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First published online 28 October 2008
doi: 10.1242/jcs.029785

Journal of Cell Science 121, 3770-3777 (2008)
Published by The Company of Biologists 2008
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Research Article

Regulation of PLCβ1a membrane anchoring by its substrate phosphatidylinositol (4,5)-bisphosphate

Merel J. W. Adjobo-Hermans, Joachim Goedhart and Theodorus W. J. Gadella, Jr*

Swammerdam Institute for Life Sciences, Section of Molecular Cytology, Centre for Advanced Microscopy, University of Amsterdam, Kruislaan 316, NL-1098 SM, Amsterdam, The Netherlands

* Author for correspondence (e-mail: gadella{at}science.uva.nl)

Accepted 1 September 2008

Basic knowledge as to the subcellular location and dynamics of PLCβ isozymes is scant. Here, we report on the subcellular location of GFP-PLCβ1a and the use of total internal reflection fluorescence (TIRF) microscopy to examine the dynamics of GFP-PLCβ1a at the plasma membrane upon stimulation of Gq-coupled receptors. Using this technique, we observed PLCβ1a dissociation from the plasma membrane upon addition of agonist. An increase in intracellular calcium and a decrease in PtdIns(4,5)P2 both coincided with a translocation of PLCβ1a from the plasma membrane into the cytosol. In order to differentiate between calcium and PtdIns(4,5)P2, rapamycin-induced heterodimerization of FRB and FKBP12 fused to 5-phosphatase IV was used to instantaneously convert PtdIns(4,5)P2 into PtdIns(4)P. Addition of rapamycin caused PLCβ1a to dissociate from the plasma membrane, indicating that removal of PtdIns(4,5)P2 is sufficient to cause translocation of PLCβ1a from the plasma membrane. In conclusion, PLCβ1a localization is regulated by its own substrate.

Key words: PLCβ, PtdIns(4,5)P2, TIRF


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