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Updated: May 23, 2025

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
Published on: August 13, 2012
SMCT1 has a low affinity to PDZ domain containing 1 protein
Qingyang Zhang1,2, Jacob Clinton1, Kristina Westerlund1
1Department of Protein Science, KTH Royal Institute of Technology, Stockholm, Stockholm, Sweden.
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.
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