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Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel

M. Jirku, L. Bumba, L. Bednarova, M. Kubala, M. Sulc, M. Franek, L. Vyklicky, J. Vondrasek, J. Teisinger, K. Bousova,

. 2015 ; 207 (-) : 135-42. [pub] 20151027

Language English Country Netherlands

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc16027991

Transient receptor potential melastatin-1 (TRPM1) is a calcium channel that is essential for the depolarization of photo-responsive retinal bipolar cells, but most of the physiological functions and cellular roles of this channel are still poorly understood. Most transient receptor potential (TRP) channels are typically regulated by intracellular proteins and other signaling molecules. Phosphatidylinositol-4,5 bisphosphate (PIP2), a minor phospholipid component of cell membranes, has previously been shown to directly bind TRP channels and to play a unique role in modulating receptor function. To characterize the binding of PIP2 as a potential regulator of TRPM1, we utilized biophysical methods and molecular modeling to study the interactions of PIP2 with an N-terminal fragment of TRPM1 (residues A451-N566). The basic N-terminal residue K464 of TRPM1 suggests that it is part of putative pleckstrin homology (PH) domain and is involved in the interactions with PIP2. This is the first report detailing the binding of PIP2 at the N-terminus of the TRPM1 receptor.

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$a Transient receptor potential melastatin-1 (TRPM1) is a calcium channel that is essential for the depolarization of photo-responsive retinal bipolar cells, but most of the physiological functions and cellular roles of this channel are still poorly understood. Most transient receptor potential (TRP) channels are typically regulated by intracellular proteins and other signaling molecules. Phosphatidylinositol-4,5 bisphosphate (PIP2), a minor phospholipid component of cell membranes, has previously been shown to directly bind TRP channels and to play a unique role in modulating receptor function. To characterize the binding of PIP2 as a potential regulator of TRPM1, we utilized biophysical methods and molecular modeling to study the interactions of PIP2 with an N-terminal fragment of TRPM1 (residues A451-N566). The basic N-terminal residue K464 of TRPM1 suggests that it is part of putative pleckstrin homology (PH) domain and is involved in the interactions with PIP2. This is the first report detailing the binding of PIP2 at the N-terminus of the TRPM1 receptor.
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$a Bumba, Ladislav $u Institute of Microbiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
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$a Bednarova, Lucie $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 16610 Prague, Czech Republic.
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$a Kubala, Martin $u Faculty of Science, Palacky University, 78341 Olomouc, Czech Republic.
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$a Sulc, Miroslav $u Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic; Institute of Microbiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
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$a Franek, Miloslav $u 3rd Faculty of Medicine, Charles University in Prague, 10000 Prague, Czech Republic.
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$a Vyklicky, Ladislav $u Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
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$a Vondrasek, Jiri $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 16610 Prague, Czech Republic.
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$a Teisinger, Jan $u Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
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$a Bousova, Kristyna $u Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic; 2nd Faculty of Medicine, Charles University in Prague, 15006 Prague, Czech Republic. Electronic address: kristyna.bousova@fgu.cas.cz.
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