DOD
Search
Discussions
Biomedical Jobmarket
News
DOD Alert
Edit DOD
 
ACCOUNT
Login
Register
Forgotten Password?
 
 
Structure and regulation of voltage-gated Ca2+ channels.
 
Diabetes OD > Diabetic Complications > Cardiovascular > Calcium > Calcium channel > Journal Article > Journal Article

(Journal Article): Structure and regulation of voltage-gated Ca2+ channels.
 
Catterall WA
 
IN: Annu Rev Cell Dev Biol 2000; 16(1):521-555
Impact Factor(s) of Annu Rev Cell Dev Biol: 23.69 (2005), 17.804 (2004), 22.638 (2003), 22.87 (2002), 27.106 (2001)

Fulltext:    HTML  PDF

ABSTRACT: Voltage-gated Ca(2+) channels mediate Ca(2+) entry into cells in response to membrane depolarization. Electrophysiological studies reveal different Ca(2+) currents designated L-, N-, P-, Q-, R-, and T-type. The high-voltage-activated Ca(2+) channels that have been characterized biochemically are complexes of a pore-forming alpha1 subunit of approximately 190-250 kDa; a transmembrane, disulfide-linked complex of alpha2 and delta subunits; an intracellular beta subunit; and in some cases a transmembrane gamma subunit. Ten alpha1 subunits, four alpha2delta complexes, four beta subunits, and two gamma subunits are known. The Cav1 family of alpha1 subunits conduct L-type Ca(2+) currents, which initiate muscle contraction, endocrine secretion, and gene transcription, and are regulated primarily by second messenger-activated protein phosphorylation pathways. The Cav2 family of alpha1 subunits conduct N-type, P/Q-type, and R-type Ca(2+) currents, which initiate rapid synaptic transmission and are regulated primarily by direct interaction with G proteins and SNARE proteins and secondarily by protein phosphorylation. The Cav3 family of alpha1 subunits conduct T-type Ca(2+) currents, which are activated and inactivated more rapidly and at more negative membrane potentials than other Ca(2+) current types. The distinct structures and patterns of regulation of these three families of Ca(2+) channels provide a flexible array of Ca(2+) entry pathways in response to changes in membrane potential and a range of possibilities for regulation of Ca(2+) entry by second messenger pathways and interacting proteins.

TYPE OF PUBLICATION: Review

Articles citing this article:



 
Respond on this Journal Article!
Hint: Your Response should directly apply to Structure and regulation of voltage-gated Ca2+ channels.. Please check, if this context applies best to your contribution. Otherwise click HERE to change to the appropriate subject area. The actual subject area is Journal Article.