Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis

Farrell, Kristen B.; McDonald, S.M.; Lamb, Andrew K.; Worcester, Colette; Peersen, Olve B.; Pietro, Santiago M. Di

doi:10.1083/jcb.201604123

Cited by 15 publications

(39 citation statements)

References 57 publications

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“…S. cerevisiae Bbc1 was also shown to recruit the Tda2-Aim21 complex, which regulates capping protein recruitment (Farrell et al, 2017;Shin et al, 2018). However, this role of Bbc1 has not yet been explored in S. pombe.…”

Section: Comparison With Budding Yeastmentioning

confidence: 99%

The S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly

MacQuarrie

Mangione

Carroll

et al. 2019

Journal of Cell Science

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Arp2/3 complex-nucleated branched actin networks provide the key force necessary for endocytosis. The Arp2/3 complex is activated by nucleation-promoting factors including the Schizosaccharomyces pombe Wiskott-Aldrich syndrome protein (Wsp1) and myosin-1 (Myo1). There are >40 known yeast endocytic proteins with distinct spatial and temporal localizations and functions; however, it is still unclear how these proteins work together to drive endocytosis. Here, we used quantitative live-cell imaging to determine the function of the uncharacterized S. pombe protein Bbc1. We discovered that Myo1 interacts with and recruits Bbc1 to sites of endocytosis. Bbc1 competes with the verprolin Vrp1 for localization to patches and association with Myo1, thus releasing Vrp1 and its binding partner Wsp1 from Myo1. Normally Myo1 remains at the base of the endocytic invagination and Vrp1-Wsp1 internalizes with the endocytic vesicle. However, in the absence of Bbc1, a portion of Vrp1-Wsp1 remains with Myo1 at the base of the invagination, and endocytic structures internalize twice as far. We propose that Bbc1 disrupts a transient interaction of Myo1 with Vrp1 and Wsp1 and thereby limits Arp2/3 complex-mediated nucleation of actin branches at the plasma membrane. This article has an associated First Person interview with the first author of the paper.

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Section: Comparison With Budding Yeastmentioning

confidence: 99%

The S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly

MacQuarrie

Mangione

Carroll

et al. 2019

Journal of Cell Science

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“…While this article was being assembled, Farrell et al (2017) reported the existence and characterization of the Aim21/Tda2 complex, its localization, and the structure of Tda2. We concur with much of their study and provide important new information about the mechanism of Aim21/Tda2 localization and uncover its function as a factor that regulates the assembly at the barbed end to balance the actin distribution between cables and patches.…”

Section: Introductionmentioning

confidence: 99%

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

Shin

Leeuwen

Boone

et al. 2018

MBoC

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“…This finding agrees with previous data in human cells that interaction of CP with CPI-containing proteins contributes to CP localization. The specific CP binding partners in actin patches are unknown in S. pombe, but may involve the homologue of S. cerevisiae Aim21, which was recently proposed to bind CP through the CPI-binding residues and contribute to its localization to actin patches [19], though this finding was not reproduced in a second study [20]. Consistent with this hypothesis, deletion of S. pombe Aim21 was identified in our genome-wide screen to have fusion defects [44].…”

Section: Cp-formin Competition Is Best Revealed In Cells In Which It mentioning

confidence: 68%

“…Indeed, CP carrying surface mutations that block CPI motif binding retain capping activity in vitro, but lose localization and function in vivo, indicating that binding partners are required for its activity in vivo [18]. Furthermore, the Aim21/Tda2 complex, which binds CP through the same surface residues, modulates CP recruitment and activity at actin patches in yeast [19,20]. By keeping filaments short, CP promotes Arp2/3 branching and plays a major role in the force production of dendritic networks [21].…”

Section: Introductionmentioning

confidence: 99%

Capping protein insulates Arp2/3-assembled actin patches from formins

Billault-Chaumartin

Martin

2019

Preprint

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How actin structures of distinct identities and functions co-exist within the same environment is a critical self-organization question. Fission yeast cells have a simple actin cytoskeleton made of four structures: Arp2/3 assembles actin patches around endocytic pits; the formins For3, Cdc12 and Fus1 assemble actin cables, the cytokinetic ring during division, and the fusion focus during sexual reproduction, respectively. The focus concentrates the delivery of hydrolases by myosin V to digest the cell wall for cell fusion. We discovered that cells lacking capping protein (CP), a heterodimer that blocks barbed-end dynamics and associates with actin patches, exhibit a delay in fusion. Consistent with CP-formin competition for barbed-end binding, Fus1, F-actin and the linear filament marker tropomyosin hyper-accumulate at the fusion focus in absence of CP. However, myosin V and exocytic cargoes are diverted to ectopic foci and reduced at the fusion focus, which underlies the fusion defect. Remarkably, ectopic foci coincide with actin patches, which now contain low levels of Fus1. During mitotic growth, actin patches lacking CP similarly display a dual identity, as they accumulate the formins For3 and Cdc12 and are co-decorated by tropomyosin and the patch marker fimbrin. Thus, CP serves to protect Arp2/3-nucleated structures from formin activity.

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Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis

Cited by 15 publications

References 57 publications

The S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly

The S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly

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

Capping protein insulates Arp2/3-assembled actin patches from formins

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