EXOC3

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Exocyst complex component 3
Identifiers
Symbols EXOC3 ; SEC6; SEC6L1; Sec6p
External IDs Template:OMIM5 Template:MGI HomoloGene38296
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Exocyst complex component 3, also known as EXOC3, is a human gene.[1]

The protein encoded by this gene is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. The complex is also essential for the biogenesis of epithelial cell surface polarity.[1]

References

  1. 1.0 1.1 "Entrez Gene: EXOC3 exocyst complex component 3".

Further reading

  • Hsu SC, TerBush D, Abraham M, Guo W (2004). "The exocyst complex in polarized exocytosis". Int. Rev. Cytol. 233: 243–65. doi:10.1016/S0074-7696(04)33006-8. PMID 15037366.
  • Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Hsu SC, Ting AE, Hazuka CD; et al. (1997). "The mammalian brain rsec6/8 complex". Neuron. 17 (6): 1209–19. PMID 8982167.
  • Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.
  • Kee Y, Yoo JS, Hazuka CD; et al. (1998). "Subunit structure of the mammalian exocyst complex". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14438–43. PMID 9405631.
  • Hsu SC, Hazuka CD, Roth R; et al. (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments". Neuron. 20 (6): 1111–22. PMID 9655500.
  • Brymora A, Valova VA, Larsen MR; et al. (2001). "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): 29792–7. doi:10.1074/jbc.C100320200. PMID 11406615.
  • Polzin A, Shipitsin M, Goi T; et al. (2002). "Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles". Mol. Cell. Biol. 22 (6): 1714–22. PMID 11865051.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "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): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Inoue M, Chang L, Hwang J; et al. (2003). "The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin". Nature. 422 (6932): 629–33. doi:10.1038/nature01533. PMID 12687004.
  • Jikuya H, Takano J, Kikuno R; et al. (2003). "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones". DNA Res. 10 (1): 49–57. PMID 12693554.
  • Wang S, Hsu SC (2004). "Immunological characterization of exocyst complex subunits in cell differentiation". Hybrid. Hybridomics. 22 (3): 159–64. doi:10.1089/153685903322286575. PMID 12954101.
  • Moskalenko S, Tong C, Rosse C; et al. (2004). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID 14525976.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.

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