Abstract 5098:In silicoanalysis of the membrane targeting mechanism of the pleckstrin homology domains within the oncogenic Grb2-associated-binding protein family

Author(s):  
Antonio Lopez ◽  
Ezza Awan ◽  
Areeba Zaheer ◽  
Shaneen Singh
2004 ◽  
Vol 32 (5) ◽  
pp. 707-711 ◽  
Author(s):  
M.A. Lemmon

PH domains (pleckstrin homology domains) are the 11th most common domain in the human genome and are best known for their ability to target cellular membranes by binding specifically to phosphoinositides. Recent studies in yeast have shown that, in fact, this is a property of only a small fraction of the known PH domains. Most PH domains are not capable of independent membrane targeting, and those capable of doing so (approx. 33%) appear, most often, to require both phosphoinositide and non-phosphoinositide determinants for their subcellular localization. Several recent studies have suggested that small GTPases such as ARF family proteins play a role in defining PH domain localization. Some others have described a signalling role for PH domains in regulating small GTPases, although phosphoinositides may also play a role. These findings herald a change in our perspective of PH domain function, which will be significantly more diverse than previously supposed.


2004 ◽  
Vol 13 (5) ◽  
pp. 677-688 ◽  
Author(s):  
Jong W. Yu ◽  
Jeannine M. Mendrola ◽  
Anjon Audhya ◽  
Shaneen Singh ◽  
David Keleti ◽  
...  

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