Heteromerization of TRP channel subunits: extending functional diversity.
10.1007/s13238-010-0108-9
- Author:
Wei CHENG
1
;
Changsen SUN
;
Jie ZHENG
Author Information
1. Lab of Biomedical Optics, College of Physics and Optoelectronic Engineering, Dalian University of Technology, Dalian 116023, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Ankyrin Repeat;
Humans;
Models, Molecular;
Protein Interaction Domains and Motifs;
Protein Multimerization;
Protein Structure, Quaternary;
Protein Structure, Tertiary;
Protein Subunits;
TRPC Cation Channels;
chemistry;
genetics;
physiology
- From:
Protein & Cell
2010;1(9):802-810
- CountryChina
- Language:English
-
Abstract:
Transient receptor potential (TRP) channels are widely found throughout the animal kingdom. By serving as cellular sensors for a wide spectrum of physical and chemical stimuli, they play crucial physiological roles ranging from sensory transduction to cell cycle modulation. TRP channels are tetrameric protein complexes. While most TRP subunits can form functional homomeric channels, heteromerization of TRP channel subunits of either the same subfamily or different subfamilies has been widely observed. Heteromeric TRP channels exhibit many novel properties compared to their homomeric counterparts, indicating that co-assembly of TRP channel subunits has an important contribution to the diversity of TRP channel functions.
