Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2004-8-12
pubmed:abstractText
A feature shared between Drosophila rhodopsin and nearly all other G protein-coupled receptors is agonist-dependent protein phosphorylation. Despite extensive analyses of Drosophila phototransduction, the identity and function of the rhodopsin kinase (RK) have been elusive. Here, we provide evidence that G protein-coupled receptor kinase 1 (GPRK1), which is most similar to the beta-adrenergic receptor kinases, G protein-coupled receptor kinase 2 (GRK2) and GRK3, is the fly RK. We show that GPRK1 is enriched in photoreceptor cells, associates with the major Drosophila rhodopsin, Rh1, and phosphorylates the receptor. As is the case with mammalian GRK2 and GRK3, Drosophila GPRK1 includes a C-terminal pleckstrin homology domain, which binds to phosphoinositides and the Gbetagamma subunit. To address the role of GPRK1, we generated transgenic flies that expressed higher and lower levels of RK activity. Those flies with depressed levels of RK activity displayed a light response with a much larger amplitude than WT. Conversely, the amplitude of the light response was greatly suppressed in transgenic flies expressing abnormally high levels of RK activity. These data point to an evolutionarily conserved role for GPRK1 in modulating the amplitude of the visual response.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-10097103, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-10339543, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-10567430, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-10611962, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-10624964, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-10704496, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-11086989, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-11086990, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-11150735, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-11713293, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-11754840, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-11852136, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-12488531, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-12718862, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-12742390, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-12848937, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-12881416, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-1316807, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-1425685, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-14963491, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-1662381, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-3133115, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-7827093, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-8175732, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-8365418, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-9047319, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-9325250, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-9419375, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-9516442, http://linkedlifedata.com/resource/pubmed/commentcorrection/15289614-9667002
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
101
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11874-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Rhodopsin kinase activity modulates the amplitude of the visual response in Drosophila.
pubmed:affiliation
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.