ArticleMolecular biology of the cell2008
Analysis of unregulated formin activity reveals how yeast can balance F-actin assembly between different microfilament-based organizations.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 33 citations in OpenAlex.
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- Bil2 Is a Novel Inhibitor of the Yeast Formin Bnr1 Required for Proper Actin Cable Organization and Polarized Secretion.Frontiers in cell and developmental biology · 2021Article
- F-Actin Cytoskeleton Network Self-Organization Through Competition and Cooperation.Annual review of cell and developmental biology · 2020Review
- A Cdc42 GEF, Gef1, through endocytosis organizes F-BAR Cdc15 along the actomyosin ring and promotes concentric furrowing.Journal of cell science · 2019Article
- Discovery of functional interactions among actin regulators by analysis of image fluctuations in an unperturbed motile cell system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables.Molecular biology of the cell · 2018Article
- Global treadmilling coordinates actin turnover and controls the size of actin networks.Nature reviews. Molecular cell biology · 2017Review
- Internetwork competition for monomers governs actin cytoskeleton organization.Nature reviews. Molecular cell biology · 2016Article
- Computational model of polarized actin cables and cytokinetic actin ring formation in budding yeast.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Profilin-1 serves as a gatekeeper for actin assembly by Arp2/3-dependent and -independent pathways.Developmental cell · 2015Article
- Homeostatic actin cytoskeleton networks are regulated by assembly factor competition for monomers.Current biology : CB · 2014Article
- Control of polarized growth by the Rho family GTPase Rho4 in budding yeast: requirement of the N-terminal extension of Rho4 and regulation by the Rho GTPase-activating protein Bem2.Eukaryotic cell · 2013Article
- Fission yeast sec3 bridges the exocyst complex to the actin cytoskeleton.Traffic (Copenhagen, Denmark) · 2012Article
- Regulation of the formin Bnr1 by septins anda MARK/Par1-family septin-associated kinase.Molecular biology of the cell · 2012Article
- A systems-biology approach to yeast actin cables.Advances in experimental medicine and biology · 2012Article
- Cotranslational transport of ABP140 mRNA to the distal pole of S. cerevisiae.The EMBO journal · 2011Article
- A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop.RNA (New York, N.Y.) · 2011Article
- Cytoskeletal dynamics in fission yeast: a review of models for polarization and division.HFSP journal · 2010Article
- The yeast formin Bnr1p has two localization regions that show spatially and temporally distinct association with septin structures.Molecular biology of the cell · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Formins are regulated actin-nucleating proteins that are widespread among eukaryotes. Overexpression of unregulated formins in budding yeast is lethal and causes a massive accumulation of disorganized cable-like filaments. To explore the basis of this lethality, a cDNA library was screened to identify proteins whose overexpression could rescue the lethality conferred by unregulated Bnr1p expression. Three classes of suppressors encoding actin-binding proteins were isolated. One class encodes proteins that promote the assembly of actin cables (TPM1, TPM2, and ABP140), suggesting that the lethality was rescued by turning disorganized filaments into functional cables. The second class encodes proteins that bind G-actin (COF1, SRV2, and PFY1), indicating that reduction of the pool of actin available for cable formation may also rescue lethality. Consistent with this, pharmacological or genetic reduction of available actin also protected the cell from overproduction of unregulated Bnr1p. The third class consists of Las17p, an activator of the formin-independent Arp2/3p-dependent actin nucleation pathway. These results indicate that proper assembly of actin cables is sensitive to the appropriate balance of their constituents and that input into one pathway for actin filament assembly can affect another. Thus, cells must have a way of ensuring a proper balance between actin assembly pathways.
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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.