Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5666
pubmed:dateCreated
2004-3-26
pubmed:abstractText
mDia1, a Rho effector, belongs to the Formin family of proteins, which shares the conserved tandem FH1-FH2 unit structure. Formins including mDia1 accelerate actin nucleation while interacting with actin filament fast-growing ends. Here our single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells. The movement of mDia1 FH1-FH2 was blocked by actin-perturbing drugs, and the speed of mDia1 FH1-FH2 movement appeared to correlate with actin elongation rates. In vitro, mDia1 FH1-FH2 associated persistently with the growing actin barbed end. mDia1 probably moves processively along the growing end of actin filaments in cells, and Formins may be a molecular motility machinery that is independent from motor proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Bicyclo Compounds, Heterocyclic, http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin D, http://linkedlifedata.com/resource/pubmed/chemical/Depsipeptides, http://linkedlifedata.com/resource/pubmed/chemical/Diap1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Myosins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles, http://linkedlifedata.com/resource/pubmed/chemical/Thiazolidines, http://linkedlifedata.com/resource/pubmed/chemical/jasplakinolide, http://linkedlifedata.com/resource/pubmed/chemical/latrunculin B, http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
303
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2007-10
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15044801-Actin Cytoskeleton, pubmed-meshheading:15044801-Actins, pubmed-meshheading:15044801-Animals, pubmed-meshheading:15044801-Bicyclo Compounds, Heterocyclic, pubmed-meshheading:15044801-Biopolymers, pubmed-meshheading:15044801-Carrier Proteins, pubmed-meshheading:15044801-Cytochalasin D, pubmed-meshheading:15044801-Depsipeptides, pubmed-meshheading:15044801-Mice, pubmed-meshheading:15044801-Microtubules, pubmed-meshheading:15044801-Movement, pubmed-meshheading:15044801-Mutation, pubmed-meshheading:15044801-Myosins, pubmed-meshheading:15044801-Peptides, Cyclic, pubmed-meshheading:15044801-Recombinant Fusion Proteins, pubmed-meshheading:15044801-Thiazoles, pubmed-meshheading:15044801-Thiazolidines, pubmed-meshheading:15044801-Xenopus, pubmed-meshheading:15044801-rhoA GTP-Binding Protein
pubmed:year
2004
pubmed:articleTitle
Actin polymerization-driven molecular movement of mDia1 in living cells.
pubmed:affiliation
Department of Pharmacology, Kyoto University Faculty of Medicine, Yoshida Konoe-cho, Sakyo-ku, Kyoto, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't