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| Zou,Yi; Zhong,Wenping. |
| PH domains (pleckstrin homology) are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular apartments with assistances of alternative binding partners. PH domain-containing proteins are 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, displayed moderate phosphoinositide binding specificity. Full length PEPP2 associated with both 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,... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Microtubule; Membrane; Phosphoinositide; Microviscosity; Wortmannin. |
| Ano: 2012 |
URL: http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0327-95452012000300005 |
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