Abstract
PH (pleckstrin homology) domains are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular compartments with as - sistances of alternative binding partners. PH domain-containing proteins have been found to be involved in a wide range of cellular events, including signalling, cytoskeleton rearrangement and vesicular trafficking. Here we showed that a novel PH domain-containing protein, PEPP2 (also known as PLEKHA5), displays mode- rate phosphoinositide binding specificity. Full length PEPP2 was observed to variably associate with both the plasma membrane and microtubules. The membrane-associated PEPP2 nucleated at cell-cell contacts and the leading edge of migrating cells. Overexpression of PEPP2 increased membrane microviscosity, in- dicating a potential role for PEPP2 in regulating function of microtubule-dependent membrane functions.
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