PIP2 and PIP3 interact with N-terminus region of TRPM4 channel.
作者： Kristyna Bousova , Michaela Jirku , Ladislav Bumba , Lucie Bednarova , Miroslav Sulc
DOI: 10.1016/J.BPC.2015.06.004
关键词: Chemistry 、 Biophysics 、 Transient receptor potential channel 、 Biochemistry 、 TRPC1 、 Neurotransmission 、 Receptor 、 Ion channel 、 Binding site 、 Binding selectivity 、 Cardiac conduction
摘要: Abstract The transient receptor potential melastatin 4 (TRPM4) is a calcium-activated non-selective ion channel broadly expressed in variety of tissues. Receptor has been identified as crucial modulator numerous calcium dependent mechanisms the cell such immune response, cardiac conduction, neurotransmission and insulin secretion. It known that phosphoinositide lipids (PIPs) play unique role regulation TRP function. However molecular mechanism this process still unknown. We characterized binding site PIP2 its structural analogue PIP3 E733–W772 proximal region TRPM4 N-terminus via biophysical modeling methods. specific positions R755 R767 domain were being important for interactions with PIP2/PIP3 ligands. Their mutations caused partial loss specificity. interaction channels never described before. These findings provide new insight into ligand domains channel.
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