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J. Biol. Chem., Vol. 276, Issue 45, 42401-42408, November 9, 2001
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From the Secretory Physiology Section, Gene Therapy and
Therapeutics Branch, NIDCR, National Institutes of Health
Bethesda, Maryland 20892
Ca2+ influx via plasma membrane
Trp3 channels is proposed to be regulated by a reversible interaction
with inositol trisphosphate receptor (IP3R) in the
endoplasmic reticulum. Condensation of the cortical actin layer has
been suggested to physically disrupt this interaction and inhibit
Trp3-mediated Ca2+ influx. This study examines the effect
of cytoskeletal reorganization on the localization and function of Trp3
and key Ca2+ signaling proteins. Calyculin-A treatment
resulted in formation of condensed actin layer at the plasma membrane;
internalization of Trp3, G
Stabilization of Cortical Actin Induces
Internalization of Transient Receptor Potential 3 (Trp3)-associated Caveolar Ca2+ Signaling Complex and Loss
of Ca2+ Influx without Disruption of Trp3-Inositol
Trisphosphate Receptor Association*
,,
q/11, phospholipase
C
, and caveolin-1; and attenuation of
1-oleoyl-2-acetyl-sn-glycerol- and ATP-stimulated
Sr2+ influx. Importantly, Trp3 and IP3R-3
remained co-localized inside the cell and were co-immunoprecipitated.
Jasplakinolide also induced internalization of Trp3 and caveolin-1.
Pretreatment of cells with cytochalasin D or staurosporine did not
affect Trp3 but prevented calyculin-A-induced effects. Based on these
data, we suggest that Trp3 is assembled in a caveolar Ca2+
signaling complex with IP3R, SERCA, Gq/11,
phospholipase C, caveolin-1, and ezrin. Furthermore, our data
demonstrate that conditions which stabilize cortical actin induce loss
of Trp3 activity due to internalization of the Trp3-signaling complex, not disruption of IP3R-Trp3 interaction. This suggests that
localization of the Trp3-associated signaling complex, rather than
Trp3-IP3R coupling, depends on the status of the actin cytoskeleton.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Contributed equally to the results of this work.
§
To whom correspondence should be addressed: Bldg. 10, Rm. 1N-113,
National Institutes of Health, Bethesda, MD 20892. Tel.: 301-496-5298;
Fax: 301-402-1228; E-mail: indu.ambudkar@nih.gov.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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