Formins at a glance

Breitsprecher, Dennis; Goode, Bruce L.

doi:10.1242/jcs.107250

Cited by 282 publications

(279 citation statements)

References 159 publications

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“…Error bars are S.D. For scoring latrunculin A (LatA) 2 -resistant actin cables, 5-ml cultures of wild type, kel1⌬, kel2⌬, and bud14⌬ strains were grown in YPD to log phase. Cells were pelleted, resuspended in 1 ml of YPD, and allowed to recover for 30 min.…”

Section: Methodsmentioning

confidence: 99%

“…Formins are a widely conserved family of proteins that directly nucleate, elongate, and/or bundle actin filaments and perform a variety of biological roles ranging from the control of cell motility and adhesion to the regulation of intracellular transport and formation of cytokinetic actin rings (1,2). It has recently become clear that most formins interact with additional cellular factors that govern their activities in distinct ways, including the release of formins from autoinhibition (e.g.…”

mentioning

confidence: 99%

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Saccharomyces cerevisiae Kelch Proteins and Bud14 Protein Form a Stable 520-kDa Formin Regulatory Complex That Controls Actin Cable Assembly and Cell Morphogenesis

Gould

Chesarone-Cataldo

Alioto

et al. 2014

Journal of Biological Chemistry

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Background: Kelch proteins are required for cell morphogenesis, but their molecular functions have remained elusive. Results: S. cerevisiae Kel1 and Kel2 form a stable complex with the formin-binding protein Bud14 to regulate actin cable assembly. Conclusion: Kel1 and Kel2 directly regulate formins to control the actin cytoskeleton. Significance: These findings help resolve the roles of S. cerevisiae Kel1 and Kel2 in morphogenesis.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Saccharomyces cerevisiae Kelch Proteins and Bud14 Protein Form a Stable 520-kDa Formin Regulatory Complex That Controls Actin Cable Assembly and Cell Morphogenesis

Gould

Chesarone-Cataldo

Alioto

et al. 2014

Journal of Biological Chemistry

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“…Actin-related protein 2/3 (Arp2/3), formins, and tandem-G-actin-binding proteins are the three classes of known actin nucleators in nonmuscle cells (1)(2)(3)(4)(5)(6)(7). Arp2/3-mediated actin nucleation produces branched actin networks, whereas formins and tandem-G-actin-binding nucleators result in long, unbranched actin filaments (1)(2)(3)(4)(5)(6)(7).…”

mentioning

confidence: 99%

Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells

Chen

Kondrashkina

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Leiomodin (Lmod) is a class of potent tandem-G-actin-binding nucleators in muscle cells. Lmod mutations, deletion, or instability are linked to lethal nemaline myopathy. However, the lack of highresolution structures of Lmod nucleators in action severely hampered our understanding of their essential cellular functions. Here we report the crystal structure of the actin-Lmod2 162-495 nucleus. The structure contains two actin subunits connected by one Lmod2 162-495 molecule in a non-filament-like conformation. Complementary functional studies suggest that the binding of Lmod2 stimulates ATP hydrolysis and accelerates actin nucleation and polymerization. The high level of conservation among Lmod proteins in sequence and functions suggests that the mechanistic insights of human Lmod2 uncovered here may aid in a molecular understanding of other Lmod proteins. Furthermore, our structural and mechanistic studies unraveled a previously unrecognized level of regulation in mammalian signal transduction mediated by certain tandem-G-actin-binding nucleators.actin nucleation | nemaline myopathy | pointed-end elongation

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“…Actin cross-linking factors (7; e.g., fascin, actinin, and myosin II) assemble F-actin into networks or bundles and/or exert pulling forces. Different classes of myosin motors (8,9) mediate cargo (C) transport towards the plus or minusends of the filaments. F-actin can be post-translationally modified (PM) by specialized enzymes another by a range of different cross-linking proteins or myosin motor proteins; stabilizing filaments, weaving them into different classes of networks, using them as highways for transport processes or as scaffolds to pull and generate forces [7,38].…”

Section: Actin Dynamicsmentioning

confidence: 99%

Mathematical-Computational Simulation of Cytoskeletal Dynamics

Moura

Kritz

Leal

et al. 2016

Mathematical Modeling and Computational Intelligence in Engineering Applications

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Actin and microtubules are components of the cytoskeleton, and are key mediators of neuron growth and maintenance. Knowing how they are regulated enhances our understanding of neural development, ageing, degeneration, and regeneration. However, biological investigation alone will not unravel the complex cytoskeletal machinery. We expect that inquiries about the cytoskeleton can be significantly enhanced if their physico-chemical behavior is concealed and summarized in mathematical and computational models that can be coupled to concepts of biological regulation. Our computational modeling concerns the mechanical aspects associated with the dynamics of relatively simple, finger-like membrane protrusions called filopodia. Here we propose an alternative approach for representing the displacement of molecules and cytoplasmic fluid in the extremely narrow and long filopodia and discuss strategies to couple the particle-in-cell method with algorithms for laminar flow to model the two phases of actin dynamics: polymerization into filaments which are pulled back into the cell and compensatory G-actin drift towards its tip to supply polymerization. We use nerve cells of the fruit fly Drosophila as an effective, genetically amenable biological system to generate experimental data as the basis for the abstract models and their validation.

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Formins at a glance

Cited by 282 publications

References 159 publications

Saccharomyces cerevisiae Kelch Proteins and Bud14 Protein Form a Stable 520-kDa Formin Regulatory Complex That Controls Actin Cable Assembly and Cell Morphogenesis

Saccharomyces cerevisiae Kelch Proteins and Bud14 Protein Form a Stable 520-kDa Formin Regulatory Complex That Controls Actin Cable Assembly and Cell Morphogenesis

Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells

Mathematical-Computational Simulation of Cytoskeletal Dynamics

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