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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-4-13
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pubmed:abstractText |
Recent research on F-actin capping proteins has concentrated on three main areas. The discovery that controlled actin polymerization is the driving force for intracellular movement suggests an important role for capping proteins in regulating filament number and length. A capping protein from Dictyostelium (related to heat-shock protein HSP70) has been characterized that is activated by external stimuli. This provides a pivotal connection between extracellular signalling, cytoskeletal reorganization and locomotory behaviour. The roles of individual actin-binding sites in the gelsolin family of severing/capping proteins and binding sites for phosphatidylinositol 4,5-bisphosphate have been identified.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0955-0674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
63-9
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:8383512-Actins,
pubmed-meshheading:8383512-Amino Acid Sequence,
pubmed-meshheading:8383512-Animals,
pubmed-meshheading:8383512-Binding Sites,
pubmed-meshheading:8383512-Cell Movement,
pubmed-meshheading:8383512-Fungal Proteins,
pubmed-meshheading:8383512-Kinetics,
pubmed-meshheading:8383512-Microfilament Proteins,
pubmed-meshheading:8383512-Molecular Sequence Data,
pubmed-meshheading:8383512-Molecular Structure,
pubmed-meshheading:8383512-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:8383512-Phosphatidylinositols,
pubmed-meshheading:8383512-Phosphorylation,
pubmed-meshheading:8383512-Polymers,
pubmed-meshheading:8383512-Protein Binding,
pubmed-meshheading:8383512-Signal Transduction
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pubmed:year |
1993
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pubmed:articleTitle |
F-actin capping proteins.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Review
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