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Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide–protein co‐operative mechanism
[摘要]

Pleckstrin homology (PH) domains are protein modules found in proteins involved in many cellular processes. The majority of PH domain-containing proteins require membrane association for their function. It has been shown that most PH domains interact directly with the cell membrane by binding to phosphoinositides with a broad range of specificity and affinity. While a highly specific binding of the PH domain to a phosphoinositide can be necessary and sufficient for the correct recruitment of the host protein to the membrane, a weaker and less specific interaction may be necessary but not sufficient, thus probably requiring alternative, co-operative mechanisms.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Pleckstrin homology domain;Phosphoinositide;Membrane targeting;Signal transduction;Phosphoinositide 3-kinase;PH;pleckstrin homology;β-ARK;β-adrenergic receptor kinase;Btk;Bruton's tyrosine kinase;IRS;insulin receptor substrate;PHIP;PH-interacting protein;PtdIns-4;5-P2;phosphatidylinositol 4;5-bisphosphate;PI 3-K;phosphoinositide 3-kinase;PLC;phospholipase C;Grp1;general receptor for 3-phosphoinositides;PtdIns-3;4;5-P3;phosphatidylinositol 3;4;5-trisphosphate;PTB;phosphotyrosine binding;DAG K-δ;diacylglycerol kinase-δ;Gab1;Grb2-associated protein 1;EGF;endothelial growth factor;MBD;Met binding domain [时效性] 
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