Mapping of CaM, S100A1 and PIP2-Binding Epitopes in the Intracellular N- and C-Termini of TRPM4.

ABSTRACT: Molecular determinants of the binding of various endogenous modulators to transient receptor potential (TRP) channels are crucial for the understanding of necessary cellular pathways, as well as new paths for rational drug designs. The aim of this study was to characterise interactions between the TRP cation channel subfamily melastatin member 4 (TRPM4) and endogenous intracellular modulators-calcium-binding proteins (calmodulin (CaM) and S100A1) and phosphatidylinositol 4, 5-bisphosphate (PIP₂). We have found binding epitopes at the N- and C-termini of TRPM4 shared by CaM, S100A1 and PIP₂. The binding affinities of short peptides representing the binding epitopes of N- and C-termini were measured by means of fluorescence anisotropy (FA). The importance of representat

SUBMITTER: Bousova K 

PROVIDER: S-EPMC7352223 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature