EXOC5: Difference between revisions

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* {{cite journal | vauthors = Brymora A, Valova VA, Larsen MR, Roufogalis BD, Robinson PJ | title = The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene. | journal = J. Biol. Chem. | volume = 276 | issue = 32 | pages = 29792–7 | year = 2001 | pmid = 11406615 | doi = 10.1074/jbc.C100320200 }}
* {{cite journal | vauthors = Brymora A, Valova VA, Larsen MR, Roufogalis BD, Robinson PJ | title = The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene. | journal = J. Biol. Chem. | volume = 276 | issue = 32 | pages = 29792–7 | year = 2001 | pmid = 11406615 | doi = 10.1074/jbc.C100320200 }}
* {{cite journal | vauthors = Polzin A, Shipitsin M, Goi T, Feig LA, Turner TJ | title = Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles. | journal = Mol. Cell. Biol. | volume = 22 | issue = 6 | pages = 1714–22 | year = 2002 | pmid = 11865051 | pmc = 135608 | doi = 10.1128/MCB.22.6.1714-1722.2002 }}
* {{cite journal | vauthors = Polzin A, Shipitsin M, Goi T, Feig LA, Turner TJ | title = Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles. | journal = Mol. Cell. Biol. | volume = 22 | issue = 6 | pages = 1714–22 | year = 2002 | pmid = 11865051 | pmc = 135608 | doi = 10.1128/MCB.22.6.1714-1722.2002 }}
* {{cite journal | vauthors = Inoue M, Chang L, Hwang J, Chiang SH, Saltiel AR | title = The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin. | journal = Nature | volume = 422 | issue = 6932 | pages = 629–33 | year = 2003 | pmid = 12687004 | doi = 10.1038/nature01533 }}
* {{cite journal | vauthors = Inoue M, Chang L, Hwang J, Chiang SH, Saltiel AR | title = The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin. | journal = Nature | volume = 422 | issue = 6932 | pages = 629–33 | year = 2003 | pmid = 12687004 | doi = 10.1038/nature01533 | url = https://deepblue.lib.umich.edu/bitstream/2027.42/62982/1/nature01533.pdf }}
* {{cite journal | vauthors = Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA | title = Ral GTPases regulate exocyst assembly through dual subunit interactions. | journal = J. Biol. Chem. | volume = 278 | issue = 51 | pages = 51743–8 | year = 2004 | pmid = 14525976 | doi = 10.1074/jbc.M308702200 }}
* {{cite journal | vauthors = Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA | title = Ral GTPases regulate exocyst assembly through dual subunit interactions. | journal = J. Biol. Chem. | volume = 278 | issue = 51 | pages = 51743–8 | year = 2004 | pmid = 14525976 | doi = 10.1074/jbc.M308702200 }}
* {{cite journal | vauthors = Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P | title = ARF6 controls post-endocytic recycling through its downstream exocyst complex effector. | journal = J. Cell Biol. | volume = 163 | issue = 5 | pages = 1111–21 | year = 2004 | pmid = 14662749 | pmc = 2173613 | doi = 10.1083/jcb.200305029 }}
* {{cite journal | vauthors = Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P | title = ARF6 controls post-endocytic recycling through its downstream exocyst complex effector. | journal = J. Cell Biol. | volume = 163 | issue = 5 | pages = 1111–21 | year = 2004 | pmid = 14662749 | pmc = 2173613 | doi = 10.1083/jcb.200305029 }}

Revision as of 12:25, 4 November 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Exocyst complex component 5 is a protein that in humans is encoded by the EXOC5 gene.[1][2]

Function

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.[2]

Interactions

EXOC5 has been shown to interact with Arf6.[3]

References

  1. Guo W, Roth D, Gatti E, De Camilli P, Novick P (Apr 1997). "Identification and characterization of homologues of the Exocyst component Sec10p". FEBS Lett. 404 (2–3): 135–9. doi:10.1016/S0014-5793(97)00109-9. PMID 9119050.
  2. 2.0 2.1 "Entrez Gene: EXOC5 exocyst complex component 5".
  3. Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P (Dec 2003). "ARF6 controls post-endocytic recycling through its downstream exocyst complex effector". J. Cell Biol. 163 (5): 1111–21. doi:10.1083/jcb.200305029. PMC 2173613. PMID 14662749.

Further reading