TY - JOUR
T1 - A dynamic Dab2 keeps myosin VI stable on track
AU - Cirilo, Joseph A.
AU - Yengo, Christopher M.
N1 - Funding Information:
Funding and additional information—The work was supported by NIH grants to C. M. Y. (HL127699, HL150953) and a research supplement to J. A. C. (HL150953-01S1). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
Publisher Copyright:
© 2021 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
PY - 2021/1/1
Y1 - 2021/1/1
N2 - Myosins are actin-based motor proteins known to perform a variety of different mechanical tasks in cells including transporting cargo, generating tension, and linking the cytoskeleton and membrane. Myosins that function as transporters often form complexes with adaptor proteins and vesicular membranes, making it unclear how they transport their cargo through the actin cytoskeletal network. Rai et al. now use single-molecule kinetics, FRET, and DNA origami scaffolds that mimic motor-adaptor complexes to reveal that the myosin VI-Dab2 complex, which is held together weakly and turns over rapidly, can facilitate processive transport without disruption of the cytoskeleton.
AB - Myosins are actin-based motor proteins known to perform a variety of different mechanical tasks in cells including transporting cargo, generating tension, and linking the cytoskeleton and membrane. Myosins that function as transporters often form complexes with adaptor proteins and vesicular membranes, making it unclear how they transport their cargo through the actin cytoskeletal network. Rai et al. now use single-molecule kinetics, FRET, and DNA origami scaffolds that mimic motor-adaptor complexes to reveal that the myosin VI-Dab2 complex, which is held together weakly and turns over rapidly, can facilitate processive transport without disruption of the cytoskeleton.
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U2 - 10.1016/j.jbc.2021.100640
DO - 10.1016/j.jbc.2021.100640
M3 - Review article
C2 - 34237899
AN - SCOPUS:85105336105
SN - 0021-9258
VL - 296
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
M1 - 100640
ER -