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

FEBS Letters

Maffucci, Tania¹  Falasca, Marco¹ 

[1] The Sackler Institute, University College London, 5 University Street, London WC1E 6JJ, UK

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;   

DOI  :  10.1016/S0014-5793(01)02909-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown