Matches in SemOpenAlex for { <https://semopenalex.org/work/W2052473372> ?p ?o ?g. }
Showing items 1 to 74 of
74
with 100 items per page.
- W2052473372 endingPage "8580" @default.
- W2052473372 startingPage "8572" @default.
- W2052473372 abstract "PDZ domains bind to the carboxyl-termini of target proteins, and some PDZ domains are capable of oligomerization to facilitate the formation of intracellular signaling complexes. The Na(+)/H(+) exchanger regulatory factor (NHERF-1; also called EBP50) and its relative NHERF-2 (also called E3KARP, SIP-1, and TKA-1) both have two PDZ domains. We report here that the PDZ domains of NHERF-1 and NHERF-2 bind specifically to each other but not to other PDZ domains. Purified NHERF-2 PDZ domains associate with each other robustly in the absence of any associated proteins, but purified NHERF-1 PDZ domains associate with each other only weakly when examined alone. The oligomerization of the NHERF-1 PDZ domains is greatly facilitated when they are bound with carboxyl-terminal ligands, such as the carboxyl-termini of the beta(2)-adrenergic receptor or the platelet-derived growth factor receptor. Oligomerization of full-length NHERF-1 is also enhanced by mutation of serine 289 to aspartate (S289D), which mimics the phosphorylated form of NHERF-1. Co-immunoprecipitation experiments with differentially tagged versions of the NHERF proteins reveal that NHERF-1 and NHERF-2 form homo- and hetero-oligomers in a cellular context. A point-mutated version of NHERF-1 (S289A), which cannot be phosphorylated on serine 289, exhibits a reduced capacity for co-immunoprecipitation from cells. These studies reveal that both NHERF-1 and NHERF-2 can oligomerize, which may facilitate NHERF-mediated formation of cellular signaling complexes. These studies furthermore reveal that oligomerization of NHERF-1, but not NHERF-2, is highly regulated by association with other proteins and by phosphorylation." @default.
- W2052473372 created "2016-06-24" @default.
- W2052473372 creator A5045324134 @default.
- W2052473372 creator A5081172086 @default.
- W2052473372 date "2001-06-26" @default.
- W2052473372 modified "2023-09-26" @default.
- W2052473372 title "Oligomerization of NHERF-1 and NHERF-2 PDZ Domains: Differential Regulation by Association with Receptor Carboxyl-Termini and by Phosphorylation" @default.
- W2052473372 cites W2048932608 @default.
- W2052473372 doi "https://doi.org/10.1021/bi0103516" @default.
- W2052473372 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11456497" @default.
- W2052473372 hasPublicationYear "2001" @default.
- W2052473372 type Work @default.
- W2052473372 sameAs 2052473372 @default.
- W2052473372 citedByCount "105" @default.
- W2052473372 countsByYear W20524733722012 @default.
- W2052473372 countsByYear W20524733722013 @default.
- W2052473372 countsByYear W20524733722014 @default.
- W2052473372 countsByYear W20524733722015 @default.
- W2052473372 countsByYear W20524733722016 @default.
- W2052473372 countsByYear W20524733722017 @default.
- W2052473372 countsByYear W20524733722018 @default.
- W2052473372 countsByYear W20524733722019 @default.
- W2052473372 countsByYear W20524733722021 @default.
- W2052473372 crossrefType "journal-article" @default.
- W2052473372 hasAuthorship W2052473372A5045324134 @default.
- W2052473372 hasAuthorship W2052473372A5081172086 @default.
- W2052473372 hasConcept C104317684 @default.
- W2052473372 hasConcept C11960822 @default.
- W2052473372 hasConcept C151730666 @default.
- W2052473372 hasConcept C154428179 @default.
- W2052473372 hasConcept C170493617 @default.
- W2052473372 hasConcept C185592680 @default.
- W2052473372 hasConcept C2776414213 @default.
- W2052473372 hasConcept C2779343474 @default.
- W2052473372 hasConcept C51639874 @default.
- W2052473372 hasConcept C55493867 @default.
- W2052473372 hasConcept C71829478 @default.
- W2052473372 hasConcept C86803240 @default.
- W2052473372 hasConcept C95444343 @default.
- W2052473372 hasConceptScore W2052473372C104317684 @default.
- W2052473372 hasConceptScore W2052473372C11960822 @default.
- W2052473372 hasConceptScore W2052473372C151730666 @default.
- W2052473372 hasConceptScore W2052473372C154428179 @default.
- W2052473372 hasConceptScore W2052473372C170493617 @default.
- W2052473372 hasConceptScore W2052473372C185592680 @default.
- W2052473372 hasConceptScore W2052473372C2776414213 @default.
- W2052473372 hasConceptScore W2052473372C2779343474 @default.
- W2052473372 hasConceptScore W2052473372C51639874 @default.
- W2052473372 hasConceptScore W2052473372C55493867 @default.
- W2052473372 hasConceptScore W2052473372C71829478 @default.
- W2052473372 hasConceptScore W2052473372C86803240 @default.
- W2052473372 hasConceptScore W2052473372C95444343 @default.
- W2052473372 hasIssue "29" @default.
- W2052473372 hasLocation W20524733721 @default.
- W2052473372 hasLocation W20524733722 @default.
- W2052473372 hasOpenAccess W2052473372 @default.
- W2052473372 hasPrimaryLocation W20524733721 @default.
- W2052473372 hasRelatedWork W1961279801 @default.
- W2052473372 hasRelatedWork W1978122481 @default.
- W2052473372 hasRelatedWork W2030936981 @default.
- W2052473372 hasRelatedWork W2035437790 @default.
- W2052473372 hasRelatedWork W2044655831 @default.
- W2052473372 hasRelatedWork W2074618332 @default.
- W2052473372 hasRelatedWork W2125033869 @default.
- W2052473372 hasRelatedWork W2537140536 @default.
- W2052473372 hasRelatedWork W3096764497 @default.
- W2052473372 hasRelatedWork W2136545008 @default.
- W2052473372 hasVolume "40" @default.
- W2052473372 isParatext "false" @default.
- W2052473372 isRetracted "false" @default.
- W2052473372 magId "2052473372" @default.
- W2052473372 workType "article" @default.