{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:08:48Z","timestamp":1791295728944,"version":"4.1.0"},"reference-count":49,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2002,3,1]],"date-time":"2002-03-01T00:00:00Z","timestamp":1014940800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>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.<\/jats:p>","DOI":"10.1093\/genetics\/160.3.923","type":"journal-article","created":{"date-parts":[[2021,4,28]],"date-time":"2021-04-28T05:46:08Z","timestamp":1619588768000},"page":"923-934","source":"Crossref","is-referenced-by-count":51,"title":["The Novel Adaptor Protein, Mti1p, and Vrp1p, a Homolog of Wiskott-Aldrich Syndrome Protein-Interacting Protein (WIP), May Antagonistically Regulate Type I Myosins in <i>Saccharomyces cerevisiae<\/i>"],"prefix":"10.1093","volume":"160","author":[{"given":"Junko","family":"Mochida","sequence":"first","affiliation":[{"name":"Division of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, 060-0815, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takaharu","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"Division of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, 060-0815, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konomi","family":"Fujimura-Kamada","sequence":"additional","affiliation":[{"name":"Division of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, 060-0815, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuma","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Division of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, 060-0815, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2002,3,1]]},"reference":[{"key":"2022010508463935900_R1","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1083\/jcb.98.3.934","article-title":"Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae","volume":"98","author":"Adams","year":"1984","journal-title":"J. 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