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Regulation of class V myosin

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Abstract

Class V myosin (myosin-5) is a molecular motor that functions as an organelle transporter. The activation of myosin-5′s motor function has long been known to be associated with a transition from the folded conformation in the off-state to the extended conformation in the on-state, but only recently have we begun to understand the underlying mechanism. The globular tail domain (GTD) of myosin-5 has been identified as the inhibitory domain and has recently been shown to function as a dimer in regulating the motor function. The folded off-state of myosin-5 is stabilized by multiple intramolecular interactions, including head–GTD interactions, GTD–GTD interactions, and interactions between the GTD and the C-terminus of the first coiled-coil segment. Any cellular factor that affects these intramolecular interactions and thus the stability of the folded conformation of myosin-5 would be expected to regulate myosin-5 motor function. Both the adaptor proteins of myosin-5 and Ca2+ are potential regulators of myosin-5 motor function, because they can destabilize its folded conformation. A combination of these regulators provides a versatile scheme in regulating myosin-5 motor function in the cell.

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Abbreviations

CaM:

Calmodulin

EFBD:

The exon-F binding domain

ELC:

Essential light chain

GTBD:

GTD-binding domain

GTD:

Globular tail domain

GTBM:

GTD-binding motif

Mlph:

Melanophilin

myosin-5:

Class V myosin

Myo5a:

Vertebrate myosin-5a

Myo5b:

Vertebrate myosin-5b

Myo5c:

Vertebrate myosin-5c

DmMyo5:

Drosophila myosin-5

Myo2p:

The budding yeast class V myosin Myo2p

Myo4p:

The budding yeast class V myosin Myo4p

Myo51:

The fission yeast class V myosin Myo51

Myo52:

The fission yeast class V myosin Myo52

RH1/2:

RILP-homology region-1/-2

Rilp:

Rab interacting lysosomal protein

Rilpl1/2:

Rab interacting lysosomal protein like protein 1/2

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Acknowledgements

This work was supported by the National Basic Research Program of China (2013CB932802) and the National Natural Science Foundation of China (31470791 and 31171367).

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Author notes

  1. Ning Zhang and Lin-Lin Yao contributed equally.

Authors and Affiliations

  1. Group of Cell Motility and Muscle Contraction, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing, 100101, China

    Ning Zhang, Lin-Lin Yao & Xiang-dong Li

  2. University of Chinese Academy of Sciences, Beijing, 100049, China

    Xiang-dong Li

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  1. Ning Zhang
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Zhang, N., Yao, LL. & Li, Xd. Regulation of class V myosin. Cell. Mol. Life Sci. 75, 261–273 (2018). https://doi.org/10.1007/s00018-017-2599-5

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  • DOI: https://doi.org/10.1007/s00018-017-2599-5

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