Pleckstrin Homology Domain Containing Family M, Member 2 (PLEKHM2)

SKIP protein contains an N-terminal RUN motif and a C-terminal pleckstrin homology domain. SKIP localized to the cytosol in HeLa cells and was partially recruited to membranes upon ectopic expression of SifA.The deduced protein contains 1,020 amino acids. RT-PCR ELISA detected intermediate expression in all tissues examined.

SKIP inhibited kinesin recruitment during Salmonella infection, and SKIP activity was required for positioning and maintenance of the Salmonella-containing vacuole. In uninfected cells, SKIP depletion by RNA interference led to scattering of Golgi vesicles. The RUN domain of SKIP interacted with kinesin, and recruitment of SKIP to membranes displaced kinesin. Boucrot et al. (2005) hypothesized that SKIP is a negative regulator of kinesin motor activity within a regulatory complex of proteins.