Ca2+-dependent regulation and binding of calmodulin to multiple sites of Transient Receptor Potential Melastatin 3 (TRPM3) ion channels

Cell Calcium ◽  
2018 ◽  
Vol 73 ◽  
pp. 40-52 ◽  
Author(s):  
Julia Przibilla ◽  
Sandeep Dembla ◽  
Oleksandr Rizun ◽  
Annette Lis ◽  
Martin Jung ◽  
...  
Keyword(s):  
Ion Channels ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Transient Receptor Potential Melastatin ◽  
Transient Receptor

scholarly journals Alternative Splicing of a Protein Domain Indispensable for Function of Transient Receptor Potential Melastatin 3 (TRPM3) Ion Channels

2012 ◽  
Vol 287 (44) ◽  
pp. 36663-36672 ◽  
Author(s):  
Julia Frühwald ◽  
Julia Camacho Londoño ◽  
Sandeep Dembla ◽  
Stefanie Mannebach ◽  
Annette Lis ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Ion Channels ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Protein Domain ◽  
Transient Receptor Potential Melastatin ◽  
Transient Receptor

scholarly journals Scalaradial Is a Potent Inhibitor of Transient Receptor Potential Melastatin 2 (TRPM2) Ion Channels

2017 ◽  
Vol 80 (10) ◽  
pp. 2741-2750 ◽  
Author(s):  
John G. Starkus ◽  
Peter Poerzgen ◽  
Kristine Layugan ◽  
Kelly Galbraith Kawabata ◽  
Jun-Ichi Goto ◽  
...  
Keyword(s):  
Ion Channels ◽  
Transient Receptor Potential ◽  
Potent Inhibitor ◽  
Receptor Potential ◽  
Transient Receptor Potential Melastatin ◽  
Transient Receptor

TRPM3, a biophysical enigma?

2007 ◽  
Vol 35 (1) ◽  
pp. 89-90 ◽  
Author(s):  
J. Oberwinkler
Keyword(s):  
Alternative Splicing ◽  
Ion Channels ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Sodium Concentration ◽  
Pore Region ◽  
Bivalent Cations ◽  
Transient Receptor Potential Melastatin ◽  
Ion Conducting ◽  
Transient Receptor

TRPM3 [TRP (transient receptor potential) melastatin 3] is one of the least investigated proteins of the TRP family of ion channels. Heterologously expressed TRPM3 channels are constitutively active, have an outwardly rectifying current–voltage relationship and are inhibited by intracellular Mg2+ ions. Besides these rather common features, in which TRPM3 channels resemble the closely related channels TRPM6 and TRPM7, TRPM3 channels have several unique characteristics. The TRPM3 gene encodes a plethora of different proteins owing to alternative splicing and alternative exon usage. One site of alternative splicing affects the ion-conducting pore region and profoundly alters the pore properties of the encoded channels. The channels having the longer pore region efficiently conduct univalent cations, but are only poorly permeated by bivalent cations. Conversely, the channels with the shorter pore region are highly permeable to bivalent cations. Unusually, the short-pore TRPM3 channels are inhibited by extracellular Na+ ions. At physiological sodium concentration, this block is very strong, making it difficult to envision a physiological function for these ion channels. Recently, pharmacological investigations have been initiated in order to identify substances that influence TRPM3 channel activity. With the use of such substances, it might be possible to identify TRPM3 channels in their native environment and to elucidate some of their physiological roles. Hopefully, TRPM3 channels will then no longer appear to be as enigmatic as they do right now.

scholarly journals The G protein-biased PZM21 and TRV130 act as partial agonists of μ-opioid receptors signaling to ion channel targets

2018 ◽  
Author(s):  
Yevgen Yudin ◽  
Tibor Rohacs
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
G Protein ◽  
Opioid Receptors ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Partial Agonists ◽  
Transient Receptor Potential Melastatin ◽  
Transient Receptor ◽  
Μ Opioid Receptors

Opioids exert many of their acute effects through modulating ion channels via Gβγ subunits. Some of their side effects are attributed to β-arrestin recruitment, and several biased agonists that do not activate this pathway have been developed recently. Here we tested the effects of TRV130, PZM21 and herkinorin, three G-protein biased agonists of μ-opioid receptors (μOR), on ion channel targets. Compared to the full μOR agonist DAMGO, all three biased agonists induced smaller activation of G protein-coupled inwardly rectifying potassium channels (GIRK2), and smaller inhibition of Transient Receptor Potential Melastatin (TRPM3) channels. Furthermore, co-application of TRV130 or PZM21, but not herkinorin reduced the effects of DAMGO on both ion channels. CaV2.2 was also inhibited less by PZM21 and TRV130 than by DAMGO. TRV130, PZM21 and herkinorin were also less effective than DAMGO in inducing dissociation of the Gαi /Gβγ complex. We conclude that TRV130, PZM21 are partial agonists of μOR.

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