Myosin-I molecular motors at a glance

McIntosh, Betsy B.; Ostap, E. Michael

doi:10.1242/jcs.186403

Cited by 110 publications

(115 citation statements)

References 135 publications

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“…Eight class I myosins are expressed in human and mice, encompassing six short‐tailed (Myo1a, Myo1b, Myo1c, Myo1d, Myo1g, and Myo1h) and two long‐tailed (Myo1e and Myo1f) myosins . Both short‐tailed and long‐tailed myosins have a TH1 (tail homology) domain enriched with basic amino acids, thus permitting its interaction with the plasma membrane.…”

Section: Class I Myosinsmentioning

confidence: 99%

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Class I myosins: Highly versatile proteins with specific functions in the immune system

Girón-Pérez

Piedra-Quintero

Santos-Argumedo

2019

Journal of Leukocyte Biology

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Connections established between cytoskeleton and plasma membrane are essential in cellular processes such as cell migration, vesicular trafficking, and cytokinesis. Class I myosins are motor proteins linking the actin‐cytoskeleton with membrane phospholipids. Previous studies have implicated these molecules in cell functions including endocytosis, exocytosis, release of extracellular vesicles and the regulation of cell shape and membrane elasticity. In immune cells, those proteins also are involved in the formation and maintenance of immunological synapse‐related signaling. Thus, these proteins are master regulators of actin cytoskeleton dynamics in different scenarios. Although the localization of class I myosins has been described in vertebrates, their functions, regulation, and mechanical properties are not very well understood. In this review, we focused on and summarized the current understanding of class I myosins in vertebrates with particular emphasis in leukocytes.

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Section: Class I Myosinsmentioning

confidence: 99%

“…Schizosaccharomyces pombe (Myo1p), Saccharomyces cerevisiae (myo3p and myo5p), and Dictyostelium discoideum (MyoA, MyoE, MyoF, MyoB, MyoC, MyoD, and MyoH) have some paralogs of short and long tail myosins . MyoA, MyoE, MyoF, contain a TH1 region similar to Myo1c and Myo1g …”

Section: Class I Myosinsmentioning

confidence: 99%

Class I myosins: Highly versatile proteins with specific functions in the immune system

Girón-Pérez

Piedra-Quintero

Santos-Argumedo

2019

Journal of Leukocyte Biology

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“…The most prominent was myosin-Ic (Myo1c) (Fig. 4b), a member of class I myosin molecular motors, involved in regulating membrane tension, cell adhesion, and actin architecture 27 . Co-immunoprecipitation experiments confirmed that Myo1c associated with C-terminally-truncated, but also full length iASPP ( Fig.…”

Section: Myo1c Is a Partner Of Iaspp Involved In Spindle Positioningmentioning

confidence: 99%

iASPP contributes to cortex rigidity, astral microtubule capture and mitotic spindle positioning

Mangon

Salaün

Bouali

et al. 2019

Preprint

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The microtubule plus-end binding protein EB1 is the core of a complex protein network which regulates microtubule dynamics during important biological processes such as cell motility and mitosis. We found that iASPP, an inhibitor of p53 and predicted regulatory subunit of the PP1 phosphatase, associates with EB1 at microtubule plus-ends via a SxIP motif. iASPP silencing or mutation of the SxIP motif led to defective microtubule capture at the leading edge of migrating cells, and at the cortex of mitotic cells leading to abnormal positioning of the mitotic spindle. These effects were recapitulated by the knockdown of Myosin-Ic (Myo1c), identified as a novel partner of iASPP. Moreover, iASPP or Myo1c knockdown cells failed to round up during mitosis because of defective cortical rigidity. We propose that iASPP, together with EB1 and Myo1c, contributes to mitotic cell cortex rigidity, allowing astral microtubule capture and appropriate positioning of the mitotic spindle.

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“…Class I myosins are actin-binding motor proteins that typically function at sites of actin-based membrane deformation during cell shape changes. Humans have 8 class I myosins (Myo1a-h), whose expression and function differs across tissues (1). All class I myosins contain an Nterminal motor domain, a neck region that binds calmodulin or calmodulin-like light chains, and a short membrane-binding tail.…”

Section: Introductionmentioning

confidence: 99%

Human Myosin 1e tail but not motor domain replaces fission yeast Myo1 domains to support myosin-I function during endocytosis

Barger

James

Pellenz

et al. 2019

Preprint

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In both unicellular and multicellular organisms, long-tailed class I myosins function in clathrin-mediated endocytosis. Myosin 1e (Myo1e) in vertebrates and Myo1 in fission yeast have similar domain organization, yet whether these proteins or their individual protein domains are functionally interchangeable remains unknown. In an effort to assess functional conservation of class I myosins, we tested whether human Myo1e could replace Myo1 in fission yeast Schizosaccharomyces pombe and found that it was unable to substitute for yeast Myo1. To determine if any individual protein domain is responsible for the inability of Myo1e to function in yeast, we created human-yeast myosin-I chimeras. By functionally testing these chimeric myosins in vivo, we concluded that the Myo1e motor domain is unable to function in yeast, even when combined with the yeast Myo1 tail and a full complement of yeast regulatory light chains. Conversely, the Myo1e tail, when attached to the yeast Myo1 motor domain, supports localization to actin patches and partially rescues the endocytosis defect in myo1Δ cells. Further dissection showed that both the TH1 and TH2-SH3 domains in the human Myo1e tail are required for localization and function of chimeric myosin-I at endocytic sites. Overall, this study provides insights into the role of individual myosin-I domains, expands the utility of fission yeast as a simple model system to study the effects of disease-associated MYO1E mutations, and supports a model of co-evolution between a myosin motor and its actin track.

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Myosin-I molecular motors at a glance

Cited by 110 publications

References 135 publications

Class I myosins: Highly versatile proteins with specific functions in the immune system

Class I myosins: Highly versatile proteins with specific functions in the immune system

iASPP contributes to cortex rigidity, astral microtubule capture and mitotic spindle positioning

Human Myosin 1e tail but not motor domain replaces fission yeast Myo1 domains to support myosin-I function during endocytosis

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