CYTH4: Difference between revisions
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'''Cytohesin-4''' is a [[protein]] that in humans is encoded by the ''CYTH4'' [[gene]].<ref name="pmid10591208">{{cite journal | vauthors = Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP | title = The DNA sequence of human chromosome 22 | journal = Nature | volume = 402 | issue = 6761 | pages = 489–95 |date=Dec 1999 | pmid = 10591208 | pmc = | doi = 10.1038/990031 |display-authors=etal}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSCD4 pleckstrin homology, Sec7 and coiled-coil domains 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27128| accessdate = }}</ref> | '''Cytohesin-4''' is a [[protein]] that in humans is encoded by the ''CYTH4'' [[gene]].<ref name="pmid10591208">{{cite journal | vauthors = Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP | title = The DNA sequence of human chromosome 22 | journal = Nature | volume = 402 | issue = 6761 | pages = 489–95 |date=Dec 1999 | pmid = 10591208 | pmc = | doi = 10.1038/990031 |display-authors=etal}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSCD4 pleckstrin homology, Sec7 and coiled-coil domains 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27128| accessdate = }}</ref> | ||
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{{PBB_Summary | {{PBB_Summary | ||
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| summary_text = This gene encodes a member of the cytohesin (CYTH) family, formerly known as the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. CYTH4 exhibits GEP activity in vitro with both ARF1 and ARF5 but is inactive with ARF6. The CYTH4 and CYTH1 gene structures are very similar.<ref name="entrez" /> | | summary_text = This gene encodes a member of the cytohesin (CYTH) family, formerly known as the PSCD ([[pleckstrin homology]], Sec7 and [[coiled-coil]] domains) family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with [[phospholipids]] and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and [[membrane trafficking]]. CYTH4 exhibits GEP activity in vitro with both [[ARF1]] and [[ARF5]] but is inactive with [[ARF6]]. The CYTH4 and [[CYTH1]] gene structures are very similar.<ref name="entrez" /> | ||
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Revision as of 20:24, 28 February 2018
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Cytohesin-4 is a protein that in humans is encoded by the CYTH4 gene.[1][2]
This gene encodes a member of the cytohesin (CYTH) family, formerly known as the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. CYTH4 exhibits GEP activity in vitro with both ARF1 and ARF5 but is inactive with ARF6. The CYTH4 and CYTH1 gene structures are very similar.[2]
References
- ↑ Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al. (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
- ↑ 2.0 2.1 "Entrez Gene: PSCD4 pleckstrin homology, Sec7 and coiled-coil domains 4".
Further reading
- Morishige M, Hashimoto S, Ogawa E, et al. (2008). "GEP100 links epidermal growth factor receptor signalling to Arf6 activation to induce breast cancer invasion". Nat. Cell Biol. 10 (1): 85–92. doi:10.1038/ncb1672. PMID 18084281.
- 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.
- Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- 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.
- Venkateswarlu K (2003). "Interaction protein for cytohesin exchange factors 1 (IPCEF1) binds cytohesin 2 and modifies its activity". J. Biol. Chem. 278 (44): 43460–9. doi:10.1074/jbc.M304078200. PMID 12920129.
- 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.
- Ogasawara M, Kim SC, Adamik R, et al. (2000). "Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors". J. Biol. Chem. 275 (5): 3221–30. doi:10.1074/jbc.275.5.3221. PMID 10652308.
- Trofatter JA, Long KR, Murrell JR, et al. (1996). "An expression-independent catalog of genes from human chromosome 22". Genome Res. 5 (3): 214–24. doi:10.1101/gr.5.3.214. PMID 8593609.
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