| pubmed-article:2326262 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2326262 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:2326262 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:2326262 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:2326262 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2326262 | lifeskim:mentions | umls-concept:C0060611 | lld:lifeskim |
| pubmed-article:2326262 | lifeskim:mentions | umls-concept:C0386210 | lld:lifeskim |
| pubmed-article:2326262 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:2326262 | pubmed:dateCreated | 1990-5-24 | lld:pubmed |
| pubmed-article:2326262 | pubmed:abstractText | The calcium-dependent proteolysis of fodrin has been implicated in the regulation of secretion, neutrophil and platelet activation, and long-term potentiation in neurons. In vitro studies indicate that calcium-dependent protease I (calpain I) cleaves fodrin in the middle of the alpha subunit and in the COOH-terminal third of the beta subunit. Cleavage at the beta site requires calmodulin, which binds with high affinity to a single site in the alpha subunit. In vitro binding assays, nondenaturing gel electrophoresis, and velocity sedimentation identify a linkage between calcium-dependent protease I proteolysis of fodrin and the ability of calmodulin to regulate the self-association of fodrin and its interaction with actin. Three functional states appear to exist: (i) intact fodrin, which constitutively forms tetramers and binds F-actin; (ii) alpha-cleaved fodrin, which loses its ability to self-associate and bind F-actin in the presence of calmodulin; and (iii) alpha,beta-cleaved fodrin, a form that is incompetent to establish tetramers or bind actin. Because actin binding and fodrin self-association occur at opposite ends of the molecule, whereas calmodulin binds at its center, these results indicate that long-range interactions exist within fodrin. They also offer an example of how two calcium-dependent regulatory processes may act synergistically to reversibly regulate a linkage between the membrane and the cytoskeleton. | lld:pubmed |
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| pubmed-article:2326262 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2326262 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2326262 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2326262 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2326262 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2326262 | pubmed:author | pubmed-author:MorrowJ SJS | lld:pubmed |
| pubmed-article:2326262 | pubmed:author | pubmed-author:HarrisA SAS | lld:pubmed |
| pubmed-article:2326262 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2326262 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2326262 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2326262 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2326262 | pubmed:pagination | 3009-13 | lld:pubmed |
| pubmed-article:2326262 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2326262 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2326262 | pubmed:articleTitle | Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. | lld:pubmed |
| pubmed-article:2326262 | pubmed:affiliation | Department of Pathology, Yale University School of Medicine, New Haven, CT 06510. | lld:pubmed |
| pubmed-article:2326262 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2326262 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2326262 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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