TY  - JOUR
AU  - Sandal, Massimo
AU  - Paltrinieri, Daniele
AU  - Carloni, Paolo
AU  - Musiani, Francesco
AU  - Giorgetti, Alejandro
TI  - Structure/Function Relationships of Phospholipases C Beta
JO  - Current protein & peptide science
VL  - 14
IS  - 8
SN  - 1389-2037
CY  - Hilversum
PB  - Bentham Science Publ.
M1  - FZJ-2015-03608
SP  - 650 - 657
PY  - 2013
AB  - Phospholipases C beta (PLC-βs) 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 Gq family (Gαq), the Gβγ subunits released by the inhibitory G-protein (Gi) and Ca2+ ions. Here we review current structural insights on these important proteins, with a particular focus on the most structurally characterized isoform (PLC-β3) and the activation mechanism operated by Gαq. 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-βs. - See more at: http://www.eurekaselect.com/116059/article#sthash.cojH1BB1.dpuf
LB  - PUB:(DE-HGF)16 ; PUB:(DE-HGF)36
C6  - pmid:24384033
UR  - <Go to ISI:>//WOS:000329125100002
DO  - DOI:10.2174/13892037113146660085
UR  - https://juser.fz-juelich.de/record/201303
ER  -