Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Physiology
64 (2002), S. 289-311
ISSN:
0066-4278
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Medicine
,
Biology
Notes:
Abstract A surprising variety of ion channels found in a wide range of species from Homo to Paramecium use calmodulin (CaM) as their constitutive or dissociable Ca2+-sensing subunits. The list includes voltage-gated Ca2+ channels, various Ca2+- or ligand-gated channels, Trp family channels, and even the Ca2+-induced Ca2+ release channels from organelles. Our understanding of CaM chemistry and its relation to enzymes has been instructive in channel research, yet the intense study of CaM regulation of ion channels has also revealed unexpected CaM chemistry. The findings on CaM channel interactions have indicated the existence of secondary interaction sites in addition to the primary CaM-binding peptides and the functional differences between the N- and C-lobes of CaM. The study of CaM in channel biology will figure into our understanding on how this uniform, universal, vital, and ubiquitous Ca2+ decoder coordinates the myriad local and global cell physiological transients.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.physiol.64.100301.111649
Permalink
|
Location |
Call Number |
Expected |
Availability |
