Pleckstrin homology domains: not just for phosphoinositides. Export

@article{citeulike:859298, abstract = {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.}, address = {Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Blvd, Philadelphia, PA 19104-6059, USA. mlemmon@mail.med.upenn.edu}, author = {Lemmon, M. A.}, citeulike-article-id = {859298}, citeulike-linkout-0 = {http://dx.doi.org/10.1042/BST0320707}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15493994}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15493994}, doi = {10.1042/BST0320707}, issn = {0300-5127}, journal = {Biochem Soc Trans}, keywords = {gtpase, pkd, rap1}, month = {November}, number = {Pt 5}, pages = {707--711}, posted-at = {2006-09-22 20:25:17}, priority = {0}, title = {Pleckstrin homology domains: not just for phosphoinositides.}, url = {http://dx.doi.org/10.1042/BST0320707}, volume = {32}, year = {2004} }

TY - JOUR ID - citeulike:859298 L3 - citeulike-article-id:859298 N2 - 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. IS - Pt 5 JF - Biochem Soc Trans SN - 0300-5127 AD - Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Blvd, Philadelphia, PA 19104-6059, USA. mlemmon@mail.med.upenn.edu EP - 711 TI - Pleckstrin homology domains: not just for phosphoinositides. VL - 32 SP - 707 KW - gtpase KW - pkd KW - rap1 AU - Lemmon, MA PY - 2004/11// UR - http://dx.doi.org/10.1042/BST0320707 ER -