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lüll Direct interaction with Rab11a targets the epithelial Ca2+ channels TRPV5 and TRPV6 to the plasma membrane van de Graaf SF; Chang Q; Mensenkamp AR; Hoenderop JG; Bindels RJMol Cell Biol 2006[Jan]; 26 (1): 303-12TRPV5 and TRPV6 are the most Ca2+-selective members of the transient receptor potential (TRP) family of cation channels and play a pivotal role in the maintenance of Ca2+ balance in the body. However, little is known about the mechanisms controlling the plasma membrane abundance of these channels to regulate epithelial Ca2+ transport. In this study, we demonstrated the direct and specific interaction of GDP-bound Rab11a with TRPV5 and TRPV6. Rab11a colocalized with TRPV5 and TRPV6 in vesicular structures underlying the apical plasma membrane of Ca2+-transporting epithelial cells. This GTPase recognized a conserved stretch in the carboxyl terminus of TRPV5 that is essential for channel trafficking. Furthermore, coexpression of GDP-locked Rab11a with TRPV5 or TRPV6 resulted in significantly decreased Ca2+ uptake, caused by diminished channel cell surface expression. Together, our data demonstrated the important role of Rab11a in the trafficking of TRPV5 and TRPV6. Rab11a exerts this function in a novel fashion, since it operates via direct cargo interaction while in the GDP-bound configuration.|Amino Acid Sequence[MESH]|Animals[MESH]|Calcium Channels/analysis/genetics/*metabolism[MESH]|Calcium/metabolism[MESH]|Cell Membrane/chemistry/*metabolism[MESH]|Cytoplasmic Vesicles/chemistry[MESH]|Epithelial Cells/metabolism[MESH]|Guanosine Diphosphate/metabolism[MESH]|Humans[MESH]|Mice[MESH]|Molecular Sequence Data[MESH]|Mutation[MESH]|Protein Interaction Mapping[MESH]|Protein Transport[MESH]|TRPV Cation Channels/analysis/genetics/*metabolism[MESH]|rab GTP-Binding Proteins/analysis/*metabolism[MESH] |