Journal: | Biocell |
Database: | PERIÓDICA |
System number: | 000366026 |
ISSN: | 0327-9545 |
Authors: | Zou, Yi1 Zhong, Wenping1 |
Institutions: | 1Jinan University, School of Life Science and Technology, Guangzhou, Guangdong. China |
Year: | 2012 |
Season: | Dic |
Volumen: | 36 |
Number: | 3 |
Pages: | 127-132 |
Country: | Argentina |
Language: | Inglés |
Document type: | Artículo |
Approach: | Experimental, analítico |
English abstract | 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 |
Disciplines: | Biología |
Keyword: | Biología celular, Membrana celular, Citoesqueleto, Proteínas, Microtúbulos, Fosfoinositidas, Viscosidad |
Keyword: | Biology, Cell biology, Cell membrane, Cytoskeleton, Proteins, Microtubules, Phosphoinositides, Viscosity |
Full text: | Texto completo (Ver HTML) |