Faculty Opinions recommendation of The role of the TRP channel NompC in Drosophila larval and adult locomotion.

Author(s):  
Andy Groves
Keyword(s):  
2006 ◽  
Vol 290 (6) ◽  
pp. F1295-F1302 ◽  
Author(s):  
Stan F. J. van de Graaf ◽  
Joost G. J. Hoenderop ◽  
René J. M. Bindels

The epithelial Ca2+ channels TRPV5 and TRPV6 are the most Ca2+-selective members of the TRP channel superfamily. These channels are the prime target for hormonal control of the active Ca2+ flux from the urine space or intestinal lumen to the blood compartment. Insight into their regulation is, therefore, pivotal in our understanding of the (patho)physiology of Ca2+ homeostasis. The recent elucidation of TRPV5/6-associated proteins has provided new insight into the molecular mechanisms underlying the regulation of these channels. In this review, we describe the various means of TRPV5/6 regulation, the role of channel-associated proteins herein, and the relationship between both processes.


2016 ◽  
Vol 15 (3) ◽  
pp. e276
Author(s):  
S. Kajioka ◽  
M. Hayashi ◽  
T. Maki ◽  
R. Takahashi ◽  
M. Etoh

2019 ◽  
Vol 58 ◽  
pp. 314-323 ◽  
Author(s):  
Lejla Zubcevic ◽  
Seok-Yong Lee
Keyword(s):  

Physiology ◽  
2011 ◽  
Vol 26 (1) ◽  
pp. 14-22 ◽  
Author(s):  
Ken Abe ◽  
Rosa Puertollano

Some members of the transient receptor potential (TRP) channel superfamily have proved to be essential in maintaining adequate ion homeostasis, signaling, and membrane trafficking in the endosomal pathway. The unique properties of the TRP channels confer cells the ability to integrate cytosolic and intraluminal stimuli and allow maintained and regulated release of Ca2+ from endosomes and lysosomes.


2013 ◽  
Vol 6 (1) ◽  
pp. 10-22 ◽  
Author(s):  
Mahendra Bishnoi ◽  
Louis S. Premkumar

Over the last fifteen years after the successful cloning of the first nociceptive Transient Receptor Potential (TRP) channel, TRP Vanilloid 1, other members of the TRP channel family have been cloned, characterized and implicated in different modalities of pain. Tremendous progress has been made with regard to the specific role of these TRP channels in nociception using electrophysiological and molecular methods, along with behavioral models combined with gene disruption techniques. This review summarizes the evidence supporting the role of TRP channels (TRP Vanilloid 1, TRP Vanilloid 2, TRP Vanilloid 3, TRP Vanilloid 4, TRP Ankyrin 1, TRP Melastatin 2, TRP Melastatin 3, TRP Melastatin 8, TRP Mucolipin 3 and TRP Canonical 1, 6) involved in nociception. The review also highlights the current status and future avenues for developing TRP channel modulators as analgesic agents.


2019 ◽  
Author(s):  
Gregory E. Miner ◽  
Katherine D. Sullivan ◽  
Annie Guo ◽  
Matthew L. Starr ◽  
EZ C. Ellis ◽  
...  

ABSTRACTThe transport of Ca2+ across membranes precedes the fusion and fission of various lipid bilayers. Yeast vacuoles during hyperosmotic shock become fragmented through fission events that require Ca2+ efflux of their luminal stores through the TRP channel Yvc1. This requires the production of the lipid PI(3,5)P2 by Fab1. Ca2+ is also released during vacuole fusion upon trans-SNARE complex assembly, however, the role of PI(3,5)P2 remains unclear. Here we demonstrate that elevated PI(3,5)P2 levels abolish Ca2+ efflux during fusion, indicating that PI(3,5)P2 has opposing effects on Ca2+ transport in fission versus fusion. Notably, Ca2+ efflux was enhanced when PI(3,5)P2 levels were reduced. Importantly, the effect of PI(3,5)P2 on Ca2+ flux was independent of Yvc1. Rather, the effect was dependent on the Ca2+ pump Pmc1. Vacuoles lacking Pmc1 were resistant to the effects of PI(3,5)P2, while those lacking Yvc1 remained sensitive. Furthermore altering PI(3,5)P2 levels affects the interactions of Pmc1 with the Vo component Vph1 and the R-SNARE Nyv1. We now propose a model in which elevated PI(3,5)P2 activates continued Pmc1 function to prevent the accumulation of released extraluminal Ca2+.SummaryDuring osmotic stress PI(3,5)P2 triggers Ca2+ release from vacuoles. Here we show PI(3,5)P2 stimulates Ca2+ uptake by vacuoles during fusion, illustrating that it has a dual role in Ca2+ transport.


Neuron ◽  
2010 ◽  
Vol 67 (3) ◽  
pp. 373-380 ◽  
Author(s):  
Li E. Cheng ◽  
Wei Song ◽  
Loren L. Looger ◽  
Lily Yeh Jan ◽  
Yuh Nung Jan
Keyword(s):  

2017 ◽  
Vol 130 (4) ◽  
pp. 735-744 ◽  
Author(s):  
Anke Di ◽  
Tomohiro Kiya ◽  
Haixia Gong ◽  
Xiaopei Gao ◽  
Asrar B. Malik

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