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Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level

Author

Listed:
  • Lucia Gardini

    (University of Florence
    National Institute of Optics—National Research Council)

  • Sarah M. Heissler

    (National Institutes of Health)

  • Claudia Arbore

    (University of Florence
    University of Florence)

  • Yi Yang

    (National Institutes of Health
    Hunan Agricultural University)

  • James R. Sellers

    (National Institutes of Health)

  • Francesco S. Pavone

    (University of Florence
    National Institute of Optics—National Research Council
    University of Florence)

  • Marco Capitanio

    (University of Florence
    University of Florence)

Abstract

Myosin-5B is one of three members of the myosin-5 family of actin-based molecular motors. Despite its fundamental role in recycling endosome trafficking and in collective actin network dynamics, the molecular mechanisms underlying its motility are inherently unknown. Here we combine single-molecule imaging and high-speed laser tweezers to dissect the mechanoenzymatic properties of myosin-5B. We show that a single myosin-5B moves processively in 36-nm steps, stalls at ~2 pN resistive forces, and reverses its directionality at forces >2 pN. Interestingly, myosin-5B mechanosensitivity differs from that of myosin-5A, while it is strikingly similar to kinesin-1. In particular, myosin-5B run length is markedly and asymmetrically sensitive to force, a property that might be central to motor ensemble coordination. Furthermore, we show that Ca2+ does not affect the enzymatic activity of the motor unit, but abolishes myosin-5B processivity through calmodulin dissociation, providing important insights into the regulation of postsynaptic cargoes trafficking in neuronal cells.

Suggested Citation

  • Lucia Gardini & Sarah M. Heissler & Claudia Arbore & Yi Yang & James R. Sellers & Francesco S. Pavone & Marco Capitanio, 2018. "Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05251-z
    DOI: 10.1038/s41467-018-05251-z
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    Cited by:

    1. C. Arbore & M. Sergides & L. Gardini & G. Bianchi & A. V. Kashchuk & I. Pertici & P. Bianco & F. S. Pavone & M. Capitanio, 2022. "α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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