2005
DOI: 10.1074/jbc.m411089200
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Regulation of the Ca2+ Sensitivity of the Nonselective Cation Channel TRPM4

Abstract: TRPM4, a Ca2؉ -activated cation channel of the transient receptor potential superfamily, undergoes a fast desensitization to Ca 2؉ . The mechanisms underlying the alterations in Ca 2؉ sensitivity are unknown. Here we show that cytoplasmic ATP reversed Ca 2؉ sensitivity after desensitization, whereas mutations to putative ATP binding sites resulted in faster and more complete desensitization. Phorbol ester-induced activation of protein kinase C (PKC) increased the Ca 2؉ sensitivity of wildtype TRPM4 but not of … Show more

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Cited by 252 publications
(314 citation statements)
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“…Only TRPM4 is expressed in BMMCs, and the lack of TRPM4 in Trpm4 -/-mast cells was not compensated for by upregulation of TRPM5 expression. The properties of the endogenous CAN channel in BMMCs described here are very similar to the properties of TRPM4 currents recorded after overexpression of Trpm4 cDNA in HEK293 cells 16,17,24,36 . Both currents had identical permeability profiles and had similar single-channel conductance.…”
Section: Discussionsupporting
confidence: 56%
“…Only TRPM4 is expressed in BMMCs, and the lack of TRPM4 in Trpm4 -/-mast cells was not compensated for by upregulation of TRPM5 expression. The properties of the endogenous CAN channel in BMMCs described here are very similar to the properties of TRPM4 currents recorded after overexpression of Trpm4 cDNA in HEK293 cells 16,17,24,36 . Both currents had identical permeability profiles and had similar single-channel conductance.…”
Section: Discussionsupporting
confidence: 56%
“…The previously proposed modulation sites for phosphorylation, PtdInsP 2 binding or calmodulin binding at the C-terminal domain do not appear to be accessible based on the structure 14,16 . However, the structural feature of the C-terminal domain would imply that the coiled coil is capable of undergoing an up-and-down sliding motion, which, in turn, can induce lateral movement through the stretcher helices and propagate to the channel transmembrane pore through the middle tier LHD (Fig.…”
Section: Resultsmentioning
confidence: 86%
“…The 400-residue NBD, hypothesized to be the ATP binding site 16 , is an α/β protein with a central β-sheet formed by nine predominantly parallel β-strands (β3-β11) and its overall architecture partially resembles the Rossmann-fold dinucleotide binding proteins (Fig. 2a).…”
Section: Resultsmentioning
confidence: 99%
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