Negatively charged amino acids near and in transient receptor potential (TRP) domain of TRPM4 channel are one determinant of its Ca2+ sensitivity.

doi:10.1074/jbc.M114.606087

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Article

Negatively charged amino acids near and in transient receptor potential (TRP) domain of TRPM4 channel are one determinant of its Ca2+ sensitivity.

The Journal of biological chemistry - 19 Dec 2014

Yamaguchi Soichiro, Tanimoto Akira, Otsuguro Ken-ichi, Hibino Hiroshi, Ito Shigeo

Abstract excerpt

Transient receptor potential (TRP) channel melastatin subfamily member 4 (TRPM4) is a broadly expressed nonselective monovalent cation channel. TRPM4 is activated by membrane depolarization and intracellular Ca(2+), which is essential for the activation. The Ca(2+) sensitivity is known to be regulated by calmodulin and membrane phosphoinositides, such as phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). Although...

Topics

Animals
Aspartic Acid
Binding Sites
Calcium
Cations, Divalent
Cobalt
Glutamic Acid
HEK293 Cells
Humans
Male
Membrane Potentials

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Patch-Clamp Techniques

Phosphatidylinositol 4,5-Diphosphate

Rats, Inbred BN

TRPM Cation Channels

Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 25378404
DOI: 10.1074/jbc.M114.606087
PMCID: PMC4271215

Genes

TRPM4
TRPM2
TRPM5
TRPM8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Negatively charged amino acids near and in transient receptor potential (TRP) domain of TRPM4 channel are one determinant of its Ca2+ sensitivity.PMID 25378404Read ↗

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