| pubmed-article:2762319 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C0025979 | lld:lifeskim |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C0012120 | lld:lifeskim |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:2762319 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:2762319 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:2762319 | pubmed:dateCreated | 1989-9-19 | lld:pubmed |
| pubmed-article:2762319 | pubmed:abstractText | Because myosin thick filaments form in the actin-rich cortex of nonmuscle cells, we have examined the role of Dictyostelium actin filaments in the assembly of Dictyostelium myosin (type II). Fluorescence energy transfer and light-scattering assembly assays indicate that self-association of Dictyostelium myosin into bipolar thick filaments is kinetically regulated by actin filament networks. Regulation is nucleotide dependent but does not require ATP hydrolysis. Myosin assembly is accelerated approximately 5-fold by actin filaments when either 1 mM ATP or 1 mM adenosine 5'-[beta,gamma-imido]triphosphate (AMP-P[NH]P) is present. However, actin filaments together with 1 mM ADP abolish myosin assembly. Accelerated assembly appears to require transient binding of myosin molecules to actin filaments before incorporation into thick filaments. Fluorescence energy-transfer assays demonstrate that myosin associates with actin filaments at a rate that is equivalent to the accelerated myosin assembly rate, evidence that myosin to actin binding is a rate-limiting step in accelerated thick filament formation. Actin filament networks are also implicated in regulation of thick filament formation, since fragmentation of F-actin networks by severin causes immediate cessation of accelerated myosin assembly. Electron microscopic studies support a model of actin filament-mediated myosin assembly. In ADP, myosin monomers rapidly decorate F-actin, preventing extensive formation of thick filaments. In AMP-P[NH]P, myosin assembles along actin filaments, forming structures that resemble primitive stress fibers. Taken together, these data suggest a model in which site-directed assembly of thick filaments in Dictyostelium is mediated by the interaction of myosin monomers with cortical actin filament networks. | lld:pubmed |
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| pubmed-article:2762319 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2762319 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2762319 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2762319 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2762319 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2762319 | pubmed:author | pubmed-author:PardeeJ DJD | lld:pubmed |
| pubmed-article:2762319 | pubmed:author | pubmed-author:MahajanR KRK | lld:pubmed |
| pubmed-article:2762319 | pubmed:author | pubmed-author:JohnsJ AJA | lld:pubmed |
| pubmed-article:2762319 | pubmed:author | pubmed-author:VaughanK TKT | lld:pubmed |
| pubmed-article:2762319 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2762319 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2762319 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2762319 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2762319 | pubmed:pagination | 6161-5 | lld:pubmed |
| pubmed-article:2762319 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2762319 | pubmed:meshHeading | pubmed-meshheading:2762319-... | lld:pubmed |
| pubmed-article:2762319 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2762319 | pubmed:articleTitle | Actin filaments mediate Dictyostelium myosin assembly in vitro. | lld:pubmed |
| pubmed-article:2762319 | pubmed:affiliation | Department of Cell Biology and Anatomy, Cornell University Medical College, New York, NY 10021. | lld:pubmed |
| pubmed-article:2762319 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2762319 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2762319 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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