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Papers In Press, published online ahead of print April 20, 2006
Otolaryngology and Molecular & Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5739
Corresponding Author: hellers{at}stanford.edu
TRPV4 is a cation channel that responds to a variety of stimuli including mechanical forces, temperature, and ligand binding. We set out to identify TRPV4-interacting proteins by performing yeast two-hybrid screens and we isolated with the avian TRPV4 amino-terminus the chicken orthologues of mammalian PACSINs 1 and 3. The PACSINs are a protein family consisting of three members that have been implicated in synaptic vesicular membrane trafficking and regulation of dynamin-mediated endocytotic processes. In biochemical interaction assays we found that all three murine PACSIN isoforms can bind to the amino-terminus of rodent TRPV4. No member of the PACSIN protein family was able to biochemically interact with TRPV1 and TRPV2. Co-expression of PACSIN 3, but not PACSINs 1 and 2, shifted the ratio of plasma membrane-associated versus cytosolic TRPV4 toward an apparent increase of plasma membrane-associated TRPV4 protein. A similar shift was also observable when we blocked dynamin-mediated endocytotic processes, suggesting that PACSIN 3 specifically affects TRPV4’s endocytosis, thereby modulating the ion channel’s subcellular localization. Mutational analysis shows that the interaction of the two proteins requires both a TRPV4-specific proline-rich domain upstream of the channel’s ankyrin repeats and the carboxyl-terminal Src-homology 3 (SH3) domain of PACSIN 3. Such a functional interaction could be important in cell types that show distribution of both proteins to the same subcellular regions such as renal tubule cells where the proteins are associated with the luminal plasma membrane.
J. Biol. Chem, 10.1074/jbc.M602452200
Submitted on March 15, 2006
Revised on April 17, 2006
Accepted on April 20, 2006
PACSINs bind to the TRPV4 cation channel: PACSIN 3 modulates the subcellular localization of TRPV4
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