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J. Biol. Chem., Vol. 277, Issue 50, 48303-48310, December 13, 2002
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From the Rammelkamp Center for Education and Research, MetroHealth
Medical Center, and Department of Physiology and Biophysics, Case
Western Reserve University School of Medicine,
Cleveland, Ohio 44106
TRPC genes encode
a ubiquitous family of ion channel proteins responsible for
Ca2+ influx following stimulation of G-protein-coupled
membrane receptors linked to phospholipase C. These channels may be
localized to large multimeric signaling complexes via association with
PDZ-containing scaffolding proteins. Based on sequence homology, the
TRPC channel family can be divided into two major subgroups: TRPC1,
-C4, and -C5 and TRPC3, -C6, and -C7. Although TRPC channels are
thought to be tetramers, the actual subunit composition remains
unknown. To determine subunit arrangement, individual TRPC channel
pairs were heterologously expressed in Sf9 insect cells and
immunoprecipitated using affinity-purified rabbit polyclonal antibodies
specific for each channel subtype. Reciprocal co-immunoprecipitations
showed that TRPC1, -C4, and -C5 co-associate and that TRPC3, -C6, and -C7 co-associate but that cross-association between the two major subgroups does not occur. Additionally, the interaction between each
TRPC channel and the PDZ-containing protein, INAD (protein responsible
for the
inactivation-no-after-potential
Drosophila mutant), was examined. TRPC1, -C4, and -C5
co-immunoprecipitated with INAD, whereas TRPC3, -C6, and -C7 did not.
To define channel subunit interactions in vivo,
immunoprecipitations were performed from isolated rat brain
synaptosomal preparations. The results revealed that TRPC1, -C4, and
-C5 co-associate and that TRPC3, -C6, and -C7 co-associate in both
cortex and cerebellum but that cross-association between the two major
subgroups does not occur. These results demonstrate that TRPC channels
are present in nerve terminals and provide the first direct evidence
for selective assembly of channel subunits in
vivo.
Selective Association of TRPC Channel Subunits in Rat Brain
Synaptosomes*,
*
This work was supported in part by General Medical Sciences,
National Institutes of Health Grant GM52019 (to W. P. S.) and by
American Heart Association, Northeast Ohio Affiliate, postdoctoral fellowship award 20381B (to M. G.).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.
The on-line version of this article (available at
http://www.jbc.org) contains two additional figures.
To whom all correspondence should be addressed: Rammelkamp Center,
Rm. R322, MetroHealth Medical Center, 2500 MetroHealth Dr., Cleveland,
OH 44109-1998. Tel.: 216-778-8965; Fax: 216-778-8997; E-mail:
wschilling@metrohealth.org.
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S. Cayouette, M. P. Lussier, E.-L. Mathieu, S. M. Bousquet, and G. Boulay Exocytotic Insertion of TRPC6 Channel into the Plasma Membrane upon Gq Protein-coupled Receptor Activation J. Biol. Chem., February 20, 2004; 279(8): 7241 - 7246. [Abstract] [Full Text] [PDF]
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 R. L. Corteling, S. Li, J. Giddings, J. Westwick, C. Poll, and I. P. Hall Expression of Transient Receptor Potential C6 and Related Transient Receptor Potential Family Members in Human Airway Smooth Muscle and Lung Tissue Am. J. Respir. Cell Mol. Biol., February 1, 2004; 30(2): 145 - 154. [Abstract] [Full Text] [PDF]
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R. Ma, D. Rundle, J. Jacks, M. Koch, T. Downs, and L. Tsiokas Inhibitor of Myogenic Family, a Novel Suppressor of Store-operated Currents through an Interaction with TRPC1 J. Biol. Chem., December 26, 2003; 278(52): 52763 - 52772. [Abstract] [Full Text] [PDF]
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A. Dietrich, M. Mederos y Schnitzler, J. Emmel, H. Kalwa, T. Hofmann, and T. Gudermann N-Linked Protein Glycosylation Is a Major Determinant for Basal TRPC3 and TRPC6 Channel Activity J. Biol. Chem., November 28, 2003; 278(48): 47842 - 47852. [Abstract] [Full Text] [PDF]
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C. Strubing, G. Krapivinsky, L. Krapivinsky, and D. E. Clapham Formation of Novel TRPC Channels by Complex Subunit Interactions in Embryonic Brain J. Biol. Chem., October 3, 2003; 278(40): 39014 - 39019. [Abstract] [Full Text] [PDF]
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