Linked Life Data

21148312

Source:http://linkedlifedata.com/resource/pubmed/id/21148312

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2011-2-21
pubmed:abstractText
Mono-ADP-ribosylation is a reversible post-translational modification that can modulate the functions of target proteins. We have previously demonstrated that the ? subunit of heterotrimeric G proteins is endogenously mono-ADP-ribosylated, and once modified, the ?? dimer is inactive toward its effector enzymes. To better understand the physiological relevance of this post-translational modification, we have studied its hormonal regulation. Here, we report that G? subunit mono-ADP-ribosylation is differentially modulated by G protein-coupled receptors. In intact cells, hormone stimulation of the thrombin receptor induces G? subunit mono-ADP-ribosylation, which can affect G protein signaling. Conversely, hormone stimulation of the gonadotropin-releasing hormone receptor (GnRHR) inhibits G? subunit mono-ADP-ribosylation. We also provide the first demonstration that activation of the GnRHR can activate the ADP-ribosylation factor Arf6, which in turn inhibits G? subunit mono-ADP-ribosylation. Indeed, removal of Arf6 from purified plasma membranes results in loss of GnRHR-mediated inhibition of G? subunit mono-ADP-ribosylation, which is fully restored by re-addition of purified, myristoylated Arf6. We show that Arf6 acts as a competitive inhibitor of the endogenous ADP-ribosyltransferase and is itself modified by this enzyme. These data provide further understanding of the mechanisms that regulate endogenous ADP-ribosylation of the G? subunit, and they demonstrate a novel role for Arf6 in hormone regulation of G? subunit mono-ADP-ribosylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
286
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5995-6005
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Mono-ADP-ribosylation of the G protein betagamma dimer is modulated by hormones and inhibited by Arf6.
pubmed:affiliation
G Protein-mediated Signalling Laboratory, Consorzio Mario Negri Sud, Via Nazionale, 8/A 66030 Santa Maria Imbaro (Chieti), Italy. nadia.dani@ircc.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't