scholarly journals Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains

EMBO Reports ◽  
2010 ◽  
Vol 11 (4) ◽  
pp. 279-284 ◽  
Author(s):  
Marc Lenoir ◽  
Ünal Coskun ◽  
Michal Grzybek ◽  
Xinwang Cao ◽  
Sabine B Buschhorn ◽  
...  
Keyword(s):  
Structural Basis ◽  
Golgi Membrane ◽  
Pleckstrin Homology ◽  
Homology Domains

scholarly journals Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains

2000 ◽  
Vol 6 (2) ◽  
pp. 373-384 ◽  
Author(s):  
Kathryn M. Ferguson ◽  
Jennifer M. Kavran ◽  
Vijay G. Sankaran ◽  
Emmanuel Fournier ◽  
Steven J. Isakoff ◽  
...  
Keyword(s):  
Structural Basis ◽  
Pleckstrin Homology ◽  
Homology Domains

scholarly journals Structural Basis of 3-Phosphoinositide Recognition by Pleckstrin Homology Domains

2000 ◽  
Vol 6 (2) ◽  
pp. 385-394 ◽  
Author(s):  
Susan E. Lietzke ◽  
Sahana Bose ◽  
Thomas Cronin ◽  
Jes Klarlund ◽  
Anil Chawla ◽  
...  
Keyword(s):  
Structural Basis ◽  
Pleckstrin Homology ◽  
Phosphoinositide Recognition ◽  
Homology Domains

Pleckstrin homology domains: not just for phosphoinositides

2004 ◽  
Vol 32 (5) ◽  
pp. 707-711 ◽  
Author(s):  
M.A. Lemmon
Keyword(s):  
Subcellular Localization ◽  
Human Genome ◽  
Small Gtpases ◽  
Membrane Targeting ◽  
Ph Domain ◽  
Cellular Membranes ◽  
Pleckstrin Homology ◽  
Ph Domains ◽  
Common Domain ◽  
Homology Domains

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.

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