Faculty Opinions recommendation of Inositol lipid binding and membrane localization of isolated pleckstrin homology (PH) domains. Studies on the PH domains of phospholipase C delta 1 and p130.

2002 ◽  
Author(s):  
Carole Parent
Keyword(s):  
Phospholipase C ◽  
Lipid Binding ◽  
Membrane Localization ◽  
Pleckstrin Homology ◽  
Ph Domains

scholarly journals Inositol Lipid Binding and Membrane Localization of Isolated Pleckstrin Homology (PH) Domains

2002 ◽  
Vol 277 (30) ◽  
pp. 27412-27422 ◽  
Author(s):  
Péter Várnai ◽  
Xuena Lin ◽  
Sang Bong Lee ◽  
Galina Tuymetova ◽  
Tzvetanka Bondeva ◽  
...  
Keyword(s):  
Lipid Binding ◽  
Membrane Localization ◽  
Pleckstrin Homology ◽  
Ph Domains

scholarly journals Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae

2018 ◽  
Vol 74 (5) ◽  
pp. 315-321 ◽  
Author(s):  
Imtiaz Ali ◽  
Sungmin Eu ◽  
Daniel Koch ◽  
Nathalie Bleimling ◽  
Roger S. Goody ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Membrane Binding ◽  
Lipid Binding ◽  
Relative Orientation ◽  
Pleckstrin Homology ◽  
Gtpase Activating Protein ◽  
Ph Domains

The structure of the tandem lipid-binding PX and pleckstrin-homology (PH) domains of the Cdc42 GTPase-activating protein Bem3 from Saccharomyces cerevisiae (strain S288c) has been determined to a resolution of 2.2 Å (R work = 21.1%, R free = 23.4%). It shows that the domains adopt a relative orientation that enables them to simultaneously bind to a membrane and suggests possible cooperativity in membrane binding.

scholarly journals Lipid binding by the N-terminal motif mediates plasma membrane localization of Bordetella effector protein BteA

2021 ◽  
pp. 100607
Author(s):  
Ivana Malcova ◽  
Ladislav Bumba ◽  
Filip Uljanic ◽  
Darya Kuzmenko ◽  
Jana Nedomova ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Binding ◽  
Membrane Localization ◽  
Effector Protein ◽  
Plasma Membrane Localization

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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