Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-2-12
pubmed:abstractText
Formin family proteins act as processive cappers of actin filaments, and determine the dynamics of a number of intracellular processes that are based on actin polymerization. The rate of filament growth upon processive capping varies within a broad range depending on the formin type and presence of profilin. While FH2 domains of various formins slow down polymerization by different extents, the FH1-FH2 domains in conjunction with profilin accelerate the reaction. Study of the physical mechanism of processive capping is vital for understanding the intracellular actin dynamics. We propose a model predicting that variation of a single physical parameter-the effective elastic energy of the formin-capped barbed end-results in the observed diversity of the polymerization rates. The model accounts for the whole range of the experimental results including the drastic slowing down of polymerization by FH2 of Cdc12 formin and the 4.5-fold acceleration of the reaction by FH1-FH2 of mDai1 formin in the presence of profilin. Fitting the theoretical predictions to the experimental curves provides the values of the effective elastic energies of different formin-barbed end complexes.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-11402062, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-11696322, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-11740491, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-11875440, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-12052901, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-12525176, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-12600310, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-12888296, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-14561409, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-14647292, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15030751, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15037312, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15501440, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15507212, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15556992, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15596547, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15635372, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15668168, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15743909, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15908944, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15950879, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-15994886, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-16157699, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-16364624, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-16439214, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-16461277, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-16483928, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-3790531, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-5775699, http://linkedlifedata.com/resource/pubmed/commentcorrection/17158576-9105045
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1542-0086
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1512-21
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Actin polymerization upon processive capping by formin: a model for slowing and acceleration.
pubmed:affiliation
Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't