PSCD1

From Wikipedia, the free encyclopedia

Pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1)

PDB rendering based on 1bc9.

Available structures: 1bc9, 1u2b

Identifiers

Symbol(s)

PSCD1; B2-1; CYTOHESIN-1; D17S811E; FLJ34050; FLJ41900; SEC7

External IDs

OMIM: 182115 MGI: 1334257 HomoloGene: 31262

Gene ontology
Molecular Function:	• ARF guanyl-nucleotide exchange factor activity • protein binding
Cellular Component:	• intracellular • cytoplasm • plasma membrane
Biological Process:	• vesicle-mediated transport • regulation of cell adhesion • regulation of ARF protein signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004762 (mRNA)
NP_004753 (protein)

NM_011180 (mRNA)
NP_035310 (protein)

Location

Chr 17: 74.18 - 74.29 Mb

Chr 11: 117.98 - 118.03 Mb

Pubmed search

[1]

[2]

Pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1), also known as PSCD1, is a human gene.^[1]

Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a member of the PSCD 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 PSCDs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. The PSCD1 is highly expressed in natural killer and peripheral T cells, and regulates the adhesiveness of integrins at the plasma membrane of lymphocytes. PSCD1 protein is 83% homologous to PSCD2.^[1]

[edit] References

^ ^a ^b Entrez Gene: PSCD1 pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1).

[edit] Further reading

Liu L, Pohajdak B (1992). "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7.". Biochim. Biophys. Acta 1132 (1): 75–8. PMID 1511013.
Dixon B, Mansour M, Pohajdak B (1993). "Assignment of human B2-1 gene (D17S811E) to chromosome 17qter by PCR analysis of somatic cell hybrids and fluorescence in situ hybridization.". Cytogenet. Cell Genet. 63 (1): 42–4. PMID 8449036.
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.
Kolanus W, Nagel W, Schiller B, et al. (1996). "Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule.". Cell 86 (2): 233–42. PMID 8706128.
Meacci E, Tsai SC, Adamik R, et al. (1997). "Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor.". Proc. Natl. Acad. Sci. U.S.A. 94 (5): 1745–8. PMID 9050849.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Nagel W, Zeitlmann L, Schilcher P, et al. (1998). "Phosphoinositide 3-OH kinase activates the beta2 integrin adhesion pathway and induces membrane recruitment of cytohesin-1.". J. Biol. Chem. 273 (24): 14853–61. PMID 9614087.
Betz SF, Schnuchel A, Wang H, et al. (1998). "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1.". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7909–14. PMID 9653114.
Nagel W, Schilcher P, Zeitlmann L, Kolanus W (1998). "The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function.". Mol. Biol. Cell 9 (8): 1981–94. PMID 9693361.
Pacheco-Rodriguez G, Meacci E, Vitale N, et al. (1998). "Guanine nucleotide exchange on ADP-ribosylation factors catalyzed by cytohesin-1 and its Sec7 domain.". J. Biol. Chem. 273 (41): 26543–8. PMID 9756891.
Rietzler M, Bittner M, Kolanus W, et al. (1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins.". J. Biol. Chem. 273 (42): 27459–66. PMID 9765275.
Schürmann A, Schmidt M, Asmus M, et al. (1999). "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D.". J. Biol. Chem. 274 (14): 9744–51. PMID 10092663.
Pacheco-Rodriguez G, Patton WA, Adamik R, et al. (1999). "Structural elements of ADP-ribosylation factor 1 required for functional interaction with cytohesin-1.". J. Biol. Chem. 274 (18): 12438–44. PMID 10212218.
Venkateswarlu K, Gunn-Moore F, Tavaré JM, Cullen PJ (1999). "EGF-and NGF-stimulated translocation of cytohesin-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohesin-1 PH domain.". J. Cell. Sci. 112 ( Pt 12): 1957–65. PMID 10341214.
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. PMID 10652308.
Vitale N, Pacheco-Rodriguez G, Ferrans VJ, et al. (2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1).". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148.
Lee SY, Mansour M, Pohajdak B (2000). "B2-1, a Sec7- and pleckstrin homology domain-containing protein, localizes to the Golgi complex.". Exp. Cell Res. 256 (2): 515–21. doi:10.1006/excr.2000.4845. PMID 10772823.
Geiger C, Nagel W, Boehm T, et al. (2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1.". EMBO J. 19 (11): 2525–36. doi:10.1093/emboj/19.11.2525. PMID 10835351.
Dierks H, Kolanus J, Kolanus W (2001). "Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain.". J. Biol. Chem. 276 (40): 37472–81. doi:10.1074/jbc.M101502200. PMID 11438522.
Tang P, Cheng TP, Agnello D, et al. (2002). "Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity.". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2625–9. doi:10.1073/pnas.052712999. PMID 11867758.