ArticleThe Journal of cell biology1997
Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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Who cites it
96 citing papers in PubMed, 245 citations in OpenAlex.
- Exploring roles for essential proteins in yeast filamentous growth identifies the WASP homolog Las17 as a regulator of the Cdc42-dependent fMAPK pathway.bioRxiv : the preprint server for biology · 2026Article
- Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation.Communications biology · 2025Article
- Loss of cytoplasmic actin filaments raises nuclear actin levels to drive INO80C-dependent chromosome fragmentation.Nature communications · 2024Article
- Phosphorylation of the WH2 domain in yeast Las17/WASP regulates G-actin binding and protein function during endocytosis.Scientific reports · 2021Article
- Article
- WASP family proteins, more than Arp2/3 activators.Biochemical Society transactions · 2016Review
- Polarized Exocytosis Induces Compensatory Endocytosis by Sec4p-Regulated Cortical Actin Polymerization.PLoS biology · 2016Article
- Elucidating Key Motifs Required for Arp2/3-Dependent and Independent Actin Nucleation by Las17/WASP.PloS one · 2016Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Exploration of the dynamic properties of protein complexes predicted from spatially constrained protein-protein interaction networks.PLoS computational biology · 2014Article
- Targeting and functional mechanisms of the cytokinesis-related F-BAR protein Hof1 during the cell cycle.Molecular biology of the cell · 2013Article
- Lsb1 is a negative regulator of las17 dependent actin polymerization involved in endocytosis.PloS one · 2013Article
- SLAC, a complex between Sla1 and Las17, regulates actin polymerization during clathrin-mediated endocytosis.Molecular biology of the cell · 2012Article
- Cell polarization and cytokinesis in budding yeast.Genetics · 2012Review
- From networks of protein interactions to networks of functional dependencies.BMC systems biology · 2012Article
- Wsp1 is downstream of Cin1 and regulates vesicle transport and actin cytoskeleton as an effector of Cdc42 and Rac1 in Cryptococcus neoformans.Eukaryotic cell · 2012Article
- Rong Li: tipping the balance in cell biology. Interview by Caitlin Sedwick.The Journal of cell biology · 2011Article
- Endosomal Na+ (K+)/H+ exchanger Nhx1/Vps44 functions independently and downstream of multivesicular body formation.The Journal of biological chemistry · 2011Article
- Actin organization and dynamics in filamentous fungi.Nature reviews. Microbiology · 2011Review
- The endocytic adaptor proteins of pathogenic fungi: charting new and familiar pathways.Medical mycology · 2011Review
36 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 delta bee1 cells form aberrant bundles that do not contain most of the cortical cytoskeletal components. It is significant that delta bee1 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-containing 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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.