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| | '''Exocyst complex component 1''' is a [[protein]] that in humans is encoded by the ''EXOC1'' [[gene]].<ref name="pmid11042152">{{cite journal | vauthors = Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z | title = Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells | journal = Genome Res | volume = 10 | issue = 10 | pages = 1546–60 |date=Nov 2000 | pmid = 11042152 | pmc = 310934 | doi =10.1101/gr.140200 }}</ref><ref name="pmid11406615">{{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 |date=Aug 2001 | pmid = 11406615 | pmc = | doi = 10.1074/jbc.C100320200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EXOC1 exocyst complex component 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55763| accessdate = }}</ref> | ||
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| summary_text = 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 the 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. Alternatively spliced transcript variants encoding distinct isoforms have been described.<ref name="entrez" | | summary_text = 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 [[Cell membrane|plasma membrane]]. Though best characterized in yeast, the component proteins and functions of the [[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 remodeling|actin cytoskeletal remodeling]] and vesicle transport machinery. Alternatively spliced transcript variants encoding distinct isoforms have been described.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Hsu SC, TerBush D, Abraham M, Guo W |title=The exocyst complex in polarized exocytosis |journal=Int. Rev. Cytol. |volume=233 |issue= |pages= 243–65 |year= 2004 |pmid= 15037366 |doi= 10.1016/S0074-7696(04)33006-8 | series=International Review of Cytology | isbn=978-0-12-364637-8 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Kee Y, Yoo JS, Hazuka CD |title=Subunit structure of the mammalian exocyst complex |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14438–43 |year= 1998 |pmid= 9405631 |doi=10.1073/pnas.94.26.14438 | pmc=25013 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Hsu SC, Hazuka CD, Roth R |title=Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments |journal=Neuron |volume=20 |issue= 6 |pages= 1111–22 |year= 1998 |pmid= 9655500 |doi=10.1016/S0896-6273(00)80493-6 |display-authors=etal}} | ||
*{{cite journal | vauthors=Matern HT, Yeaman C, Nelson WJ, Scheller RH |title=The Sec6/8 complex in mammalian cells: Characterization of mammalian Sec3, subunit interactions, and expression of subunits in polarized cells |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 17 |pages= 9648–53 |year= 2001 |pmid= 11493706 |doi= 10.1073/pnas.171317898 | pmc=55506 }} | |||
*{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Gevaert K, Goethals M, Martens L |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Inoue M, Chang L, Hwang J |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 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Moskalenko S, Tong C, Rosse C |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 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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Exocyst complex component 1 is a protein that in humans is encoded by the EXOC1 gene.[1][2][3]
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 the 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. Alternatively spliced transcript variants encoding distinct isoforms have been described.[3]
References
- ↑ Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Nov 2000). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
- ↑ Brymora A, Valova VA, Larsen MR, Roufogalis BD, Robinson PJ (Aug 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.
- ↑ 3.0 3.1 "Entrez Gene: EXOC1 exocyst complex component 1".
Further reading
- Hsu SC, TerBush D, Abraham M, Guo W (2004). "The exocyst complex in polarized exocytosis". Int. Rev. Cytol. International Review of Cytology. 233: 243–65. doi:10.1016/S0074-7696(04)33006-8. ISBN 978-0-12-364637-8. PMID 15037366.
- 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. doi:10.1073/pnas.94.26.14438. PMC 25013. 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. doi:10.1016/S0896-6273(00)80493-6. PMID 9655500.
- Matern HT, Yeaman C, Nelson WJ, Scheller RH (2001). "The Sec6/8 complex in mammalian cells: Characterization of mammalian Sec3, subunit interactions, and expression of subunits in polarized cells". Proc. Natl. Acad. Sci. U.S.A. 98 (17): 9648–53. doi:10.1073/pnas.171317898. PMC 55506. PMID 11493706.
- 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. PMC 139241. PMID 12477932.
- Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- 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.
- 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.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- 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. PMC 528928. PMID 15489334.
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