SciELO - Scientific Electronic Library Online

 
vol.36 número3Knockdown of apoptosis-inducing factor disrupts function of respiratory complex IStructural analysis of flagellar axonemes from inner arm dynein knockdown strains of Trypanosoma brucei índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados

Revista

Articulo

Indicadores

  • No hay articulos citadosCitado por SciELO

Links relacionados

Compartir


Biocell

versión impresa ISSN 0327-9545

Resumen

ZOU, Yi  y  ZHONG, Wenping. A likely role for a novel PH-domain containing protein, PEPP2, in connecting membrane and cytoskeleton. Biocell [online]. 2012, vol.36, n.3, pp.127-132. ISSN 0327-9545.

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, indicating a potential role of PEPP2 in regulating function of membrane and microtubules.

Palabras clave : Microtubule; Membrane; Phosphoinositide; Microviscosity; Wortmannin.

        · texto en Inglés

 

Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons