Document Detail


Residues in the pore region of Drosophila transient receptor potential A1 dictate sensitivity to thermal stimuli.
MedLine Citation:
PMID:  23027824     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The capacity to sense temperature is essential for the survival of all animals. At the molecular level, ion channels belonging to the transient receptor potential (TRP) family of channels function as temperature sensors in animals across several phyla. TRP channels are opened directly by changes in temperature and show pronounced sensitivity at their activation range. To determine how temperature activates these channels, we analysed channels belonging to the TRPA family, which detect heat in insects and cold in mammals. By constructing chimeric proteins consisting of human and Drosophila TRPA1 channels, we mapped regions that regulate thermal activation and identified residues in the pore helix that invert temperature sensitivity of TRPA1. From analysis of individual channels we defined the gating reaction of Drosophila TRPA1 and determined how mutagenesis alters the energy landscape for channel opening. Our results reveal specific molecular requirements for thermal activation of TRPA1 and provide mechanistic insight into this process.
Authors:
Hong Wang; Melanie Schupp; Sandra Zurborg; Paul A Heppenstall
Related Documents :
23865724 - Dynamics and thermodynamics of crystalline polymorphs. part 2: β-glycine, analysis of ...
18999774 - Fermi arcs in the superconducting clustered state for underdoped cuprate superconductors.
19405674 - Miniature diamond anvil cell for broad range of high pressure measurements.
20867054 - Formation of a three-dimensional network of v trimers in a2v13o22 (a=ba, sr).
10916104 - Effect of vitamin e-bonded membrane on the 8-hydroxy 2'-deoxyguanosine level in leukocy...
19399484 - Converting cold into pain.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-10-01
Journal Detail:
Title:  The Journal of physiology     Volume:  591     ISSN:  1469-7793     ISO Abbreviation:  J. Physiol. (Lond.)     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-02     Completed Date:  2013-06-13     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  0266262     Medline TA:  J Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  185-201     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Calcium Channels / chemistry,  physiology*
Drosophila
Drosophila Proteins / chemistry,  physiology*
Hot Temperature
Humans
Mutation
Nerve Tissue Proteins / chemistry,  physiology*
Porosity
TRPC Cation Channels / chemistry,  physiology*
Transient Receptor Potential Channels / chemistry,  physiology*
Chemical
Reg. No./Substance:
0/Calcium Channels; 0/Drosophila Proteins; 0/Nerve Tissue Proteins; 0/TRPA1 protein, human; 0/TRPC Cation Channels; 0/Transient Receptor Potential Channels; 0/TrpA1 protein, Drosophila
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The information content of physiological and epileptic brain activity.
Next Document:  Challenges for health psychology: Theorizing belief and beyond.