ArticleProtoplasma2005
The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis.
Article in Protoplasma, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Phosphoinositides, Major Actors in Membrane Trafficking and Lipid Signaling Pathways.International journal of molecular sciences · 2017Review
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis.Molecular biology of the cell · 2012Article
- Lessons from yeast for clathrin-mediated endocytosis.Nature cell biology · 2011Review
- Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast.Current biology : CB · 2011Article
- Actin dynamics and endocytosis in yeast and mammals.Current opinion in biotechnology · 2010Review
- Physical mechanisms of signal integration by WASP family proteins.Annual review of biochemistry · 2010Review
- Functions of actin in endocytosis.Cellular and molecular life sciences : CMLS · 2009Review
- A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- btn1 affects endocytosis, polarization of sterol-rich membrane domains and polarized growth in Schizosaccharomyces pombe.Traffic (Copenhagen, Denmark) · 2008Article
- Central roles of small GTPases in the development of cell polarity in yeast and beyond.Microbiology and molecular biology reviews : MMBR · 2007Review
- The vtc4 gene influences polyphosphate storage, morphogenesis, and virulence in the maize pathogen Ustilago maydis.Eukaryotic cell · 2006Article
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Authors and funding
7 authors.
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Abstract
The formation of actin filaments is crucial for endocytosis and other interrelated cellular phenomena such as motility, polarized morphogenesis, and cytokinesis. In this paper we have investigated the role of the WASP/Las17-interacting protein Bzz1p in endocytosis and trafficking to the vacuole. We and others have recently shown that Bzz1p is an actin patch protein that interacts directly with Las17p via a SH3-polyproline interaction. Bzz1p functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. In an in vitro bead assay, GST-Bzz1p fusion protein triggers a functional actin polymerization machinery through its two C-terminal SH3 domains. In this paper we implicate Bzz1p with the type I myosins both in fluid-phase and in the internalization step of receptor-mediated endocytosis. As deduced from their localization as GFP fusions, the vacuolar delivery of endocytic and biosynthetic cargoes as well as the multivesicular body pathway appear unaffected. We further elucidate Bzz1p direct participation in actin polymerization by demonstrating that each of the SH3 domains of Bzz1p individually is able to trigger actin polymerization in a cell-free system dependent on Arp2/3, Las17p, Vrp1p, and the type I myosins. Taken together, our results show that Bzz1p participates, essentially via its SH3 domains, in early steps of endocytosis together with known actin nucleation activators.
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