Source:http://linkedlifedata.com/resource/pubmed/id/17623778
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 15
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pubmed:dateCreated |
2007-7-24
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pubmed:abstractText |
G-protein-coupled receptors (GPCRs) transduce the binding of extracellular stimuli into intracellular signalling cascades that can lead to morphological changes. Here, we demonstrate that stimulation of the calcium-sensing receptor (CaSR), a GPCR that promotes chemotaxis by detecting increases in extracellular calcium, triggers plasma membrane (PM) ruffling via a pathway that involves beta-arrestin 1, Arf nucleotide binding site opener (ARNO), ADP-ribosylating factor 6 (ARF6) and engulfment and cell motility protein (ELMO). Expression of dominant negative beta-arrestin 1 or its knockdown with siRNA impaired the CaSR-induced PM ruffling response. Expression of a catalytically inactive ARNO also reduced CaSR-induced PM ruffling. Furthermore, beta-arrestin 1 co-immunoprecipitated with the CaSR and ARNO under resting conditions. Agonist treatment did not markedly alter beta-arrestin 1 binding to the CaSR or to ARNO but it did elicit the translocation and colocalisation of the CaSR, beta-arrestin 1 and ARNO to membrane protrusions. Furthermore, ARF6 and ELMO, two proteins known to couple ARNO to the cytoskeleton, were required for CaSR-dependent morphological changes and translocated to the PM ruffles. These data suggest that cells ruffle upon CaSR stimulation via a mechanism that involves translocation of beta-arrestin 1 pre-assembled with the CaSR or ARNO, and that ELMO plays an essential role in this CaSR-signalling-induced cytoskeletal reorganisation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosylation factor 6,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Arrestins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/ELMO1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcium-Sensing,
http://linkedlifedata.com/resource/pubmed/chemical/beta-arrestin,
http://linkedlifedata.com/resource/pubmed/chemical/cytohesin-2
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
120
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2489-97
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pubmed:dateRevised |
2010-10-11
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pubmed:meshHeading |
pubmed-meshheading:17623778-ADP-Ribosylation Factors,
pubmed-meshheading:17623778-Actins,
pubmed-meshheading:17623778-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17623778-Arrestins,
pubmed-meshheading:17623778-Calcium,
pubmed-meshheading:17623778-Cell Line,
pubmed-meshheading:17623778-Cell Membrane,
pubmed-meshheading:17623778-Cell Movement,
pubmed-meshheading:17623778-Cell Shape,
pubmed-meshheading:17623778-GTPase-Activating Proteins,
pubmed-meshheading:17623778-Humans,
pubmed-meshheading:17623778-Receptors, Calcium-Sensing
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pubmed:year |
2007
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pubmed:articleTitle |
The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO ARF6 ELMO protein network.
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pubmed:affiliation |
Department of Anatomy, MRC Centre for Synaptic Plasticity, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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