Qingyang Zhang, Jacob Clinton, Kristina Westerlund, Carsten Mim
{"title":"SMCT1 has a low affinity to PDZ domain containing 1 protein.","authors":"Qingyang Zhang, Jacob Clinton, Kristina Westerlund, Carsten Mim","doi":"10.17912/micropub.biology.001502","DOIUrl":null,"url":null,"abstract":"<p><p>Sodium-coupled monocarboxylate transporter 1 (SMCT1) is a membrane transporter abundantly expressed in colon, kidney, thyroid, brain; and silenced in cancer cells. It transports monocarboxylic acids with little specificity into cells. Based on pulldown experiments, it was proposed that the scaffolding protein PDZ Domain Containing 1 (PDZK1) regulates its surface expression and increases SMCT1's transportation efficiency. Here, we performed pull-down assays, Surface Plasmon Resonance (SPR), and Micro Scale Thermophoresis (MST) to evaluate the affinity between SMCT1 and two PDZ domains in PDZK1. Our results show that SMCT1 binds to these PDZ domains. However, the estimated equilibrium dissociation constants are higher than in canonical PDZ domains and likely physiological not relevant.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2025 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11883465/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"microPublication biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17912/micropub.biology.001502","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Sodium-coupled monocarboxylate transporter 1 (SMCT1) is a membrane transporter abundantly expressed in colon, kidney, thyroid, brain; and silenced in cancer cells. It transports monocarboxylic acids with little specificity into cells. Based on pulldown experiments, it was proposed that the scaffolding protein PDZ Domain Containing 1 (PDZK1) regulates its surface expression and increases SMCT1's transportation efficiency. Here, we performed pull-down assays, Surface Plasmon Resonance (SPR), and Micro Scale Thermophoresis (MST) to evaluate the affinity between SMCT1 and two PDZ domains in PDZK1. Our results show that SMCT1 binds to these PDZ domains. However, the estimated equilibrium dissociation constants are higher than in canonical PDZ domains and likely physiological not relevant.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
