About CYTH / Cytohesin:
Previously known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1), Cytohesin-1 is a member of the cytohesin 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.
In Cytohesin, the coiled-coil motif is involved in homodimerization. You will also find that the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity and the PH domain interacts with phospholipids. The PH domain is primarily responsible for association of CYTHs with membranes.
CYTHs help to mediate the regulation of protein sorting and membrane trafficking. The CYTH1 in particular is highly expressed in natural killer and peripheral T cells It also regulates the adhesiveness of integrins at the plasma membrane of lymphocytes. CYTH1 protein is 83% homologous to CYTH2.
In regards to interactions, CYTH1 has been shown to interact with: ARFRP1, CD18 and TRIM23.