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

  Articoli su Riviste JCR/ISI  (anno 2018)

Autori:  Gardini L., Heissler S.M., Arbore C., Yang Y., Sellers J. R., Pavone FS., Capitanio M

Affiliazione Autori:  [Gardini, Lucia; Arbore, Claudia; Pavone, Francesco S.; Capitanio, Marco] Univ Florence, LENS European Lab Nonlinear Spect, Via Nello Carrara 1, I-50019 Sesto Fiorentino, Italy. [Gardini, Lucia; Pavone, Francesco S.] CNR, Natl Inst Opt, Largo Fermi 6, I-50125 Florence, Italy. [Heissler, Sarah M.; Yang, Yi; Sellers, James R.] NHLBI, Lab Mol Physiol, NIH, Bldg 10, Bethesda, MD 20892 USA. [Arbore, Claudia; Pavone, Francesco S.; Capitanio, Marco] Univ Florence, Dept Phys & Astron, Via Sansone 1, I-50019 Sesto Fiorentino, Italy. [Yang, Yi] Hunan Agr Univ, Hunan Prov Key Lab Prot Engn Anim Vaccines, Changsha 410128, Hunan, Peoples R China.

Riassunto:   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 similar to 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.

Volume n.:  9      Pagine da: 2844-1  a: 2844-12
DOI: 10.1038/s41467-018-05251-z

   *Citazioni: 1
data tratti da "WEB OF SCIENCE" (marchio registrato di Thomson Reuters) ed aggiornati a:  19/05/2019

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