pubmed-article:7622560 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7622560 | lifeskim:mentions | umls-concept:C0086669 | lld:lifeskim |
pubmed-article:7622560 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
pubmed-article:7622560 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:7622560 | lifeskim:mentions | umls-concept:C0320458 | lld:lifeskim |
pubmed-article:7622560 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:7622560 | pubmed:dateCreated | 1995-8-29 | lld:pubmed |
pubmed-article:7622560 | pubmed:abstractText | The actin-activated Mg(2+)-ATPase activities of the three myosin I isoforms in Acanthamoeba castellanii are significantly expressed only after phosphorylation of a single site in the myosin I heavy chain. Synthetic phosphorylated and unphosphorylated peptides corresponding to the phosphorylation site sequences, which differ for the three myosin I isoforms, were used to raise isoform-specific antibodies that recognized only the phosphorylated myosin I or the total myosin I isoform (phosphorylated and unphosphorylated), respectively. With these antisera, the amounts of total and phosphorylated isoform were quantified, the phosphomyosin I isoforms localized, and the compartmental distribution of the phosphomyosin isoforms determined. Myosin IA, which was almost entirely in the actin-rich cortex, was 70-100% phosphorylated and particularly enriched under phagocytic cups. Myosins IB and IC were predominantly associated with plasma membranes and large vacuole membranes, where they were only 10-20% phosphorylated, whereas cytoplasmic myosins IB and IC, like cytoplasmic myosin IA, were mostly phosphorylated (60-100%). Moreover, phosphomyosin IB was concentrated in actively motile regions of the plasma membrane. More than 20-fold more phosphomyosin IC and 10-fold more F-actin were associated with the membranes of contracting contractile vacuoles (CV) than of filling CVs. As the total amount of CV-associated myosin IC remained constant, it must be phosphorylated at the start of CV contraction. These data extend previous proposals for the specific functions of myosin I isozymes in Acanthamoeba (Baines, I.C., H. Brzeska, and E.D. Korn. 1992. J. Cell Biol. 119: 1193-1203): phosphomyosin IA in phagocytosis, phosphomyosin IB in phagocytosis and pinocytosis, and phosphomyosin IC in contraction of the CV. | lld:pubmed |
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pubmed-article:7622560 | pubmed:language | eng | lld:pubmed |
pubmed-article:7622560 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7622560 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7622560 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7622560 | pubmed:month | Aug | lld:pubmed |
pubmed-article:7622560 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:7622560 | pubmed:author | pubmed-author:KornE DED | lld:pubmed |
pubmed-article:7622560 | pubmed:author | pubmed-author:BainesI CIC | lld:pubmed |
pubmed-article:7622560 | pubmed:author | pubmed-author:Corigliano-Mu... | lld:pubmed |
pubmed-article:7622560 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7622560 | pubmed:volume | 130 | lld:pubmed |
pubmed-article:7622560 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7622560 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7622560 | pubmed:pagination | 591-603 | lld:pubmed |
pubmed-article:7622560 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:7622560 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7622560 | pubmed:articleTitle | Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii. | lld:pubmed |
pubmed-article:7622560 | pubmed:affiliation | Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. | lld:pubmed |
pubmed-article:7622560 | pubmed:publicationType | Journal Article | lld:pubmed |
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