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* Institut für Pharmakologie und Toxikologie,
Philipps-Universität Marburg, Karl-von-Frisch-Strasse 1, D-35033
Marburg, Germany; and Edited by John H. Exton, Vanderbilt University School of
Medicine, Nashville, TN, and approved March 21, 2002 (received for review November 7, 2001)
Hormones, neurotransmitters, and growth factors give rise to
calcium entry via receptor-activated cation channels that are activated
downstream of phospholipase C activity. Members of the transient
receptor potential channel (TRPC) family have been characterized as
molecular substrates mediating receptor-activated cation influx. TRPC channels are assumed to be composed of multiple TRPC
proteins. However, the cellular principles governing the assembly of
TRPC proteins into homo- or heteromeric ion channels still remain
elusive. By pursuing four independent experimental approaches
Cell Biology
Subunit composition of mammalian transient receptor potential
channels in living cells
,, and
Institut für Pharmakologie,
Freie Universität Berlin, Thielallee 67-73, D-14195 Berlin,
Germany
i.e.,
subcellular cotrafficking of TRPC subunits, differential functional
suppression by dominant-negative subunits, fluorescence resonance
energy transfer between labeled TRPC subunits, and
coimmunoprecipitationwe investigate the combinatorial rules of TRPC
assembly. Our data show that (i) TRPC2 does not
interact with any known TRPC protein and (ii) TRPC1 has
the ability to form channel complexes together with TRPC4 and TRPC5.
(iii) All other TRPCs exclusively assemble into
homo- or heterotetramers within the confines of TRPC
subfamiliese.g., TRPC4/5 or TRPC3/6/7. The principles of
TRPC channel formation offer the conceptual framework to assess the
physiological role of distinct TRPC proteins in living cells.
To whom reprint requests should be addressed.
E-mail: guderman{at}mailer.uni-marburg.de.
www.pnas.org/cgi/doi/10.1073/pnas.102596199
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