• Je něco špatně v tomto záznamu ?

PIP2 and PIP3 interact with N-terminus region of TRPM4 channel

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

. 2015 ; 205 (-) : 24-32. [pub] 20150609

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc16020679

The transient receptor potential melastatin 4 (TRPM4) is a calcium-activated non-selective ion channel broadly expressed in a variety of tissues. Receptor has been identified as a crucial modulator of numerous calcium dependent mechanisms in the cell such as immune response, cardiac conduction, neurotransmission and insulin secretion. It is known that phosphoinositide lipids (PIPs) play a unique role in the regulation of TRP channel function. However the molecular mechanism of this process is still unknown. We characterized the binding site of PIP2 and its structural analogue PIP3 in the E733-W772 proximal region of the TRPM4 N-terminus via biophysical and molecular modeling methods. The specific positions R755 and R767 in this domain were identified as being important for interactions with PIP2/PIP3 ligands. Their mutations caused a partial loss of PIP2/PIP3 binding specificity. The interaction of PIP3 with TRPM4 channels has never been described before. These findings provide new insight into the ligand binding domains of the TRPM4 channel.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc16020679
003      
CZ-PrNML
005      
20160726092532.0
007      
ta
008      
160722s2015 ne f 000 0|eng||
009      
AR
024    7_
$a 10.1016/j.bpc.2015.06.004 $2 doi
024    7_
$a 10.1016/j.bpc.2015.06.004 $2 doi
035    __
$a (PubMed)26071843
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a ne
100    1_
$a Bousova, Kristyna $u 2nd Faculty of Medicine, Charles University in Prague, 15006 Prague, Czech Republic; Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
245    10
$a PIP2 and PIP3 interact with N-terminus region of TRPM4 channel / $c K. Bousova, M. Jirku, L. Bumba, L. Bednarova, M. Sulc, M. Franek, L. Vyklicky, J. Vondrasek, J. Teisinger,
520    9_
$a The transient receptor potential melastatin 4 (TRPM4) is a calcium-activated non-selective ion channel broadly expressed in a variety of tissues. Receptor has been identified as a crucial modulator of numerous calcium dependent mechanisms in the cell such as immune response, cardiac conduction, neurotransmission and insulin secretion. It is known that phosphoinositide lipids (PIPs) play a unique role in the regulation of TRP channel function. However the molecular mechanism of this process is still unknown. We characterized the binding site of PIP2 and its structural analogue PIP3 in the E733-W772 proximal region of the TRPM4 N-terminus via biophysical and molecular modeling methods. The specific positions R755 and R767 in this domain were identified as being important for interactions with PIP2/PIP3 ligands. Their mutations caused a partial loss of PIP2/PIP3 binding specificity. The interaction of PIP3 with TRPM4 channels has never been described before. These findings provide new insight into the ligand binding domains of the TRPM4 channel.
650    _2
$a sekvence aminokyselin $7 D000595
650    _2
$a dimyristoylfosfatidylcholin $x analogy a deriváty $x metabolismus $7 D004134
650    _2
$a lidé $7 D006801
650    _2
$a simulace molekulového dockingu $7 D062105
650    _2
$a molekulární sekvence - údaje $7 D008969
650    _2
$a peptidové fragmenty $x chemie $x metabolismus $7 D010446
650    _2
$a fosfatidylinositol-4,5-difosfát $x metabolismus $7 D019269
650    _2
$a vazba proteinů $7 D011485
650    _2
$a sekundární struktura proteinů $7 D017433
650    _2
$a kationtové kanály TRPM $x chemie $x metabolismus $7 D050053
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Jirku, Michaela $u Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic; Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic.
700    1_
$a Bumba, Ladislav $u Institute of Microbiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
700    1_
$a Bednarova, Lucie $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 16610 Prague, Czech Republic.
700    1_
$a Sulc, Miroslav $u Institute of Microbiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
700    1_
$a Franek, Miloslav $u 3rd Faculty of Medicine, Charles University in Prague, 10000 Prague, Czech Republic.
700    1_
$a Vyklicky, Ladislav $u Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
700    1_
$a Vondrasek, Jiri $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 16610 Prague, Czech Republic.
700    1_
$a Teisinger, Jan $u Institute of Physiology, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic. Electronic address: jan.teisinger@fgu.cas.cz.
773    0_
$w MED00000773 $t Biophysical chemistry $x 1873-4200 $g Roč. 205, č. - (2015), s. 24-32
856    41
$u https://pubmed.ncbi.nlm.nih.gov/26071843 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20160722 $b ABA008
991    __
$a 20160726092751 $b ABA008
999    __
$a ok $b bmc $g 1155349 $s 945207
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2015 $b 205 $c - $d 24-32 $e 20150609 $i 1873-4200 $m Biophysical chemistry $n Biophys Chem $x MED00000773
LZP    __
$a Pubmed-20160722

Najít záznam

Citační ukazatele

Možnosti archivace