ArticleMolecular and cellular biology2002
Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 93 citations in OpenAlex.
- Systems level analysis of time and stimuli specific signaling through PKA.Molecular biology of the cell · 2024Article
- Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.bioRxiv : the preprint server for biology · 2023Article
- Modulation of fungal virulence through CRZ1 regulated F-BAR-dependent actin remodeling and endocytosis in chickpea infecting phytopathogen Ascochyta rabiei.PLoS genetics · 2021Article
- The protein architecture of the endocytic coat analyzed by FRET microscopy.Molecular systems biology · 2020Article
- TheJournal of cell science · 2019Article
- Type I myosins anchor actin assembly to the plasma membrane during clathrin-mediated endocytosis.The Journal of cell biology · 2019Article
- The F-BAR Domain of Rga7 Relies on a Cooperative Mechanism of Membrane Binding with a Partner Protein during Fission Yeast Cytokinesis.Cell reports · 2019Article
- Article
- Linking up at the BAR: Oligomerization and F-BAR protein function.Cell cycle (Georgetown, Tex.) · 2016Review
- Novel Interactome of Saccharomyces cerevisiae Myosin Type II Identified by a Modified Integrated Membrane Yeast Two-Hybrid (iMYTH) Screen.G3 (Bethesda, Md.) · 2016Article
- An Engineered Minimal WASP-Myosin Fusion Protein Reveals Essential Functions for Endocytosis.Developmental cell · 2015Article
- GreedyPlus: An Algorithm for the Alignment of Interface Interaction Networks.Scientific reports · 2015Article
- Control of lipid organization and actin assembly during clathrin-mediated endocytosis by the cytoplasmic tail of the rhomboid protein Rbd2.Molecular biology of the cell · 2015Article
- Calcineurin regulates the yeast synaptojanin Inp53/Sjl3 during membrane stress.Molecular biology of the cell · 2015Article
- Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site.Structure (London, England : 1993) · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Involvement of the adaptor protein 3 complex in lignocellulase secretion in Neurospora crassa revealed by comparative genomic screening.Biotechnology for biofuels · 2015Article
- Quantification of cytosolic interactions identifies Ede1 oligomers as key organizers of endocytosis.Molecular systems biology · 2014Article
- Yeast RAD2, a homolog of human XPG, plays a key role in the regulation of the cell cycle and actin dynamics.Biology open · 2014Article
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7 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
In Saccharomyces cerevisiae, the WASP (Wiskott-Aldrich syndrome protein) homologue Las17p (also called Bee1p) is an important component of cortical actin patches. Las17p is part of a high-molecular-weight protein complex that regulates Arp2/3 complex-dependent actin polymerization at the cell cortex and that includes the type I myosins Myo3p and Myo5p and verprolin (Vrp1p). To identify other factors implicated with this complex in actin regulation, we isolated proteins that bind to Las17p by two-hybrid screening and affinity chromatography. Here, we report the characterization of Lsb7/Bzz1p (for Las seventeen binding protein 7), an Src homology 3 (SH3) domain protein that interacts directly with Las17p via a polyproline-SH3 interaction. Bzz1p coimmunoprecipitates in a complex with Las17p, Vrp1p, Myo3/5p, Bbc1p, Hsp70p, and actin. It colocalizes with cortical actin patches and with Las17p. This localization is dependent on Las17p, but not on F-actin. Bzz1p interacts physically and genetically with type I myosins. While deletion of BZZ1 shows no obvious phenotype, simultaneous deletion of the BZZ1, MYO3, and MYO5 genes is lethal. Overexpression of Bzz1p inhibits cell growth, and a bzz1Delta myo5Delta double mutant is unable to restore actin polarity after NaCl stress. Finally, Bzz1p in vitro is able to recruit a functional actin polymerization machinery through its SH3 domains. Its interactions with Las17p, Vrp1p, and the type I myosins are essential for this process. This suggests that Bzz1p could be implicated in the regulation of actin polymerization.
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