Document Detail


PLCβ isoforms differ in their subcellular location and their CT-domain dependent interaction with Gαq.
MedLine Citation:
PMID:  23006664     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Phospholipase C (PLC) β isoforms are implicated in various physiological processes and pathologies. However, mechanistic insight into the localization and activation of each of the isoforms is limited. Therefore, it is crucial to gain more in-depth knowledge as to the regulation of the different isoforms. Here we describe the subcellular location of full-length PLCβ isozymes and their C-terminal (CT) domains. Strikingly, we found isoforms PLCβ1 and PLCβ4 to be enriched at the plasma membrane, contrary to isoforms PLCβ2 and PLCβ3. We determined that the CT domain is an inhibitor of Gq-mediated increases in intracellular calcium, the potency of its effect being dependent upon the CT domain isoform used. Furthermore, ratiometric fluorescence resonance energy transfer (FRET) imaging was used to study the kinetics of the Gαq-CTβx interactions. By the use of recently developed tools, which enable the on-demand activation of Gαq, we could show that the interaction between constitutively active Gαq and PLCβ3 prolongs the residence time of PLCβ3 at the plasma membrane. These findings suggest that under physiological circumstances, PLCβ3 and Gαq interact in a kiss-and-run fashion, likely due to the GTPase-activating activity of PLCβ towards Gαq.
Authors:
Merel J W Adjobo-Hermans; Kevin C Crosby; Mateusz Putyrski; Arshia Bhageloe; Laura van Weeren; Carsten Schultz; Joachim Goedhart; Theodorus W J Gadella
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-9-21
Journal Detail:
Title:  Cellular signalling     Volume:  -     ISSN:  1873-3913     ISO Abbreviation:  Cell. Signal.     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-9-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8904683     Medline TA:  Cell Signal     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier Inc.
Affiliation:
Swammerdam Institute for Life Sciences, Section of Molecular Cytology, van Leeuwenhoek Centre for Advanced Microscopy, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands; Nijmegen Centre for Molecular Life Sciences, Department of Biochemistry, Radboud University Nijmegen Medical Centre, Geert Grooteplein 28, 6525 GA Nijmegen, The Netherlands. Electronic address: m.adjobo-hermans@ncmls.ru.nl.
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