Structure/Function Relationships of Phospholipases C Beta

被引：14

作者：

Sandal, Massimo ^{[1
,2
]}

Paltrinieri, Daniele ^{[1
]}

Carloni, Paolo ^{[2
,3
]}

Musiani, Francesco ^{[4
]}

Giorgetti, Alejandro ^{[1
,2
]}

机构：

[1] Univ Verona, Dept Biotechnol, I-37134 Verona, Italy

[2] German Res Sch Simulat Sci, D-52425 Julich, Germany

[3] Forschungszentrum Julich, Inst Adv Simulat, D-52425 Julich, Germany

[4] Int Sch Adv Studies ISAS SISSA, Trieste, Italy

来源：

CURRENT PROTEIN & PEPTIDE SCIENCE | 2013年 / 14卷 / 08期

关键词：

Phospholipases C beta; cell signaling; protein structural biology; PLECKSTRIN HOMOLOGY DOMAIN; SINGLE-MOLECULE TRACKING; G-ALPHA-Q; GAMMA-SUBUNITS; G-PROTEINS; MEMBRANE INTERACTIONS; BINDING PROTEIN; GTP-BINDING; ACTIVATION; SIMULATIONS;

D O I：

10.2174/13892037113146660085

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phospholipases C beta (PLC-beta s) are essential components of the signal transduction of metazoans. They catalyze the production of the second messengers inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) from the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2). These enzymes are activated by G-protein-coupled receptors (GPCRs) through the interaction with the alpha subunit of heterotrimeric G-proteins belonging to the G(q) family (G alpha(q)), the G subunits released by the inhibitory G-protein (G(i)) and Ca2+ ions. Here we review current structural insights on these important proteins, with a particular focus on the most structurally characterized isoform (PLC-beta 3) and the activation mechanism operated by G alpha(q). We propose, following the lead of recent studies, that a tight combination of experiments and molecular simulations are instrumental in further enlightening the structure/function understanding of PLC-beta s.

引用

页码：650 / 657

页数：8

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