Sodium-coupled monocarboxylate transporter 1 interacts with the RING finger- and PDZ domain-containing protein PDZRN3

The journal of physiological sciences

article

Yusuke Otsuka¹  Tomomi Furihata¹  Kiyoshi Nakagawa¹  Yuta Ohno¹  Yoshie Reien¹  Motoshi Ouchi²  Hidefumi Wakashin¹  Shuichi Tsuruoka³  Naohiko Anzai¹ 

[1] Department of Pharmacology, Chiba University Graduate School of Medicine;Department of Pharmacology and Toxicology, Dokkyo Medical University School of Medicine;Department of Nephrology, Graduate School of Medicine, Nippon Medical School

关键词: SMCT1;    PDZRN3;    Monocarboxylate;    Transporter;    PDZ protein;   

DOI  :  10.1007/s12576-019-00681-w

来源: Springer

【 摘 要 】

Sodium-coupled monocarboxylate transporter SMCT1 (SLC5A8) mediates monocarboxylate transport in the proximal tubule of the kidney. We have identified PDZK1 and PDZ domain-containing RING finger 3 (PDZRN3) as potent binding partners of SMCT1, which has a PDZ motif (Thr–Arg–Leu), by yeast two-hybrid screening and revealed that PDZK1 enhances the transport activity of SMCT1. In this study, we aimed to characterize the interaction between SMCT1 and PDZRN3 as well as to examine how PDZRN3 regulates SMCT1 function. An interaction between SMCT1 and PDZRN3 through the PDZ motif was observed in a co-immunoprecipitation assay and yeast two-hybrid assay. A transport assay showed that PDZRN3 abolished the enhancing effect of PDZK1 on nicotinate uptake via SMCT1. Our results suggest that SMCT1 interacts with PDZRN3 and that PDZRN3 may regulate SMCT1 function by interfering with the interaction between SMCT1 and PDZK1.

【 授权许可】

Unknown