A likely role for a novel PH-domain containing protein PEPP2 in connecting membrane and cytoskeleton
Título del documento: A likely role for a novel PH-domain containing protein PEPP2 in connecting membrane and cytoskeleton
Revista: Biocell
Base de datos: PERIÓDICA
Número de sistema: 000366026
ISSN: 0327-9545
Autores: 1
1
Instituciones: 1Jinan University, School of Life Science and Technology, Guangzhou, Guangdong. China
Año:
Periodo: Dic
Volumen: 36
Número: 3
Paginación: 127-132
País: Argentina
Idioma: Inglés
Tipo de documento: Artículo
Enfoque: Experimental, analítico
Resumen en inglés 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
Disciplinas: Biología
Palabras clave: Biología celular,
Membrana celular,
Citoesqueleto,
Proteínas,
Microtúbulos,
Fosfoinositidas,
Viscosidad
Keyword: Biology,
Cell biology,
Cell membrane,
Cytoskeleton,
Proteins,
Microtubules,
Phosphoinositides,
Viscosity
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