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Physiological Reviews, Vol. 82, No. 2, April 2002, pp. 429-472; 10.1152/physrev.00001.2002.
Copyright ©2002 by the American Physiological Society
Department of Physiology and the Kühne Minerva Center for Studies of Visual Transduction, The Hebrew University-Hadassah Medical School, Jerusalem, Israel
Minke, Baruch and
Boaz Cook.
TRP Channel Proteins and Signal
Transduction. Physiol. Rev. 82: 429-472, 2002.
TRP channel proteins constitute a large
and diverse family of proteins that are expressed in many tissues and
cell types. This family was designated TRP because of a spontaneously
occurring Drosophila mutant lacking TRP that responded to a
continuous light with a transient receptor potential (hence TRP). In
addition to responses to light, TRPs mediate responses to nerve growth
factor, pheromones, olfaction, mechanical, chemical, temperature, pH, osmolarity, vasorelaxation of blood vessels, and metabolic stress. Furthermore, mutations in several members of TRP-related channel proteins are responsible for several diseases, such as several tumors
and neurodegenerative disorders. TRP-related channel proteins are
found in a variety of organisms, tissues, and cell types, including
nonexcitable, smooth muscle, and neuronal cells. The large functional
diversity of TRPs is also reflected in their diverse permeability to
ions, although, in general, they are classified as nonselective
cationic channels. The molecular domains that are conserved in all
members of the TRP family constitute parts of the transmembrane
domains and in most members also the ankyrin-like repeats at the
NH2 terminal of the protein and a "TRP domain" at the
COOH terminal, which is a highly conserved 25-amino acid stretch with
still unknown function. All of the above features suggest that members
of the TRP family are "special assignment" channels, which are
recruited to diverse signaling pathways. The channels' roles and
characteristics such as gating mechanism, regulation, and permeability
are determined by evolution according to the specific functional requirements.
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