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Functional expression of the epithelial Ca(2+) channels (TRPV5 and TRPV6) requires association of the S100A10-annexin 2 complex van de Graaf SF; Hoenderop JG; Gkika D; Lamers D; Prenen J; Rescher U; Gerke V; Staub O; Nilius B; Bindels RJEMBO J 2003[Apr]; 22 (7): 1478-87TRPV5 and TRPV6 constitute the Ca(2+) influx pathway in a variety of epithelial cells. Here, we identified S100A10 as the first auxiliary protein of these epithelial Ca(2+) channels using yeast two-hybrid and GST pull-down assays. This S100 protein forms a heterotetrameric complex with annexin 2 and associates specifically with the conserved sequence VATTV located in the C-terminal tail of TRPV5 and TRPV6. Of these five amino acids, the first threonine plays a crucial role since the corresponding mutants (TRPV5 T599A and TRPV6 T600A) exhibited a diminished capacity to bind S100A10, were redistributed to a subplasma membrane area and did not display channel activity. Using GST pull-down and co-immunoprecipitation assays we demonstrated that annexin 2 is part of the TRPV5-S100A10 complex. Furthermore, the S100A10-annexin 2 pair colocalizes with the Ca(2+) channels in TRPV5-expressing renal tubules and TRPV6-expressing duodenal cells. Importantly, downregulation of annexin 2 using annexin 2-specific small interfering RNA inhibited TRPV5 and TRPV6-mediated currents in transfected HEK293 cells. In conclusion, the S100A10-annexin 2 complex plays a crucial role in routing of TRPV5 and TRPV6 to plasma membrane.|*S100 Proteins[MESH]|Animals[MESH]|Annexin A2/metabolism[MESH]|Base Sequence[MESH]|Calcitriol/metabolism[MESH]|Calcium Channels/*metabolism[MESH]|Calcium-Binding Proteins/metabolism[MESH]|DNA Primers[MESH]|Epithelium/metabolism[MESH]|Gene Silencing[MESH]|Immunohistochemistry[MESH]|Mice[MESH]|Protein Binding[MESH]|RNA Interference[MESH]|Reverse Transcriptase Polymerase Chain Reaction[MESH]|Two-Hybrid System Techniques[MESH] |
