Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a
protein that in humans is encoded by the CYTH1gene.[5][6][7]
Function
Cytohesin-1 (CYTH1) is a member of the cytohesin family. Members of this family have identical structural organization that consists of an
N-terminalcoiled-coil motif, a central Sec7 domain, and a
C-terminalpleckstrin 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. The CYTH1 is highly expressed in
natural killer and peripheral
T cells, and regulates the adhesiveness of integrins at the plasma membrane of
lymphocytes. CYTH1 protein is 83% homologous to
CYTH2.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Liu L, Pohajdak B (September 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.
doi:
10.1016/0167-4781(92)90055-5.
PMID1511013.
^Dixon B, Mansour M, Pohajdak B (April 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.
doi:
10.1159/000133498.
PMID8449036.
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.
PMID10772823.
Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a
protein that in humans is encoded by the CYTH1gene.[5][6][7]
Function
Cytohesin-1 (CYTH1) is a member of the cytohesin family. Members of this family have identical structural organization that consists of an
N-terminalcoiled-coil motif, a central Sec7 domain, and a
C-terminalpleckstrin 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. The CYTH1 is highly expressed in
natural killer and peripheral
T cells, and regulates the adhesiveness of integrins at the plasma membrane of
lymphocytes. CYTH1 protein is 83% homologous to
CYTH2.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Liu L, Pohajdak B (September 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.
doi:
10.1016/0167-4781(92)90055-5.
PMID1511013.
^Dixon B, Mansour M, Pohajdak B (April 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.
doi:
10.1159/000133498.
PMID8449036.
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.
PMID10772823.