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
in En
| LILACS
| ID: lil-694713
Responsible library:
AR1.2
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.
Key words
Full text:
1
Index:
LILACS
Main subject:
Cytoskeleton
/
Cell Membrane
/
Homeodomain Proteins
Limits:
Animals
Language:
En
Journal:
Biocell
Journal subject:
Clulas
Year:
2012
Type:
Article
/
Project document