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10.1042/BST0350105

http://scihub22266oqcxt.onion/10.1042/BST0350105
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17233613!?!17233613

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suck abstract from ncbi

pmid17233613      Biochem+Soc+Trans 2007 ; 35 (Pt 1): 105-8
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  • Regulation of TRP channels: a voltage-lipid connection #MMPMID17233613
  • Nilius B; Mahieu F; Karashima Y; Voets T
  • Biochem Soc Trans 2007[Feb]; 35 (Pt 1): 105-8 PMID17233613show ga
  • TRP (transient receptor potential) channels respond to a plethora of stimuli in a fine-tuned manner. We show here that both membrane potential and the level of PI (phosphatidylinositol) phosphates are efficient regulators of TRP channel gating. Recent work has shown that this regulation applies to several members of the TRPV (TRP vanilloid) subfamily (TRPV1 and TRPV5) and the TRPM (TRP melastatin) subfamily (TRPM4/TRPM5/TRPM7/TRPM8), whereas regulation of members of the TRPC subfamily is still disputed. The mechanism whereby PIP(2) (PI 4,5-bisphosphate) acts on TRPM4, a Ca(2+)- and voltage-activated channel, is shown in detail in this paper: (i) PIP(2) may bind directly to the channel, (ii) PIP(2) induces sensitization to activation by Ca(2+), and (iii) PIP(2) shifts the voltage dependence towards negative and physiologically more meaningful potentials. A PIP(2)-binding pocket seems to comprise a part of the TRP domain and especially pleckstrin homology domains in the C-terminus.
  • |Amino Acid Sequence[MESH]
  • |Animals[MESH]
  • |Calcium/metabolism[MESH]
  • |Cell Membrane/metabolism[MESH]
  • |Electrophysiology/methods[MESH]
  • |Humans[MESH]
  • |Lipids/*chemistry[MESH]
  • |Membrane Potentials[MESH]
  • |Models, Biological[MESH]
  • |Molecular Sequence Data[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |Sequence Homology, Amino Acid[MESH]
  • |TRPC Cation Channels/chemistry/*physiology[MESH]


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