Linked Life Data

20959621

Source:http://linkedlifedata.com/resource/pubmed/id/20959621

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-10-20
pubmed:abstractText
Calcium regulates a wide spectrum of physiological processes such as heartbeat, muscle contraction, neuronal communication, hormone release, cell division, and gene transcription. Major entryways for Ca(2+) in excitable cells are high-voltage activated (HVA) Ca(2+) channels. These are plasma membrane proteins composed of several subunits, including ?(1), ?(2)?, ?, and ?. Although the principal ?(1) subunit (Ca(v)?(1)) contains the channel pore, gating machinery and most drug binding sites, the cytosolic auxiliary ? subunit (Ca(v)?) plays an essential role in regulating the surface expression and gating properties of HVA Ca(2+) channels. Ca(v)? is also crucial for the modulation of HVA Ca(2+) channels by G proteins, kinases, and the Ras-related RGK GTPases. New proteins have emerged in recent years that modulate HVA Ca(2+) channels by binding to Ca(v)?. There are also indications that Ca(v)? may carry out Ca(2+) channel-independent functions, including directly regulating gene transcription. All four subtypes of Ca(v)?, encoded by different genes, have a modular organization, consisting of three variable regions, a conserved guanylate kinase (GK) domain, and a conserved Src-homology 3 (SH3) domain, placing them into the membrane-associated guanylate kinase (MAGUK) protein family. Crystal structures of Ca(v)?s reveal how they interact with Ca(v)?(1), open new research avenues, and prompt new inquiries. In this article, we review the structure and various biological functions of Ca(v)?, with both a historical perspective as well as an emphasis on recent advances.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1522-1210
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1461-506
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The ß subunit of voltage-gated Ca2+ channels.
pubmed:affiliation
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural