The N-terminal domain of the type 1 Ins(1,4,5)P3 receptor stably expressed in MDCK cells interacts with myosin IIA and alters epithelial cell morphology

Autor: Michel C Hours, Laurence Mery
Rok vydání: 2010
Předmět:
Zdroj: Journal of Cell Science. 123:1449-1459
ISSN: 1477-9137
0021-9533
Popis: Cytosolic Ca2+ controls a wide range of cellular events. The versatility of this second messenger depends on its ability to form diverse spatial and temporal patterns, including waves and oscillations. Ca2+-signaling patterns are thought to be determined in part by the subcellular distribution of inositol (1,4,5)-trisphosphate receptors [Ins(1,4,5)P3Rs] but little is currently known about how the localization of the Ins(1,4,5)P3R itself is regulated. Here, we report that the recruitment of GFP-tagged Ins(1,4,5)P3Rs in the vicinity of tight junctions in Madin-Darby canine kidney (MDCK) cells requires the N-terminal domain. Stable expression of this domain in polarized MDCK cells induced a flattened morphology, affected cytokinesis, accelerated cell migration in response to monolayer wounding and interfered with the cortical targeting of myosin IIA. In addition, downregulation of myosin IIA in polarized MDCK cells was found to mimic the effects of stable expression of the N-terminal part of Ins(1,4,5)P3R on cell shape and to alter localization of endogenous Ins(1,4,5)P3Rs. Taken together, these results support a model in which the recruitment of Ins(1,4,5)P3Rs at the apex of the lateral membrane in polarized MDCK cells, involves myosin IIA and might be important for the regulation of cortical actin dynamics.
Databáze: OpenAIRE