Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-5-19
pubmed:abstractText
Activation of Rho/Rac GTPases during cell signaling requires the participation of GDP/GTP exchange factors of the Dbl family. Although the structure of the catalytic core of Dbl proteins has been established recently, the molecular changes that the full-length proteins experience during normal or oncogenic conditions of stimulation are still unknown. Here, we have used single-particle electron microscopy to solve the structures of the inactive (unphosphorylated), active (phosphorylated), and constitutively active (N-terminally deleted) versions of the exchange factor Vav3. Comparison of these forms has revealed the interdomain interactions maintaining the inactive Vav3 state and the dynamic changes that the overall Vav3 structure undergoes upon tyrosine phosphorylation. We have also found that the conformations of phosphorylated Vav3 and N-terminally deleted Vav3 are distinct, indicating that the acquisition of constitutive activity by exchange factors is structurally more complex than the mere elimination of inhibitory interactions between structural domains.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-10077632, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-10523675, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-10600563, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-10669724, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-10669745, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-10748082, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11007481, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11130063, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11472090, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11718559, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11738596, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11779690, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11805146, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11889037, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-11911885, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-12094222, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-12228230, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-15465319, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-7716522, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-9150145, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-9308960, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-9438848, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-9790532, http://linkedlifedata.com/resource/pubmed/commentcorrection/15775967-9822605
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1330-40
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed-meshheading:15775967-Adaptor Proteins, Signal Transducing, pubmed-meshheading:15775967-Animals, pubmed-meshheading:15775967-Cell Cycle Proteins, pubmed-meshheading:15775967-Cells, Cultured, pubmed-meshheading:15775967-Chromatography, Affinity, pubmed-meshheading:15775967-Glutathione Transferase, pubmed-meshheading:15775967-Guanine Nucleotide Exchange Factors, pubmed-meshheading:15775967-Image Processing, Computer-Assisted, pubmed-meshheading:15775967-Mice, pubmed-meshheading:15775967-Microscopy, Electron, pubmed-meshheading:15775967-Models, Molecular, pubmed-meshheading:15775967-NIH 3T3 Cells, pubmed-meshheading:15775967-Phosphorylation, pubmed-meshheading:15775967-Protein Conformation, pubmed-meshheading:15775967-Proto-Oncogene Proteins, pubmed-meshheading:15775967-Proto-Oncogene Proteins c-vav, pubmed-meshheading:15775967-Spodoptera, pubmed-meshheading:15775967-Tyrosine
pubmed:year
2005
pubmed:articleTitle
Global conformational rearrangements during the activation of the GDP/GTP exchange factor Vav3.
pubmed:affiliation
Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural