Linked Life Data

16182515

Source:http://linkedlifedata.com/resource/pubmed/id/16182515

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-10-31
pubmed:abstractText
Many receptors for neurotransmitters and hormones rely upon members of the Gqalpha family of heterotrimeric G proteins to exert their actions on target cells. Galpha subunits of the Gq class of G proteins (Gqalpha, G11alpha, G14alpha and G15/16alpha) directly link receptors to activation of PLC-beta isoforms which, in turn, stimulate inositol lipid (i.e. calcium/PKC) signalling. Although Gqalpha family members share a capacity to activate PLC-beta, they also differ markedly in their biochemical properties and tissue distribution which predicts functional diversity. Nevertheless, established models suggest that Gqalpha family members are functionally redundant and that their cellular responses are a result of PLC-beta activation and downstream calcium/PKC signalling. Growing evidence, however, indicates that Gqalpha, G11alpha, G14alpha and G15/16alpha are functionally diverse and that many of their cellular actions are independent of inositol lipid signalling. Recent findings show that Gqalpha family members differ with regard to their linked receptors and downstream binding partners. Reported binding partners distinct from PLC-beta include novel candidate effector proteins, various regulatory proteins, and a growing list of scaffolding/adaptor proteins. Downstream of these signalling proteins, Gqalpha family members exhibit unexpected differences in the signalling pathways and the gene expression profiles they regulate. Finally, genetic studies using whole animal models demonstrate the importance of certain Gqalpha family members in cardiac, lung, brain and platelet functions among other physiological processes. Taken together, these findings demonstrate that Gqalpha, G11alpha, G14alpha and G15/16alpha regulate both overlapping and distinct signalling pathways, indicating that they are more functionally diverse than previously thought.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
135-50
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Cell signalling diversity of the Gqalpha family of heterotrimeric G proteins.
pubmed:affiliation
Department of Pharmacology, Emory University School of Medicine, 1510 Clifton Rd., Atlanta, GA 30322, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural