{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T13:35:46Z","timestamp":1791207346019,"version":"4.1.0"},"reference-count":48,"publisher":"Rockefeller University Press","issue":"3","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1997,2,10]]},"abstract":"<jats:p>Yeast protein, Bee1, exhibits sequence homology to Wiskott-Aldrich syndrome protein (WASP), a human protein that may link signaling pathways to the actin cytoskeleton. Mutations in WASP are the primary cause of Wiskott-Aldrich syndrome, characterized by immuno-deficiencies and defects in blood cell morphogenesis. This report describes the characterization of Bee1 protein function in budding yeast. Disruption of BEE1 causes a striking change in the organization of actin filaments, resulting in defects in budding and cytokinesis. Rather than assemble into cortically associated patches, actin filaments in the buds of \u0394bee1 cells form aberrant bundles that do not contain most of the cortical cytoskeletal components. It is significant that \u0394bee1 is the only mutation reported so far that abolishes cortical actin patches in the bud. Bee1 protein is localized to actin patches and interacts with Sla1p, a Src homology 3 domain\u2013containing protein previously implicated in actin assembly and function. Thus, Bee1 protein may be a crucial component of a cytoskeletal complex that controls the assembly and organization of actin filaments at the cell cortex.<\/jats:p>","DOI":"10.1083\/jcb.136.3.649","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:47:50Z","timestamp":1027702070000},"page":"649-658","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":224,"title":["Bee1, a Yeast Protein with Homology to Wiscott-Aldrich Syndrome Protein, Is Critical for the Assembly of Cortical Actin Cytoskeleton"],"prefix":"10.1083","volume":"136","author":[{"given":"Rong","family":"Li","sequence":"first","affiliation":[{"name":"Department of Cell Biology, Harvard Medical School, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1997,2,10]]},"reference":[{"key":"2023072206451359700_B1","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1126\/science.2643162","article-title":"A yeast actin-binding protein is encoded by SAC6, a gene found by suppression of an actin mutation","volume":"243","author":"Adams","year":"1989","journal-title":"Science (Wash DC)"},{"key":"2023072206451359700_B2","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1038\/354404a0","article-title":"Requirement of yeast fimbrin for actin organization and morphogenesis in vivo.","volume":"354","author":"Adams","year":"1991","journal-title":"Nature (Lond)"},{"key":"2023072206451359700_B3","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1083\/jcb.111.1.131","article-title":"CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae.","volume":"111","author":"Adams","year":"1990","journal-title":"J Cell Biol"},{"key":"2023072206451359700_B4","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 Cell Biol"},{"key":"2023072206451359700_B5","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1083\/jcb.117.5.1067","article-title":"Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiaecapping protein","volume":"117","author":"Amatruda","year":"1992","journal-title":"J Cell Biol"},{"key":"2023072206451359700_B6","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/344352a0","article-title":"Disruption of the actin cytoskeleton in yeast capping protein mutants","volume":"344","author":"Amatruda","year":"1990","journal-title":"Nature (Lond)"},{"key":"2023072206451359700_B7","doi-asserted-by":"crossref","first-page":"2817","DOI":"10.1083\/jcb.105.6.2817","article-title":"Distribution and cellular localization of actin depolymerizing factor","volume":"105","author":"Bamburg","year":"1987","journal-title":"J Cell Biol"},{"key":"2023072206451359700_B8","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/S0960-9822(02)00642-5","article-title":"Wiskott-Aldrich syndrome protein (WASP) is a binding partner for C-src family protein-tyrosine kinases","volume":"6","author":"Banin","year":"1996","journal-title":"Curr Biol"},{"key":"2023072206451359700_B9","first-page":"1295","article-title":"Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae.","volume":"11","author":"Bender","year":"1991","journal-title":"Mol Cell Biol"},{"key":"2023072206451359700_B10","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1002\/yea.320070506","article-title":"The YDp plasmid: a uniform set of vectors bearing versatile gene disruption cassettes for Saccharomyces cerevisiae.","volume":"7","author":"Berben","year":"1991","journal-title":"Yeast"},{"key":"2023072206451359700_B11","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1083\/jcb.126.4.821","article-title":"What are the basic functions of microfilaments? 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