CYTH1

Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a is_associated_with::protein that in humans is encoded by the CYTH1 is_associated_with::gene.

Function
Cytohesin-1 (CYTH1) is a member of the cytohesin family. Members of this family have identical structural organization that consists of an is_associated_with::N-terminal is_associated_with::coiled-coil motif, a central Sec7 domain, and a is_associated_with::C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in is_associated_with::homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with is_associated_with::phospholipids and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of is_associated_with::protein sorting and membrane trafficking. The CYTH1 is highly expressed in is_associated_with::natural killer and peripheral is_associated_with::T cells, and regulates the adhesiveness of integrins at the plasma membrane of is_associated_with::lymphocytes. CYTH1 protein is 83% homologous to is_associated_with::CYTH2.

Interactions
CYTH1 has been shown to interact with:
 * is_associated_with::ARFRP1,
 * is_associated_with::CD18, and
 * is_associated_with::TRIM23.