Biology:EXOC7
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
| Exo70 exocyst complex subunit | |||||||||
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 crystal structure of the s. cerevisiae exocyst component exo70p | |||||||||
| Identifiers | |||||||||
| Symbol | Exo70 | ||||||||
| Pfam | PF03081 | ||||||||
| Pfam clan | CL0295 | ||||||||
| InterPro | IPR004140 | ||||||||
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Exocyst complex component 7 is a protein that in humans is encoded by the EXOC7 gene.[1][2] It was formerly known as Exo70.
It forms one subunit of the exocyst complex. First discovered in Saccharomyces cerevisiae, this and other exocyst proteins have been observed in several other eukaryotes, including humans.[3] In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localised at the tip of the bud, the major site of exocytosis in yeast.[3] It interacts with the Rho3 GTPase.[4] This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud).[5] In humans, the functions of this protein and the exocyst complex are less well characterised: this protein is expressed in several tissues and is thought to also be involved in exocytosis.[6]
Interactions
EXOC7 has been shown to interact with EXOC4[7][8] and RHOQ.[8]
References
- ↑ "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc Natl Acad Sci U S A 99 (26): 16899–16903. Dec 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- ↑ "Entrez Gene: EXOC7 exocyst complex component 7". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23265.
- ↑ 3.0 3.1 "The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae". EMBO J. 15 (23): 6483–94. December 1996. doi:10.1002/j.1460-2075.1996.tb01039.x. PMID 8978675.
- ↑ "Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70". Mol. Cell. Biol. 19 (5): 3580–7. May 1999. doi:10.1128/MCB.19.5.3580. PMID 10207081.
- ↑ "The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity". Mol. Biol. Cell 10 (12): 4121–33. December 1999. doi:10.1091/mbc.10.12.4121. PMID 10588647.
- ↑ "Subunit structure of the mammalian exocyst complex". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14438–43. December 1997. doi:10.1073/pnas.94.26.14438. PMID 9405631. Bibcode: 1997PNAS...9414438K.
- ↑ "NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex". Nat. Cell Biol. 5 (6): 520–530. Jun 2003. doi:10.1038/ncb990. PMID 12738960.
- ↑ 8.0 8.1 "The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin". Nature 422 (6932): 629–633. Apr 2003. doi:10.1038/nature01533. PMID 12687004. Bibcode: 2003Natur.422..629I. https://deepblue.lib.umich.edu/bitstream/2027.42/62982/1/nature01533.pdf.
Further reading
- "Subunit structure of the mammalian exocyst complex". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14438–14443. 1998. doi:10.1073/pnas.94.26.14438. PMID 9405631. Bibcode: 1997PNAS...9414438K.
- "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. 1999. doi:10.1093/dnares/6.3.197. PMID 10470851.
- "Transient T cell receptor beta-chain variable region-specific expansions of CD4+ and CD8+ T cells during the early phase of pediatric human immunodeficiency virus infection: characterization of expanded cell populations by T cell receptor phenotyping". J. Infect. Dis. 181 (1): 107–120. 2000. doi:10.1086/315181. PMID 10608757.
- "Dominance of intrinsic genetic factors in shaping the human immunoglobulin Vlambda repertoire". J. Mol. Biol. 294 (2): 457–465. 2000. doi:10.1006/jmbi.1999.3243. PMID 10610771.
- "IgA and IgM V(H) repertoires in human colon: evidence for clonally expanded B cells that are widely disseminated". Gastroenterology 119 (5): 1253–1266. 2000. doi:10.1053/gast.2000.20219. PMID 11054383.
- "The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene". J. Biol. Chem. 276 (32): 29792–29797. 2001. doi:10.1074/jbc.C100320200. PMID 11406615.
- "The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin". Nature 422 (6932): 629–633. 2003. doi:10.1038/nature01533. PMID 12687004. Bibcode: 2003Natur.422..629I. https://deepblue.lib.umich.edu/bitstream/2027.42/62982/1/nature01533.pdf.
- "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–51748. 2004. doi:10.1074/jbc.M308702200. PMID 14525976.
- "The mammalian exocyst, a complex required for exocytosis, inhibits tubulin polymerization". J. Biol. Chem. 279 (34): 35958–35966. 2005. doi:10.1074/jbc.M313778200. PMID 15205466.
- "Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70". Proc. Natl. Acad. Sci. U.S.A. 102 (8): 2784–2789. 2005. doi:10.1073/pnas.0409871102. PMID 15705715. Bibcode: 2005PNAS..102.2784X.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–1178. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–1292. 2006. doi:10.1038/nbt1240. PMID 16964243.
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