期刊
IMMUNITY
卷 19, 期 5, 页码 669-678出版社
CELL PRESS
DOI: 10.1016/S1074-7613(03)00297-8
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资金
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH &HUMAN DEVELOPMENT [R01HD037091] Funding Source: NIH RePORTER
- NATIONAL CANCER INSTITUTE [R01CA081140] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI033617, R01AI038348] Funding Source: NIH RePORTER
- NCI NIH HHS [CA81140] Funding Source: Medline
- NIAID NIH HHS [AI38348, AI33617] Funding Source: Medline
- NICHD NIH HHS [HD37091] Funding Source: Medline
- NIGMS NIH HHS [GM54389, GM53590] Funding Source: Medline
Intracellular signaling by most cell surface receptors requires the generation of two major second messengers, phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P-3) and inositol-1,4,5-trisphosphate (IP3) The enzymes that produce these second messengers phosphoinositide 3-kinase (PI3K) and phospholipase C (PLC), utilize a common substrate, phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P-2). Until now, it has not been clear whether de novo PtdIns-4,5-P2 synthesis is necessary for PtdIns-3,4,5-P3 and IP3 production. Here we show that BTK, a member of the Tec family of cytoplasmic protein tyrosine kinases, associates with phosphatidylinositol-4-phosphate 5-kinases (PIP5Ks), the enzymes that synthesize PtdIns-4,5-P-2. Upon B cell receptor activation, BTK brings PIP5K to the plasma membrane as a means of generating local PtdIns-4,5-P2 synthesis. This enzyme-enzyme interaction provides a shuttling mechanism that allows BTK to stimulate the production of the substrate required by both its upstream activator, PI3K, and its downstream target, PLC-gamma2.
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