A likely role for a novel PH-domain containing protein, PEPP2, in connecting membrane and cytoskeleton
Biocell
;
36(3): 127-132, Dec. 2012. ilus, graf
Article
Dans Anglais
| LILACS
| ID: lil-694713
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.
Texte intégral:
Disponible
Indice:
LILAS (Amériques)
Sujet Principal:
Cytosquelette
/
Membrane cellulaire
/
Protéines à homéodomaine
Limites du sujet:
Animaux
langue:
Anglais
Texte intégral:
Biocell
Thème du journal:
Clulas
Année:
2012
Type:
Article
/
descriptif de projet
Pays d'affiliation:
Chine
Institution/Pays d'affiliation:
Jinan University/CN
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