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Myosin-gelsolin cooperativity in actin filament severing and actomyosin motor activity

Venukumar Vemula, Tamas Huber, Marko Usaj, View ORCID ProfileBeáta Bugyi, View ORCID ProfileAlf Mansson
doi: https://doi.org/10.1101/2020.09.02.279729
Venukumar Vemula
1Linnaeus University, Dept. of Chemistry and Biomedical Sciences, Universitetskajen, 391 82 Kalmar
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Tamas Huber
2University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, Pécs, H-7624, Hungary
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Marko Usaj
1Linnaeus University, Dept. of Chemistry and Biomedical Sciences, Universitetskajen, 391 82 Kalmar
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Beáta Bugyi
2University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, Pécs, H-7624, Hungary
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  • ORCID record for Beáta Bugyi
  • For correspondence: alf.mansson@lnu.se beata.bugyi@aok.pte.hu
Alf Mansson
1Linnaeus University, Dept. of Chemistry and Biomedical Sciences, Universitetskajen, 391 82 Kalmar
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  • ORCID record for Alf Mansson
  • For correspondence: alf.mansson@lnu.se beata.bugyi@aok.pte.hu
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Abstract

Actin is a major intracellular protein with key functions in cellular motility, signalling and structural rearrangements. Its dynamic behavior with actin filaments (F-actin) polymerising and depolymerising in response to intracellular changes, is controlled by actin-binding proteins (ABPs). Gelsolin is one of the most potent filament severing ABPs. However, myosin motors that interact with actin in the presence of ATP also produce actin filament fragmentation through motor induced shearing forces. To test the idea that gelsolin and myosin cooperate in these processes we used the in vitro motility assay, where actin filaments are propelled by surface-adsorbed heavy meromyosin (HMM) motor fragments. This allows studies of both motility and filament dynamics using isolated proteins. Gelsolin (5 nM) at very low [Ca2+] (free [Ca2+] ∼6.8 nM) appreciably enhanced actin filament severing caused by HMM-induced forces at 1 mM [MgATP], an effect that was increased at increased HMM motor density. This finding is consistent with cooperativity between actin filament severing by myosin-induced forces and by gelsolin. As further support of myosin-gelsolin cooperativity we observed reduced sliding velocity of the HMM propelled filaments in the presence of gelsolin. Overall, the results corroborate ideas for cooperative effects between gelsolin-induced alterations in the actin filaments and changes due to myosin motor activity, leading among other effects to enhanced F-actin severing of possible physiological relevance.

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Posted September 03, 2020.
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Myosin-gelsolin cooperativity in actin filament severing and actomyosin motor activity
Venukumar Vemula, Tamas Huber, Marko Usaj, Beáta Bugyi, Alf Mansson
bioRxiv 2020.09.02.279729; doi: https://doi.org/10.1101/2020.09.02.279729
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Myosin-gelsolin cooperativity in actin filament severing and actomyosin motor activity
Venukumar Vemula, Tamas Huber, Marko Usaj, Beáta Bugyi, Alf Mansson
bioRxiv 2020.09.02.279729; doi: https://doi.org/10.1101/2020.09.02.279729

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