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• W2010304848 abstract "Golgins have been implicated in the maintenance of Golgi architecture. Recent studies have shown, however, that mice lacking the golgin TRIP11/GMAP-210 have normal Golgi stacks, but show developmental problems related to defective cilium formation and function. Golgins have been implicated in the maintenance of Golgi architecture. Recent studies have shown, however, that mice lacking the golgin TRIP11/GMAP-210 have normal Golgi stacks, but show developmental problems related to defective cilium formation and function. Golgins are a group of coiled-coil proteins that localise to the Golgi and Golgi-associated vesicles and have membrane–membrane or membrane–cytoskeleton tethering activity [1Munro S. Organelle identity and the organization of membrane traffic.Nat. Cell Biol. 2004; 6: 469-472Crossref PubMed Scopus (69) Google Scholar, 2Short B. Haas A. Barr F.A. Golgins and GTPases, giving identity and structure to the Golgi apparatus.Biochim. Biophys. Acta. 2005; 1744: 383-395Crossref PubMed Scopus (190) Google Scholar, 3Shorter J. Beard M.B. Seemann J. Dirac-Svejstrup A.B. Warren G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.J. Cell Biol. 2002; 157: 45-62Crossref PubMed Scopus (161) Google Scholar]. These proteins target specific Golgi membrane subdomains by binding to a variety of GTPases of the ARF, Arl, and Rab families that have discrete localisations within the Golgi apparatus. For some golgins, the targeting to Golgi subdomains may be fine-tuned by ancillary domains with specific membrane-curvature-sensing properties, allowing discrimination between highly curved vesicles and flattened cisternae [4Drin G. Morello V. Casella J.F. Gounon P. Antonny B. Asymmetric tethering of flat and curved lipid membranes by a golgin.Science. 2008; 320: 670-673Crossref PubMed Scopus (143) Google Scholar]. Together these properties are thought to explain the long-distance recognition of targets by vesicles and the maintenance of the characteristic stacked cisternal organisation of the Golgi [1Munro S. Organelle identity and the organization of membrane traffic.Nat. Cell Biol. 2004; 6: 469-472Crossref PubMed Scopus (69) Google Scholar, 2Short B. Haas A. Barr F.A. Golgins and GTPases, giving identity and structure to the Golgi apparatus.Biochim. Biophys. Acta. 2005; 1744: 383-395Crossref PubMed Scopus (190) Google Scholar, 3Shorter J. Beard M.B. Seemann J. Dirac-Svejstrup A.B. Warren G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.J. Cell Biol. 2002; 157: 45-62Crossref PubMed Scopus (161) Google Scholar, 4Drin G. Morello V. Casella J.F. Gounon P. Antonny B. Asymmetric tethering of flat and curved lipid membranes by a golgin.Science. 2008; 320: 670-673Crossref PubMed Scopus (143) Google Scholar]. The golgin TRIP11/GMAP-210 is thought to act as a tether at the cis-Golgi as a result of dual recognition of the small GTPase ARF1 by a carboxy-terminal GRAB domain and of curved membranes by an amino-terminal lipid packing sensor (ALPS) motif [4Drin G. Morello V. Casella J.F. Gounon P. Antonny B. Asymmetric tethering of flat and curved lipid membranes by a golgin.Science. 2008; 320: 670-673Crossref PubMed Scopus (143) Google Scholar, 5Gillingham A.K. Tong A.H. Boone C. Munro S. The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.J. Cell Biol. 2004; 167: 281-292Crossref PubMed Scopus (82) Google Scholar]. Like other golgins GMAP-210 has been proposed to have an important role in maintaining a morphologically normal and functional Golgi apparatus [6Rios R.M. Sanchis A. Tassin A.M. Fedriani C. Bornens M. GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation.Cell. 2004; 118: 323-335Abstract Full Text Full Text PDF PubMed Scopus (180) Google Scholar]. Insight into golgin function now comes from a somewhat unexpected direction, namely via studies on the intraflagellar transport (IFT) complex required for bidirectional cargo transport along cilia and flagella [7Follit J.A. San Agustin J.T. Xu F. Jonassen J.A. Samtani R. Lo C.W. Pazour G.J. The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.PLoS Genet. 2008; 4: e1000315Crossref PubMed Scopus (123) Google Scholar, 8Follit J.A. Tuft R.A. Fogarty K.E. Pazour G.J. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly.Mol. Biol. Cell. 2006; 17: 3781-3792Crossref PubMed Scopus (353) Google Scholar]. The IFT complex is a conserved particle comprising at least 17 polypeptides that, together with dynein- and kinesin-family motors, mediates bidirectional transport along the axoneme of cilia and flagella [9Scholey J.M. Intraflagellar transport.Annu. Rev. Cell Dev. Biol. 2003; 19: 423-443Crossref PubMed Scopus (325) Google Scholar]. Follit et al. [8Follit J.A. Tuft R.A. Fogarty K.E. Pazour G.J. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly.Mol. Biol. Cell. 2006; 17: 3781-3792Crossref PubMed Scopus (353) Google Scholar] previously demonstrated that the IFT20 subunit is also present on the Golgi apparatus and can transit from there to the cilium and along ciliary microtubules. At the time they reasonably hypothesized that this might indicate a role for IFT20 in vesicle-mediated transport from the Golgi to cilia and that a Golgi receptor for IFT20 might exist. This group now reports compelling evidence in support of both of these ideas. In their new study, Follit et al. [7Follit J.A. San Agustin J.T. Xu F. Jonassen J.A. Samtani R. Lo C.W. Pazour G.J. The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.PLoS Genet. 2008; 4: e1000315Crossref PubMed Scopus (123) Google Scholar] first describe the identification of the golgin GMAP-210 as a direct binding partner of IFT20 that is responsible for its Golgi targeting. They then generated mice lacking GMAP-210 and found that these mice have defective transport of the transmembrane cargo protein polycystin-2 to cilia. Surprisingly, the embryonic kidney cells from these mice do not show any alterations in Golgi architecture. These mice are also unlikely to have any general defects in secretory pathway function, since the development of most major organs is essentially normal. Despite this, these mice die at birth and display defects in the development of the heart, lung and abdominal wall. By identifying GMAP-210 as a Golgi membrane receptor for IFT20, Follit et al. [7Follit J.A. San Agustin J.T. Xu F. Jonassen J.A. Samtani R. Lo C.W. Pazour G.J. The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.PLoS Genet. 2008; 4: e1000315Crossref PubMed Scopus (123) Google Scholar] have a good indicator that this golgin is important for some aspect of cilium biology. They find that, although GMAP-210 does not appear to be essential for the formation of all cilia, cultured mouse embryonic kidney cells from the GMAP-210-deficient mice have slightly shortened cilia to which the ciliary membrane protein polcystin-2 does not efficiently target. Importantly, they show that both of these defects can be rescued by expressing GMAP-210 in the cultured cells. These phenotypes are similar to those seen following partial knockdown of IFT20 in cell culture, which results in defective targeting of polycystin to cilia but otherwise apparently normal cilia [8Follit J.A. Tuft R.A. Fogarty K.E. Pazour G.J. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly.Mol. Biol. Cell. 2006; 17: 3781-3792Crossref PubMed Scopus (353) Google Scholar]. Complete knockdown of IFT20 in cell culture or targeted deletion in the collecting duct cells of the mouse kidney leads to much more severe defects in cilium formation as well as other defects leading to cystic kidney disease [10Jonassen J.A. San Agustin J. Follit J.A. Pazour G.J. Deletion of IFT20 in the mouse kidney causes misorientation of the mitotic spindle and cystic kidney disease.J. Cell Biol. 2008; 183: 377-384Crossref PubMed Scopus (178) Google Scholar]. The most parsimonious explanation for these observations is that, although GMAP-210 is required to target IFT20 to the Golgi, this Golgi-targeting mechanism is required for some but not all IFT20 functions; whether GMAP-210 has additional functions unrelated to IFT20 is unclear. The recent findings discussed above provide clear evidence that IFT20 is not just moonlighting on Golgi. Because of the interaction with GMAP-210 and effects on polycystin transport, the link to protein transport seems obvious, but it is worth briefly discussing the other reported functions of golgins. In order to address golgin function, it is clear that we need to better understand how their properties mediate their actions. Golgins have been described as microtubule-binding proteins, tethers, membrane-curvature sensors, and even transcription factors, yet none of these functions alone reveals a critical involvement in any particular pathway or tissue. If golgins are indeed tethers, then what properties would we expect such proteins to have? There is an obvious requirement for domains that allow the recognition of two membrane surfaces simultaneously, combined with an extended yet flexible architecture, so that they can recognize vesicles at a distance and then draw them towards their target organelle [1Munro S. Organelle identity and the organization of membrane traffic.Nat. Cell Biol. 2004; 6: 469-472Crossref PubMed Scopus (69) Google Scholar, 2Short B. Haas A. Barr F.A. Golgins and GTPases, giving identity and structure to the Golgi apparatus.Biochim. Biophys. Acta. 2005; 1744: 383-395Crossref PubMed Scopus (190) Google Scholar, 3Shorter J. Beard M.B. Seemann J. Dirac-Svejstrup A.B. Warren G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.J. Cell Biol. 2002; 157: 45-62Crossref PubMed Scopus (161) Google Scholar]. This structural organisation seems to hold true for all golgins studied so far [3Shorter J. Beard M.B. Seemann J. Dirac-Svejstrup A.B. Warren G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.J. Cell Biol. 2002; 157: 45-62Crossref PubMed Scopus (161) Google Scholar, 4Drin G. Morello V. Casella J.F. Gounon P. Antonny B. Asymmetric tethering of flat and curved lipid membranes by a golgin.Science. 2008; 320: 670-673Crossref PubMed Scopus (143) Google Scholar, 5Gillingham A.K. Tong A.H. Boone C. Munro S. The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.J. Cell Biol. 2004; 167: 281-292Crossref PubMed Scopus (82) Google Scholar, 11Sinka R. Gillingham A.K. Kondylis V. Munro S. Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins.J. Cell Biol. 2008; 183: 607-615Crossref PubMed Scopus (136) Google Scholar], yet direct in vivo functional evidence in support of the requirements for such domains is scarce. So what else have golgins been reported to do? Some literature indicates that they may be transcription factors. GMAP-210 was originally described as the transcription factor TRIP11 [12Chen Y. Chen P.L. Chen C.F. Sharp Z.D. Lee W.H. Thyroid hormone, T3-dependent phosphorylation and translocation of Trip230 from the Golgi complex to the nucleus.Proc. Natl. Acad. Sci. USA. 1999; 96: 4443-4448Crossref PubMed Scopus (59) Google Scholar], the golgin CASP is an alternatively spliced form of the CCAAT-displacement protein transcription factor [13Gillingham A.K. Pfeifer A.C. Munro S. CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin.Mol. Biol. Cell. 2002; 13: 3761-3774Crossref PubMed Scopus (87) Google Scholar], and golgin-45 was first described as the transcription factor JEM-1 [14Tong J.H. Duprez E. Lanotte M. JEM-1, a novel nuclear co-factor: localisation and functional interaction with AP-1.Leukemia. 1999; 13: 1982-1992Crossref PubMed Scopus (13) Google Scholar]. Apart from CASP, the evidence that golgins or their alternative splice forms are bona fide transcription factors is weak and mainly based on effects in in vitro transcriptional reporter assays. Other evidence suggests some golgins can be scaffolds for signalling pathways. The best example is GM130, which forms a kinase scaffold that is important for intracellular signalling at the Golgi, as well as being a receptor for the p115 tethering factor essential for ER-to-Golgi transport [3Shorter J. Beard M.B. Seemann J. Dirac-Svejstrup A.B. Warren G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.J. Cell Biol. 2002; 157: 45-62Crossref PubMed Scopus (161) Google Scholar, 15Preisinger C. Short B. De Corte V. Bruyneel E. Haas A. Kopajtich R. Gettemans J. Barr F.A. YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta.J. Cell Biol. 2004; 164: 1009-1020Crossref PubMed Scopus (200) Google Scholar]. Although it is possible that GMAP-210 may have signalling and transcription functions, the evidence in support of such roles is weak or lacking. The simplest explanation for the role of GMAP-210 in ciliary function is therefore that it plays a specific role in cargo sorting and/or tethering. Although a curvature-sensing module, as in the case of the GMAP-210 ALPS motif, is immediately suggestive of tethering, it is also consistent with other functions, such as cargo sorting (Figure 1), as exemplified by the sorting nexin family of proteins [16Carlton J. Bujny M. Rutherford A. Cullen P. Sorting nexins–unifying trends and new perspectives.Traffic. 2005; 6: 75-82Crossref PubMed Scopus (151) Google Scholar]. GMAP-210 might therefore target to vesicle buds or vesicles by dual recognition of both curved membranes and ARF1. Support for the link to cargo sorting rather than tethering comes from observations that the Golgi-targeting GRAB domain of the GMAP-210 family of proteins requires transmembrane proteins of the ERV14 family, which have been implicated in cargo selection during ER–Golgi trafficking [5Gillingham A.K. Tong A.H. Boone C. Munro S. The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.J. Cell Biol. 2004; 167: 281-292Crossref PubMed Scopus (82) Google Scholar]. A direct link between the ERV14 family and cargo destined for cilia has yet to be made but is an obvious avenue for future research. This raises the question of why such a specific pathway would be needed and how it is organised. Does this represent a pathway going directly from the Golgi to a subdomain of the plasma membrane where cargo destined for cilia is delivered? Polarised sorting events of this type are typically associated with the trans-Golgi network, yet GMAP-210 is localised at the cis-Golgi [5Gillingham A.K. Tong A.H. Boone C. Munro S. The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.J. Cell Biol. 2004; 167: 281-292Crossref PubMed Scopus (82) Google Scholar]. Another possibility is that GMAP-210–IFT20 complexes mark the presence of specific cilium-directed cargo early in the pathway and are later recognized at the plasma membrane as a cilium-sorting signal. Again more research is needed. These findings join mounting evidence suggesting that GMAP-210 and other golgins are not essential for normal Golgi architecture and function in all cells [17Yao R. Ito C. Natsume Y. Sugitani Y. Yamanaka H. Kuretake S. Yanagida K. Sato A. Toshimori K. Noda T. Lack of acrosome formation in mice lacking a Golgi protein, GOPC.Proc. Natl. Acad. Sci. USA. 2002; 99: 11211-11216Crossref PubMed Scopus (201) Google Scholar, 18Friggi-Grelin F. Rabouille C. Therond P. The cis-Golgi Drosophila GMAP has a role in anterograde transport and Golgi organization in vivo, similar to its mammalian ortholog in tissue culture cells.Eur. J. Cell Biol. 2006; 85: 1155-1166Crossref PubMed Scopus (26) Google Scholar, 19Hennies H.C. Kornak U. Zhang H. Egerer J. Zhang X. Seifert W. Kuhnisch J. Budde B. Natebus M. Brancati F. et al.Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6 interacting golgin.Nat. Genet. 2008; 40: 1410-1412Crossref PubMed Scopus (112) Google Scholar]. Human patients with the autosomal recessive disorder geroderma osteodysplastica, caused by loss-of-function mutations in the Rab6-binding golgin SCYL1BP1, have osteoporosis and lax, wrinkled skin [19Hennies H.C. Kornak U. Zhang H. Egerer J. Zhang X. Seifert W. Kuhnisch J. Budde B. Natebus M. Brancati F. et al.Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6 interacting golgin.Nat. Genet. 2008; 40: 1410-1412Crossref PubMed Scopus (112) Google Scholar]. Other tissues appear unaltered, and the Golgi appears to be functionally and morphologically normal. Similarly, mice lacking the coiled-coil- and PDZ-domain-containing golgin PIST/GOPc show tissue-restricted defects — in this case, abnormal acrosome formation in sperm production [17Yao R. Ito C. Natsume Y. Sugitani Y. Yamanaka H. Kuretake S. Yanagida K. Sato A. Toshimori K. Noda T. Lack of acrosome formation in mice lacking a Golgi protein, GOPC.Proc. Natl. Acad. Sci. USA. 2002; 99: 11211-11216Crossref PubMed Scopus (201) Google Scholar]. In contrast to these tissue-specific defects, SCYL1BP1 and PIST, like GMAP-210 and most other golgins and the GTPases with which they interact, are expressed in most, if not all, cells and cell lines. Why then do they show such discrete phenotypes? The emerging view, on the basis of the recent work on IFT20 and GMAP-210, suggests that different golgins are required for the transport of distinct groups of cargo molecules in specific tissues. Their ubiquitous expression may therefore be something of a red herring. Finally, were cell biologists premature in labelling golgins as ‘structural tethers’? Perhaps yes, and recent evidence indicates that the golgin nomenclature is little more useful that putting ‘p’ followed by the molecular weight when it comes to grouping the pathways in which these proteins act. Luckily, studies on the cilium suggest a productive direction for future studies of golgins in tissue-specific cargo transport functions. So, what should we do to test golgin function? Cell biological and biochemical assays can define activities such as tethering and sorting, but are often not effective in pinpointing the tissue or pathway in which this activity is critical. A combination of an animal model and high-quality cell biology and biochemistry are clearly needed if we are to untangle golgin function. As the recent work of Follit and colleagues [7Follit J.A. San Agustin J.T. Xu F. Jonassen J.A. Samtani R. Lo C.W. Pazour G.J. The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.PLoS Genet. 2008; 4: e1000315Crossref PubMed Scopus (123) Google Scholar, 8Follit J.A. Tuft R.A. Fogarty K.E. Pazour G.J. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly.Mol. Biol. Cell. 2006; 17: 3781-3792Crossref PubMed Scopus (353) Google Scholar, 10Jonassen J.A. San Agustin J. Follit J.A. Pazour G.J. Deletion of IFT20 in the mouse kidney causes misorientation of the mitotic spindle and cystic kidney disease.J. Cell Biol. 2008; 183: 377-384Crossref PubMed Scopus (178) Google Scholar] on GMAP-210 shows, sometimes the pointers come from unlikely sources, such as the cilium." @default.
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• W2010304848 title "Membrane Traffic: Golgi Stumbles over Cilia" @default.
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