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Functional and Dimerization-related Regions of Ostbeta


, : Functional and Dimerization-related Regions of Ostbeta.

The organic solute transporter, Ost/Slc51, is composed of two distinct proteins that must heterodimerize to generate transport activity, but the role of the individual subunits in mediating transport activity is unknown. The present study identified regions in Ost? required for heterodimerization with Ost?, trafficking of the Ost?-Ost? complex to the plasma membrane, and bile acid transport activity in HEK293 cells. Bimolecular fluorescence complementation analysis revealed that a 25-amino acid peptide containing the Ost? transmembrane (TM) domain heterodimerized with Ost?, although the resulting complex failed to reach the plasma membrane and generate cellular [3H]taurocholate transport activity. Deletion of the single TM domain of Ost? abolished interaction with Ost?, demonstrating that the TM segment is necessary and sufficient for formation of a heteromeric complex with Ost?. Mutation of the highly conserved tryptophan-asparagine sequence within the TM domain of Ost? to alanines did not prevent cell surface trafficking, but abolished transport activity. Removal of the N-terminal 27 amino acids of Ost? resulted in a transporter complex that reached the plasma membrane and exhibited transport activity at 3 C. Complete deletion of the C terminus of Ost? abolished [3H]taurocholate transport activity, but reinsertion of two native arginines immediately C-terminal to the TM domain rescued this defect. These positively charged residues establish the correct Nexo/Ccyt topology of the peptide, in accordance with the positive inside rule. Together, the results demonstrate that Ost? is required for both proper trafficking of Ost? and formation of the functional transport unit, and identify specific residues of Ost? critical for these processes.

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