%0 Journal Article %1 Catt_2000_521 %A Catterall, W. A. %D 2000 %J Annu. Rev. Cell. Dev. Biol. %K 11031246 Animals, Calcium Calcium, Channels, Electrophysiology, Fluid, GTP-Binding Humans, Intracellular Phosphorylation, Proteins, %P 521-55 %R 10.1146/annurev.cellbio.16.1.521 %T Structure and regulation of voltage-gated Ca$^2+$ channels. %U http://dx.doi.org/10.1146/annurev.cellbio.16.1.521 %V 16 %X 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.

@article{Catt_2000_521, abstract = {Voltage-gated {C}a$^{2+}$ channels mediate {C}a$^{2+}$ entry into cells in response to membrane depolarization. Electrophysiological studies reveal different {C}a$^{2+}$ currents designated L-, N-, P-, Q-, R-, and T-type. The high-voltage-activated {C}a$^{2+}$ 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 {C}a$^{2+}$ 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 {C}a$^{2+}$ 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 {C}a$^{2+}$ currents, which are activated and inactivated more rapidly and at more negative membrane potentials than other {C}a$^{2+}$ current types. The distinct structures and patterns of regulation of these three families of {C}a$^{2+}$ channels provide a flexible array of {C}a$^{2+}$ entry pathways in response to changes in membrane potential and a range of possibilities for regulation of {C}a$^{2+}$ entry by second messenger pathways and interacting proteins.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Catterall, W. A.}, biburl = {https://www.bibsonomy.org/bibtex/20f61ab415f9ef3c4544832d7a2c83f53/hake}, description = {The whole bibliography file I use.}, doi = {10.1146/annurev.cellbio.16.1.521}, file = {Catt_2000_521.pdf:Catt_2000_521.pdf:PDF}, interhash = {503802ad83d98e77e8b82545e06b09b1}, intrahash = {0f61ab415f9ef3c4544832d7a2c83f53}, journal = {Annu. Rev. Cell. Dev. Biol.}, key = 7, keywords = {11031246 Animals, Calcium Calcium, Channels, Electrophysiology, Fluid, GTP-Binding Humans, Intracellular Phosphorylation, Proteins,}, owner = {hake}, pages = {521-55}, pii = {16/1/521}, timestamp = {2009-06-03T11:21:08.000+0200}, title = {Structure and regulation of voltage-gated {C}a$^{2+}$ channels.}, url = {http://dx.doi.org/10.1146/annurev.cellbio.16.1.521}, volume = 16, year = 2000 }