scopus (107) Google Scholar, 25Tanowitz M. von Zastrow M. J. Biol. Chem. 2003; 278: 45978-45986Abstract Full Text Full Text PDF PubMed Scopus (136) Google Scholar). Although, for example, intracellular loop 3 is critically involved in the recognition process between the receptor and transducer/effector molecules such as the heterotrimeric G proteins and arrestins, these proteins also interact with parts of the C-terminal receptor tail (26Wong S.K. Neurosignals. 2003; 12: 1-12Crossref PubMed Scopus (109) Google Scholar, 27Cen B. Xiong Y. Ma L. Pei G. Mol. Pharmacol. 2001; 59: 758-764Crossref PubMed Scopus (63) Google Scholar, 28DeGraff J.L. Gurevich V.V. Benovic J.L. J. Biol. Chem. 2002; 277: 43247-43252Abstract Full Text Full Text PDF PubMed Scopus (69) Google Scholar, 29Schmidlin F. Roosterman D. Bunnett N.W. Am. J. Physiol. 2003; 285: C945-C958Crossref PubMed Google Scholar, 30Huttenrauch F. Nitzki A. Lin F.T. Honing S. Oppermann M. J. Biol. Chem. 2002; 277: 30769-30777Abstract Full Text Full Text PDF PubMed Scopus (84) Google Scholar). Thus, the tail contains recognition sequences and epitopes for effector as well as scaffolding proteins. Besides the so-called “helix VIII” region, i.e. a relatively short, amphipathic, and helical segment located between the intracellular end of TM-VII and a frequently occurring palmitoylated Cys motif, very little information is available concerning the secondary and tertiary structures of 7TM receptor tails, which in the available x-ray structures have appeared to be rather un-ordered (31Schwartz T.W. Holst B. Foreman J.C. Johansen T. Textbook of Receptor Pharmacology. CRC Press, Inc., Boca Raton, FL2003: 81-109Google Scholar). Nevertheless, it is known that recognition motifs for adaptor and scaffolding proteins in the tails can be coiled-coil domains or C-terminally located PDZ recognition sequences (32Sheng M. Sala C. Annu. Rev. Neurosci. 2001; 24: 1-29Crossref PubMed Scopus (997) Google Scholar, 33Burkhard P. Stetefeld J. Strelkov S.V. Trends Cell Biol. 2001; 11: 82-88Abstract Full Text Full Text PDF PubMed Scopus (798) Google Scholar). In this study, proteins proposed to be involved in post-endocytotic sorting of receptors were probed for interactions with the library of 7TM receptor tail-fusion proteins. The vast majority of 7TM receptors are internalized upon agonist stimulation. In the classical, arrestin-mediated pathway, the activated receptor is phosphorylated by G protein-coupled receptor kinases, which leads to recruitment of arrestin. Arrestin functions as an adaptor protein interacting with clathrin and AP2, thereby targeting the receptor to clathrin-coated pits and subsequent endocytosis. Following endocytosis, the receptors may enter one of two pathways (see Fig. 1). In the recycling pathway, which has been described for the β2-adrenergic receptor, the μ-opioid receptor, and the tachykinin NK1 receptor, the ligand dissociates in the acidic pH of the endosomal compartment and the receptor is dephosphorylated and subsequently returned to the plasma membrane. In contrast, in the lysosomal pathway used by the δ-opioid receptor and protease-activated receptor 1 (PAR1), the receptor is targeted for degradation in lysosomes. The mechanism behind this targeted sorting of receptors is poorly understood. However, a number of proteins have been proposed to govern the differential sorting event. ERM-binding phosphoprotein 50 (EBP50, also called Na+/H+-exchanger regulatory factor) and N-ethylmaleimide-sensitive factor (NSF) have both been suggested to be responsible for the recycling of the β2-adrenergic receptor (21Cao T.T. Deacon H.W. Reczek D. Bretscher A. von Zastrow M. Nature. 1999; 401: 286-290Crossref PubMed Scopus (545) Google Scholar, 22Cong M. Perry S.J. Hu L.A. Hanson P.I. Claing A. Lefkowitz R.J. J. Biol. Chem. 2001; 276: 45145-45152Abstract Full Text Full Text PDF PubMed Scopus (116) Google Scholar). In contrast, sorting nexin 1 (SNX1), which originally was demonstrated to be required for the lysosomal sorting of the epidermal growth factor receptor, was recently suggested to be involved in the lysosomal sorting of PAR1 as well (24Wang Y. Zhou Y. Szabo K. Haft C.R. Trejo J. Mol. Biol. Cell. 2002; 13: 1965-1976Crossref PubMed Scopus (107) Google Scholar, 34Kurten R.C. Cadena D.L. Gill G.N. Science. 1996; 272: 1008-1010Crossref PubMed Google Scholar). Protease-activated receptors are irreversibly activated by enzymatic digestion of the N-terminal segment of the receptor, and the sorting of activated receptors to lysosomes rather than recycling is critical for terminating signaling for these receptors. Another protein called G protein-coupled receptor-associated sorting protein (GASP) was recently suggested to be involved in the preferential lysosomal sorting of the δ-opioid receptor (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar). As shown in Table I, the four proteins, EBP50, NSF, SNX1, and GASP, which have been proposed to function as adaptor proteins involved in the post-endocytotic sorting of 7TM receptors, are structurally very different and have been implicated in various other cellular functions. Here, these proteins are probed for their ability to bind to the C-terminal tails of 59 different 7TM receptors as determined by GST pull-down assays, which routinely have been used to confirm protein interactions identified by co-immunoprecipitation and yeast two-hybrid screening (8Hu L.A. Tang Y. Miller W.E. Cong M. Lau A.G. Lefkowitz R.J. Hall R.A. J. Biol. Chem. 2000; 275: 38659-38666Abstract Full Text Full Text PDF PubMed Scopus (131) Google Scholar, 23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar, 35Bachner D. Kreienkamp H.J. Richter D. FEBS Lett. 2002; 526: 124-128Crossref PubMed Scopus (0) Google Scholar, 36Becamel C. Figge A. Poliak S. Dumuis A. Peles E. Bockaert J. Lubbert H. Ullmer C. J. Biol. Chem. 2001; 276: 12974-12982Abstract Full Text Full Text PDF PubMed Scopus (113) Google Scholar, 37Dev K.K. Nakajima Y. Kitano J. Braithwaite S.P. Henley J.M. Nakanishi S. J. Neurosci. 2000; 20: 7252-7257Crossref PubMed Google Scholar). In selected cases, interactions were further studied by surface plasmon resonance (SPR) technology or the interaction was characterized in more detail through gradual deletion mutagenesis of the tail protein.Table ISorting proteins interacting with 7TM receptorsEBP50/NHERFNSFSNX1GASPSize (amino acids)3587445221395General binding domainsaDomain searches were done by SMART (smart.embl-heidelberg.de) (95) and COILS (www.ch.embnet.org/software/COILS_form.html) (96).2 PDZ domains, 1 ERM domainNo known1 PX (phox homology) domain, 3 CC (coiled-coil) domainsNo knownOligomer formationHomo-oligomers and hetero-oligomers with NHERF2 (59Lau A.G. Hall R.A. Biochemistry. 2001; 40: 8572-8580Crossref PubMed Scopus (99) Google Scholar)Homohexamers (60Hanson P.I. Roth R. Morisaki H. Jahn R. Heuser J.E. Cell. 1997; 90: 523-535Abstract Full Text Full Text PDF PubMed Scopus (637) Google Scholar, 61Fleming K.G. Hohl T.M. Yu R.C. Muller S.A. Wolpensinger B. Engel A. Engelhardt H. Brunger A.T. Sollner T.H. Hanson P.I. J. Biol. Chem. 1998; 273: 15675-15681Abstract Full Text Full Text PDF PubMed Scopus (77) Google Scholar)Homotetramers and larger homo-oligomers (62Kurten R.C. Eddington A.D. Chowdhury P. Smith R.D. Davidson A.D. Shank B.B. J. Cell Sci. 2001; 114: 1743-1756Crossref PubMed Google Scholar). Hetero-oligomers with SNX2 (54Zhong Q. Lazar C.S. Tronchere H. Sato T. Meerloo T. Yeo M. Songyang Z. Emr S.D. Gill G.N. Proc. Natl. Acad. Sci. U. S. A. 2002; 99: 6767-6772Crossref PubMed Scopus (126) Google Scholar, 63Haft C.R. de la Luz S.M. Barr V.A. Haft D.H. Taylor S.I. Mol. Cell. Biol. 1998; 18: 7278-7287Crossref PubMed Google Scholar)Not knownProtein-protein interactions/complexesEzrin (64Reczek D. Berryman M. Bretscher A. J. Cell Biol. 1997; 139: 169-179Crossref PubMed Scopus (496) Google Scholar), moesin (64Reczek D. Berryman M. Bretscher A. J. Cell Biol. 1997; 139: 169-179Crossref PubMed Scopus (496) Google Scholar), merlin (65Murthy A. Gonzalez-Agosti C. Cordero E. Pinney D. Candia C. Solomon F. Gusella J. Ramesh V. J. Biol. Chem. 1998; 273: 1273-1276Abstract Full Text Full Text PDF PubMed Scopus (213) Google Scholar), radixin (65Murthy A. Gonzalez-Agosti C. Cordero E. Pinney D. Candia C. Solomon F. Gusella J. Ramesh V. J. Biol. Chem. 1998; 273: 1273-1276Abstract Full Text Full Text PDF PubMed Scopus (213) Google Scholar), NHE3 (39Hall R.A. Premont R.T. Chow C.W. Blitzer J.T. Pitcher J.A. Claing A. Stoffel R.H. Barak L.S. Shenolikar S. Weinman E.J. Grinstein S. Lefkowitz R.J. Nature. 1998; 392: 626-630Crossref PubMed Scopus (500) Google Scholar), GRK6A (66Hall R.A. Spurney R.F. Premont R.T. Rahman N. Blitzer J.T. Pitcher J.A. Lefkowitz R.J. J. Biol. Chem. 1999; 274: 24328-24334Abstract Full Text Full Text PDF PubMed Scopus (125) Google Scholar), YAP65 (67Mohler P.J. Kreda S.M. Boucher R.C. Sudol M. Stutts M.J. Milgram S.L. J. Cell Biol. 1999; 147: 879-890Crossref PubMed Scopus (159) Google Scholar), β-catenin (68Shibata T. Chuma M. Kokubu A. Sakamoto M. Hirohashi S. Hepatology. 2003; 38: 178-186Crossref PubMed Scopus (124) Google Scholar), Gαq (69Rochdi M.D. Watier V. La Madeleine C. Nakata H. Kozasa T. Parent J.L. J. Biol. Chem. 2002; 277: 40751-40759Abstract Full Text Full Text PDF PubMed Scopus (49) Google Scholar), Trp4, Trp5, PLC-β1, PLC-β2 (70Tang Y. Tang J. Chen Z. Trost C. Flockerzi V. Li M. Ramesh V. Zhu M.X. J. Biol. Chem. 2000; 275: 37559-37564Abstract Full Text Full Text PDF PubMed Scopus (217) Google Scholar), PAG (71Brdickova N. Brdicka T. Andera L. Spicka J. Angelisova P. Milgram S.L. Horejsi V. FEBS Lett. 2001; 507: 133-136Crossref PubMed Scopus (101) Google Scholar), MRP2 (72Hegedus T. Sessler T. Scott R. Thelin W. Bakos E. Varadi A. Szabo K. Homolya L. Milgram S.L. Sarkadi B. Biochem. Biophys. Res. Commun. 2003; 302: 454-461Crossref PubMed Scopus (76) Google Scholar), V-ATPase B1 (73Breton S. Wiederhold T. Marshansky V. Nsumu N.N. Ramesh V. Brown D. J. Biol. Chem. 2000; 275: 18219-18224Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar), NBC3 (74Pushkin A. Abuladze N. Newman D. Muronets V. Sassani P. Tatishchev S. Kurtz I. Am. J. Physiol. 2003; 284: C667-C673Crossref PubMed Google Scholar)αSNAP (48May A.P. Whiteheart S.W. Weis W.I. J. Biol. Chem. 2001; 276: 21991-21994Abstract Full Text Full Text PDF PubMed Scopus (82) Google Scholar), β-arrestin1 (75McDonald P.H. Cote N.L. Lin F.T. Premont R.T. Pitcher J.A. Lefkowitz R.J. J. Biol. Chem. 1999; 274: 10677-10680Abstract Full Text Full Text PDF PubMed Scopus (117) Google Scholar), Rab3, Rab4, Rab6 (76Han S.Y. Park D.Y. Park S.D. Hong S.H. Biochem. J. 2000; 352: 165-173Crossref PubMed Scopus (23) Google Scholar), GABARAP (77Kittler J.T. Rostaing P. Schiavo G. Fritschy J.M. Olsen R. Triller A. Moss S.J. Mol. Cell Neurosci. 2001; 18: 13-25Crossref PubMed Scopus (189) Google Scholar, 78Kneussel M. Brain Res. Brain Res. Rev. 2002; 39: 74-83Crossref PubMed Scopus (85) Google Scholar), GATE-16 (79Muller J.M. Shorter J. Newman R. Deinhardt K. Sagiv Y. Elazar Z. Warren G. Shima D.T. J. Cell Biol. 2002; 157: 1161-1173Crossref PubMed Scopus (67) Google Scholar, 80Sagiv Y. Legesse-Miller A. Porat A. Elazar Z. EMBO J. 2000; 19: 1494-1504Crossref PubMed Google Scholar)Hrs (81Chin L.S. Raynor M.C. Wei X. Chen H.Q. Li L. J. Biol. Chem. 2001; 276: 7069-7078Abstract Full Text Full Text PDF PubMed Scopus (162) Google Scholar), hVPS35 (82Haft C.R. de la Luz S.M. Bafford R. Lesniak M.A. Barr V.A. Taylor S.I. Mol. Biol. Cell. 2000; 11: 4105-4116Crossref PubMed Google Scholar), SNX6 (83Parks W.T. Frank D.B. Huff C. Renfrew H.C. Martin J. Meng X. de Caestecker M.P. McNally J.G. Reddi A. Taylor S.I. Roberts A.B. Wang T. Lechleider R.J. J. Biol. Chem. 2001; 276: 19332-19339Abstract Full Text Full Text PDF PubMed Scopus (109) Google Scholar), SNX15 (84Phillips S.A. Barr V.A. Haft D.H. Taylor S.I. Haft C.R. J. Biol. Chem. 2001; 276: 5074-5084Abstract Full Text Full Text PDF PubMed Scopus (68) Google Scholar)Not knownProposed interactions with receptorsβ2AR (21Cao T.T. Deacon H.W. Reczek D. Bretscher A. von Zastrow M. Nature. 1999; 401: 286-290Crossref PubMed Scopus (545) Google Scholar), KOP (47Li J.G. Chen C. Liu-Chen L.Y. J. Biol. Chem. 2002; 277: 27545-27552Abstract Full Text Full Text PDF PubMed Scopus (102) Google Scholar), CFTR (85Moyer B.D. Denton J. Karlson K.H. Reynolds D. Wang S. Mickle J.E. Milewski M. Cutting G.R. Guggino W.B. Li M. Stanton B.A. J. Clin. Investig. 1999; 104: 1353-1361Crossref PubMed Google Scholar), PTH1R (86Mahon M.J. Donowitz M. Yun C.C. Segre G.V. Nature. 2002; 417: 858-861Crossref PubMed Scopus (258) Google Scholar), PDGFR (87Maudsley S. Zamah A.M. Rahman N. Blitzer J.T. Luttrell L.M. Lefkowitz R.J. Hall R.A. Mol. Cell. Biol. 2000; 20: 8352-8363Crossref PubMed Scopus (174) Google Scholar), P2Y1 (88Hall R.A. Ostedgaard L.S. Premont R.T. Blitzer J.T. Rahman N. Welsh M.J. Lefkowitz R.J. Proc. Natl. Acad. Sci. U. S. A. 1998; 95: 8496-8501Crossref PubMed Scopus (360) Google Scholar)β2AR (22Cong M. Perry S.J. Hu L.A. Hanson P.I. Claing A. Lefkowitz R.J. J. Biol. Chem. 2001; 276: 45145-45152Abstract Full Text Full Text PDF PubMed Scopus (116) Google Scholar), AMPA-R (89Song I. Kamboj S. Xia J. Dong H. Liao D. Huganir R.L. Neuron. 1998; 21: 393-400Abstract Full Text Full Text PDF PubMed Google Scholar, 90Osten P. Srivastava S. Inman G.J. Vilim F.S. Khatri L. Lee L.M. States B.A. Einheber S. Milner T.A. Hanson P.I. Ziff E.B. Neuron. 1998; 21: 99-110Abstract Full Text Full Text PDF PubMed Scopus (300) Google Scholar, 91Nishimune A. Isaac J.T. Molnar E. Noel J. Nash S.R. Tagaya M. Collingridge G.L. Nakanishi S. Henley J.M. Neuron. 1998; 21: 87-97Abstract Full Text Full Text PDF PubMed Scopus (446) Google Scholar, 92Luscher C. Xia H. Beattie E.C. Carroll R.C. von Zastrow M. Malenka R.C. Nicoll R.A. Neuron. 1999; 24: 649-658Abstract Full Text Full Text PDF PubMed Google Scholar, 93Noel J. Ralph G.S. Pickard L. Williams J. Molnar E. Uney J.B. Collingridge G.L. Henley J.M. Neuron. 1999; 23: 365-376Abstract Full Text Full Text PDF PubMed Scopus (254) Google Scholar)EGFR (34Kurten R.C. Cadena D.L. Gill G.N. Science. 1996; 272: 1008-1010Crossref PubMed Google Scholar), PAR1 (24Wang Y. Zhou Y. Szabo K. Haft C.R. Trejo J. Mol. Biol. Cell. 2002; 13: 1965-1976Crossref PubMed Scopus (107) Google Scholar), insulin-R (63Haft C.R. de la Luz S.M. Barr V.A. Haft D.H. Taylor S.I. Mol. Cell. Biol. 1998; 18: 7278-7287Crossref PubMed Google Scholar), leptin-R (63Haft C.R. de la Luz S.M. Barr V.A. Haft D.H. Taylor S.I. Mol. Cell. Biol. 1998; 18: 7278-7287Crossref PubMed Google Scholar), PDGFR (63Haft C.R. de la Luz S.M. Barr V.A. Haft D.H. Taylor S.I. Mol. Cell. Biol. 1998; 18: 7278-7287Crossref PubMed Google Scholar), transferrin-R (63Haft C.R. de la Luz S.M. Barr V.A. Haft D.H. Taylor S.I. Mol. Cell. Biol. 1998; 18: 7278-7287Crossref PubMed Google Scholar, 94Schwarz D.G. Griffin C.T. Schneider E.A. Yee D. Magnuson T. Mol. Biol. Cell. 2002; 13: 3588-3600Crossref PubMed Scopus (68) Google Scholar)DOP (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar), β2AR (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar), α2BAR (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar), D4 (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar), MOP (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar)Proposed role in receptor recycling/degradationRecycling shown for β2AR and KOPRecycling shown for β2AR and AMPA-RLysosomal degradation shown for EGFR and PAR1Lysosomal degradation shown for DOPLocation in cellsApical membrane of epithelial cellsBoth cytosolic and membrane-associatedEndosomal membranes and cytosolThroughout the cytoplasma Domain searches were done by SMART (smart.embl-heidelberg.de) (95Letunic I. Goodstadt L. Dickens N.J. Doerks T. Schultz J. Mott R. Ciccarelli F. Copley R.R. Ponting C.P. Bork P. Nucleic Acids Res. 2002; 30: 242-244Crossref PubMed Google Scholar) and COILS (www.ch.embnet.org/software/COILS_form.html) (96Lupas A. Methods Enzymol. 1996; 266: 513-525Crossref PubMed Google Scholar). Open table in a new tab Materials—Rat NSF cDNA was provided by Jim Rothman through Bob Lefkowitz (Duke University). Human EBP50 cDNA was provided by Mark von Zastrow (UCSF). Human SNX1, GASP, and cGASP have been described previously (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar, 24Wang Y. Zhou Y. Szabo K. Haft C.R. Trejo J. Mol. Biol. Cell. 2002; 13: 1965-1976Crossref PubMed Scopus (107) Google Scholar). Human β1- and β2-adrenergic receptors were from Brian Kobilka (Stanford University). Human 5-hydroxytryptamine receptors 5-HT1A, 5-HT1D, and 5-HT1E, human histamine receptors H1, H2, and H3, and human κ-opioid (KOP) receptor were from Guthrie cDNA Resource Center (www.cdna.org). Human muscarinic acetylcholine receptors M1, M2, M3, M4, and M5 were from Tom I. Bonner (National Institutes of Health, Bethesda, MD). Human tachykinin receptor NK1 was from Norma Gerard (The Children's Hospital, Boston, MA). Human NK2 and NK3 receptors were from Jim Krause (Washington University School of Medicine, St. Louis, MO). Human somatostatin receptors SST1, SST2, SST3, SST4, and SST5 and human neuropeptide receptor Y4 were from Carsten Stidsen (Novo Nordisk A/S, Måløv, Denmark). Human vasopressin receptor V2 and human oxytocin (OT) receptor were provided by Claude Barberis (INSERM, Montpellier, France). Mouse melanocortin receptor MC1 was from Roger D. Cone (The Vollum Institute, Portland, OR). Human melanocortin receptor MC4, human melanin-concentrating hormone receptors MCH1 and MCH2, and human ghrelin receptor were from Christian E. Elling (7TM Pharma). Human angiotensin II receptor type 1 (AT1) was from Hans T. Schambye (Maxygen, Hørsholm, Denmark). Human motilin receptor was from Bruce Conklin (UCSF). Mouse δ-opioid (DOP) and mouse μ-opioid (MOP) receptors were described previously (23Whistler J.L. Enquist J. Marley A. Fong J. Gladher F. Tsuruda P. Murray S.R. von Zastrow M. Science. 2002; 297: 615-620Crossref PubMed Scopus (257) Google Scholar). Human PAR1 and PAR2 were from Shaun R. Coughlin (UCSF). Human leukotriene LTB4 receptor was cloned from a human cDNA library. Human chemokine receptors CXCR2 and CXCR4 and human cytomegalovirus chemokine receptors US28 and US27 were from Timothy N. C. Wells (Serono Pharmaceutical Research Institute, Geneva, Switzerland). Human chemoki" @default.
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• W2075074068 date "2004-12-01" @default.
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• W2075074068 title "A Library of 7TM Receptor C-terminal Tails" @default.
• W2075074068 cites W1483932465 @default.
• W2075074068 cites W1498019036 @default.
• W2075074068 cites W1505853894 @default.
• W2075074068 cites W1507084693 @default.
• W2075074068 cites W1523472972 @default.
• W2075074068 cites W1527823690 @default.
• W2075074068 cites W1554313068 @default.
• W2075074068 cites W1601621203 @default.
• W2075074068 cites W1604209299 @default.
• W2075074068 cites W1897589155 @default.
• W2075074068 cites W1933410007 @default.
• W2075074068 cites W1963136808 @default.
• W2075074068 cites W1969913785 @default.
• W2075074068 cites W1971451190 @default.
• W2075074068 cites W1972120303 @default.
• W2075074068 cites W1974363746 @default.
• W2075074068 cites W1974626719 @default.
• W2075074068 cites W1987308757 @default.
• W2075074068 cites W1988594478 @default.
• W2075074068 cites W1991550774 @default.
• W2075074068 cites W1994954589 @default.
• W2075074068 cites W1996836065 @default.
• W2075074068 cites W1999384023 @default.
• W2075074068 cites W1999396012 @default.
• W2075074068 cites W2001367759 @default.
• W2075074068 cites W2001797086 @default.
• W2075074068 cites W2005288670 @default.
• W2075074068 cites W2006783084 @default.
• W2075074068 cites W2008702542 @default.
• W2075074068 cites W2010816636 @default.
• W2075074068 cites W2011643835 @default.
• W2075074068 cites W2011914502 @default.
• W2075074068 cites W2015922146 @default.
• W2075074068 cites W2016162029 @default.
• W2075074068 cites W2018146224 @default.
• W2075074068 cites W2021100900 @default.
• W2075074068 cites W2022125301 @default.
• W2075074068 cites W2022990103 @default.
• W2075074068 cites W2023661096 @default.
• W2075074068 cites W2024028178 @default.
• W2075074068 cites W2024352808 @default.
• W2075074068 cites W2025872971 @default.
• W2075074068 cites W2026669832 @default.
• W2075074068 cites W2026919347 @default.
• W2075074068 cites W2027739935 @default.
• W2075074068 cites W2029504852 @default.
• W2075074068 cites W2033308894 @default.
• W2075074068 cites W2035202152 @default.
• W2075074068 cites W2035966690 @default.
• W2075074068 cites W2036882997 @default.
• W2075074068 cites W2039959072 @default.
• W2075074068 cites W2040367894 @default.
• W2075074068 cites W2040580510 @default.
• W2075074068 cites W2043377395 @default.
• W2075074068 cites W2047324455 @default.
• W2075074068 cites W2051446765 @default.
• W2075074068 cites W2051724639 @default.
• W2075074068 cites W2052467519 @default.
• W2075074068 cites W2052473372 @default.
• W2075074068 cites W2052999464 @default.
• W2075074068 cites W2055267308 @default.
• W2075074068 cites W2064352321 @default.
• W2075074068 cites W2067369435 @default.
• W2075074068 cites W2069156204 @default.
• W2075074068 cites W2069203092 @default.
• W2075074068 cites W2070458501 @default.
• W2075074068 cites W2073270002 @default.
• W2075074068 cites W2077399951 @default.
• W2075074068 cites W2078387010 @default.
• W2075074068 cites W2080697422 @default.
• W2075074068 cites W2081678320 @default.
• W2075074068 cites W2087280546 @default.
• W2075074068 cites W2089875752 @default.
• W2075074068 cites W2090664128 @default.
• W2075074068 cites W2091366475 @default.
• W2075074068 cites W2095250075 @default.
• W2075074068 cites W2105006060 @default.
• W2075074068 cites W2105341630 @default.
• W2075074068 cites W2106621092 @default.
• W2075074068 cites W2107502575 @default.
• W2075074068 cites W2107920932 @default.
• W2075074068 cites W2123258949 @default.
• W2075074068 cites W2125954573 @default.
• W2075074068 cites W2129285015 @default.
• W2075074068 cites W2129763785 @default.

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