| pubmed-article:11901111 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C1135629 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C1823857 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11901111 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:11901111 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11901111 | pubmed:dateCreated | 2002-3-19 | lld:pubmed |
| pubmed-article:11901111 | pubmed:abstractText | Type I myosins in yeast, Myo3p and Myo5p (Myo3/5p), are involved in the reorganization of the actin cytoskeleton. The SH3 domain of Myo5p regulates the polymerization of actin through interactions with both Las17p, a homolog of mammalian Wiskott-Aldrich syndrome protein (WASP), and Vrp1p, a homolog of WASP-interacting protein (WIP). Vrp1p is required for both the localization of Myo5p to cortical patch-like structures and the ATP-independent interaction between the Myo5p tail region and actin filaments. We have identified and characterized a new adaptor protein, Mti1p (Myosin tail region-interacting protein), which interacts with the SH3 domains of Myo3/5p. Mti1p co-immunoprecipitated with Myo5p and Mti1p-GFP co-localized with cortical actin patches. A null mutation of MTI1 exhibited synthetic lethal phenotypes with mutations in SAC6 and SLA2, which encode actin-bundling and cortical actin-binding proteins, respectively. Although the mti1 null mutation alone did not display any obvious phenotype, it suppressed vrp1 mutation phenotypes, including temperature-sensitive growth, abnormally large cell morphology, defects in endocytosis and salt-sensitive growth. These results suggest that Mti1p and Vrp1p antagonistically regulate type I myosin functions. | lld:pubmed |
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| pubmed-article:11901111 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11901111 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11901111 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11901111 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11901111 | pubmed:issn | 0016-6731 | lld:pubmed |
| pubmed-article:11901111 | pubmed:author | pubmed-author:MochidaJunkoJ | lld:pubmed |
| pubmed-article:11901111 | pubmed:author | pubmed-author:YamamotoTakah... | lld:pubmed |
| pubmed-article:11901111 | pubmed:author | pubmed-author:Fujimura-Kama... | lld:pubmed |
| pubmed-article:11901111 | pubmed:author | pubmed-author:TanakaKazumaK | lld:pubmed |
| pubmed-article:11901111 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11901111 | pubmed:volume | 160 | lld:pubmed |
| pubmed-article:11901111 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11901111 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11901111 | pubmed:pagination | 923-34 | lld:pubmed |
| pubmed-article:11901111 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11901111 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11901111 | pubmed:articleTitle | The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae. | lld:pubmed |
| pubmed-article:11901111 | pubmed:affiliation | Division of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, 060-0815, Japan. | lld:pubmed |
| pubmed-article:11901111 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11901111 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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