Cell Biology: Capturing Formin’s Mechano-Inhibition

Vavylonis, Dimitrios; Horan, Brandon G.

doi:10.1016/j.cub.2017.08.020

Cited by 3 publications

(3 citation statements)

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“…It is also not clear how binding of one or multiple profilin or profilin‐actin complexes can influence FH1 structure. This lack in understanding of basic biophysical properties of formins poses barriers to resolving many issues pertaining to their role in actin polymerization, such as the observed dependence of external force on formin‐mediated polymerization and acceleration of polymerization in the presence of co‐factors .…”

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confidence: 99%

Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin‐actin transfer

et al. 2018

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Formins accelerate actin polymerization, assumed to occur through flexible FH1 domain mediated transfer of profilin-actin to the barbed end. To study FH1 properties and address sequence effects including varying length/distribution of profilin-binding proline-rich motifs, we performed all-atom simulations of mouse mDia1, mDia2; budding yeast Bni1, Bnr1; fission yeast Cdc12, For3, and Fus1 FH1s. We find FH1 has flexible regions between high propensity polyproline helix regions. A coarse-grained model retaining sequence-specificity, assuming rigid polyproline segments, describes their size. Multiple bound profilins or profilin-actin complexes expand mDia1-FH1, which may be important in cells. Simulations of the barbed end bound to Bni1-FH1-FH2 dimer show the leading FH1 can better transfer profilin or profilin-actin, having decreasing probability with increasing distance from FH2.

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Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin‐actin transfer

et al. 2018

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“…Actin filaments are then 'captured' by myosin-II from neighboring nodes. Next, myosin-II 'pulls' nodes closer together until their attachment is 'released' by F-actin severing (Vavylonis et al, 2008;Vavylonis and Horan, 2017). Zimmermann et al reconstituted a portion of the proposed SCPR mechanism using beads (1 µm diameter) that were conjugated to either myosin-II or a formin fragment containing formin homology (FH) 2 and FH1 domains with nucleation and elongation activity, respectively (Fig.…”

Section: Cytokinesis In Vitromentioning

confidence: 99%

Molecular form and function of the cytokinetic ring

Mangione

Gould

2019

Journal of Cell Science

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Animal cells, amoebas and yeast divide using a force-generating, actin-and myosin-based contractile ring or 'cytokinetic ring' (CR). Despite intensive research, questions remain about the spatial organization of CR components, the mechanism by which the CR generates force, and how other cellular processes are coordinated with the CR for successful membrane ingression and ultimate cell separation. This Review highlights new findings about the spatial relationship of the CR to the plasma membrane and the arrangement of molecules within the CR from studies using advanced microscopy techniques, as well as mechanistic information obtained from in vitro approaches. We also consider advances in understanding coordinated cellular processes that impact the architecture and function of the CR.

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“…It is also not clear how binding of one or multiple profilin or profilin-actin complexes can influence FH1 structure. This lack in understanding of basic biophysical properties of formins poses barriers to resolving many issues pertaining to their role in actin polymerization, such as the observed dependence of external force on formin-mediated polymerization [14,27,31,51,53,56] and acceleration of polymerization in the presence of cofactors [22].…”

Section: Introductionmentioning

confidence: 99%