Results 41 to 50 of about 1,352 (160)

N-terminal Tyrosine Residues within the Potassium Channel Kir3 Modulate GTPase Activity of Gαi [PDF]

Journal of Biological Chemistry, 2002
trkB activation results in tyrosine phosphorylation of N-terminal Kir3 residues, decreasing channel activation. To determine the mechanism of this effect, we reconstituted Kir3, trkB, and the mu opioid receptor in Xenopus oocytes. Activation of trkB by BDNF (brain-derived neurotrophic factor) accelerated Kir3 deactivation following termination of mu ...
Danielle L, Ippolito, Paul A, Temkin, Sherri L, Rogalski, Charles, Chavkin   +3 more
openaire   +2 more sources

Régulation du complexe constitutif formé par le récepteur opioïde delta et le canal potassique de la famille Kir3 [PDF]

, 2015
Les opioïdes sont les analgésiques les plus efficaces dans le traitement des douleurs sévères. Ils produisent leurs effets en ciblant spécifiquement les récepteurs opioïdes localisés tout le long de la voie de perception de la douleur où ils modulent la ...
Nagi, Karim
core   +2 more sources

Mass spectrometric analysis reveals a functionally important PKA phosphorylation site in a Kir3 channel subunit [PDF]

Pflügers Archiv - European Journal of Physiology, 2009
Phosphorylation of the Kir3 channel by cAMP-dependent protein kinase (PKA) potentiates activity and strengthens channel-PIP(2) interactions, whereas phosphorylation by protein kinase C (PKC) exerts the opposite effects (Keselman et al., Channels 1:113-123, 2007; Lopes et al., Channels 1:124-134, 2007).
Radda, Rusinova, Yu-Ming Albert, Shen, Georgia, Dolios, Julio, Padovan, Heyi, Yang, Madeleine, Kirchberger, Rong, Wang, Diomedes E, Logothetis   +7 more
openaire   +2 more sources

Tyrosine Phosphorylation of Kir3 following κ-Opioid Receptor Activation of p38 MAPK Causes Heterologous Desensitization [PDF]

Journal of Biological Chemistry, 2009
Prior studies showed that tyrosine 12 phosphorylation in the N-terminal, cytoplasmic domain of the G-protein-gated inwardly rectifying potassium channel, K(ir)3.1 facilitates channel deactivation by increasing intrinsic GTPase activity of the channel.
Cecilea C, Clayton, Mei, Xu, Charles, Chavkin   +2 more
openaire   +2 more sources

Diverse Trafficking Patterns Due to Multiple Traffic Motifs in G Protein-Activated Inwardly Rectifying Potassium Channels from Brain and Heart [PDF]

, 2002
G protein-activated inwardly rectifying potassium channels (Kir3, GIRK) provide an important mechanism for neurotransmitter regulation of membrane excitability. GIRK channels are tetramers containing various combinations of Kir3 subunits (Kir3.1–Kir3.4).
Ma, Dzwokai, Raab-Graham, Kimberly, Fried, Sharon R., Zerangue, Noa, Jan, Yuh Nung, Jan, Lily Yeh   +5 more
core   +1 more source

Inwardly rectifying potassium channels (KIR) in GtoPdb v.2021.3 [PDF]

, 2021
The 2TM domain family of K channels are also known as the inward-rectifier K channel family. This family includes the strong inward-rectifier K channels (Kir2.x) that are constitutively active, the G-protein-activated inward-rectifier K channels (Kir3.x)
Lazdunski, Michel, Tucker, Stephen, Yoshihiro Kubo, Jan, Lily Y., Colin G. Nichols, Kubo, Yoshihiro, Slesinger, Paul A., Lawrence G. Palmer, Atsushi Inanobe, Nichols, Colin G., Hiroshi Hibino, Clapham, David E, Stephen Tucker, Pearson, Wade L, Lily Y. Jan, Andreas Karschin, Adelman, John P, Karschin, Andreas, Paul A. Slesinger, Pearson, Wade L., Vandenberg, Carol A., Slesinger, Paul A, Michel Lazdunski, Adelman, John P., Miki, Takashi, Seino, Susumu, Nichols, Colin G, Palmer, Lawrence G., Wade L. Pearson, Palmer, Lawrence G, Jan, Lily Y, Inanobe, Atsushi, Kurachi, Yoshihisa, Henry Sackin, Carol A. Vandenberg, Yoshihisa Kurachi, Hibino, Hiroshi, Clapham, David E., Vandenberg, Carol A, David E. Clapham, Takashi Miki, Susumu Seino, Sackin, Henry, John P. Adelman   +43 more
core   +1 more source

Developmental regulation of G protein‐gated inwardly‐rectifying K⁺(GIRK/Kir3) channel subunits in the brain [PDF]

European Journal of Neuroscience, 2011
AbstractG protein‐gated inwardly‐rectifying K+(GIRK/family 3 of inwardly‐rectifying K+) channels are coupled to neurotransmitter action and can play important roles in modulating neuronal excitability. We investigated the temporal and spatial expression of GIRK1, GIRK2 and GIRK3 subunits in the developing and adult brain of mice and rats using ...
Fernández-Alacid, L, Watanabe, M, Molnar, E, Wickman, K, Luján, R   +4 more
openaire   +3 more sources

The cationic region of Rhes mediates its interactions with specific Gβ subunits [PDF]

, 2009
Ras homologue enriched in striatum (Rhes) is a small monomeric G protein which functions in a variety of cellular processes, including attenuation of G protein-coupled receptor (GPCR)signalling.
Ladds, Graham, Hill, Claire, Goddard, Alan, Davey, John   +3 more
core   +1 more source

Opening closed inward rectifier potassium channel doors

British Journal of Pharmacology, Volume 183, Issue 10, Page 2197-2218, May 2026.
Inwardly rectifying potassium (KIR) channels are essential regulators of membrane potential in excitable and non‐excitable tissues. Although KIR channels exhibit a biophysical preference for potassium influx due to voltage‐dependent block of outward current by polyamines and Mg2+, under physiological conditions, they predominantly mediate K+ efflux ...
Anna Stary‐Weinzinger, Fabian Kaiser, Marcel A. G. van der Heyden, Saïd Bendahhou   +3 more
wiley   +1 more source

The Na+-Activated Potassium Channel Slack Shares a Similar Na+ Coordination Site with Kir3 Channels [PDF]

Biophysical Journal, 2010
Characteristics of Na+ activated potassium channel (Slack or Slo2.2) currents, including high conductance, rundown, regulation by Na+, Cl- and phosphorylation have long been reported but underlying mechanisms remain unknown. Here we report identification of a sodium regulatory site in the RCK2 domain of Slack channels by screening the C-terminus with ...
Zhang, Zhe, Rosenhouse-Dantsker, Avia, Tang, Qiongyao, Noskov, Sergei, Logothetis, Diomedes E.   +4 more
openaire   +1 more source