Abstract:
:TRPV5 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.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
van de Graaf SF,Chang Q,Mensenkamp AR,Hoenderop JG,Bindels RJdoi
10.1128/MCB.26.1.303-312.2006subject
Has Abstractpub_date
2006-01-01 00:00:00pages
303-12issue
1eissn
0270-7306issn
1098-5549pii
26/1/303journal_volume
26pub_type
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