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Acta Physiologica Congress

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Acta Physiologica 2007; Volume 189, Supplement 653
The 86th Annual Meeting of The German Physiological Society
3/25/2007-3/28/2007
Hannover, Germany


OLIGOMERIZATION OF HOCT2 STUDIED WITH THE SPLIT- UBIQUITIN MEMBRANE YEAST TWO-HYBRID TECHNIQUE
Abstract number: O11-2

Brast1 S, Schlatter1 E, Grefen1 C, Ciarimboli1 G

1Med. Klinik D, Exp. Nephrologie, Universittsklinikum Mnster

The human organic cation transporter 2 (hOCT2) is a multispecific transporter of the solute carrier family 22 (SLC22) which transports organic cations, including clinically used drugs. OCT2 shows the common structural features of the SLC22 family including intracellular COOH and NH2 termini, 12 transmembrane domains (TMD), multiple glycosylation and potential phosphorylation sites. Properties of hOCT2 have been extensively studied, however, there is no information about oligomerization. The aim of this work was to investigate whether hOCT2 is able to form oligomeric complexes. The split-ubiquitin membrane yeast two-hybrid technique (MbYTH), a special method to investigate interactions between membrane proteins within the plasma membrane in eukaryotic systems, was used. We demonstrate for the first time that hOCT2 is able to interact with itself in vivo and is able to form oligomeric comlexes. To determine which domain is responsible for this oligomerization, different truncated constructs of hOCT2 were tested with the MbYTH against the whole transporter. The presence of the TMD 1-4 resulted necessary for the truncated transporter to interact with whole hOCT2. Further investigations are necessary to determine the specific residues responsible for oligomerization, the number of hOCT2 units forming the oligomers, and whether hOCT2 monomer is functional. Supported by DFG Schl277/11-3.

To cite this abstract, please use the following information:
Acta Physiologica 2007; Volume 189, Supplement 653 :O11-2

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