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Myosin VI: two distinct roles in endocytosis

Hasson, Tama·2003·Journal of Cell Science
DOI 10.1242/jcs.00669
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Abstract

Actin is found at the cortex of the cell where endocytosis occurs, but does it play a role in this essential process? Recent studies on the unconventional myosin, myosin VI, an actin-based molecular motor, provide compelling evidence that this myosin and therefore actin is involved in two distinct steps of endocytosis in higher eukaryotes: the formation of clathrin-coated vesicles and the movement of nascent uncoated vesicles from the actin-rich cell periphery to the early endosome. Three distinct adapter proteins - GIPC, Dab2 and SAP97 - that associate with the cargo-binding tail domain of myosin VI have been identified. These proteins may recruit myosin VI to its sites of action.

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  • Dab2 links clathrin-coated cargos containing transmembrane proteins with an NPXY motif to the myosin motor, facilitating their endocytosis and directional trafficking.

    “Thus, Dab2 links clathrin-coated cargos containing transmembrane proteins with an NPXY motif to the myosin motor, facilitating their endocytosis and directional trafficking”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Hasson, 2003

  • The C-terminus of Dab2 binds the myosin VI motor protein.

    “The C-terminus binds to the myosin VI motor protein (Inoue et al., 2002; Morris et al., 2002a; Hasson, 2003; Spudich et al., 2007).”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Hasson, 2003

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Metadata

Authors
Hasson, T.
Affiliations
Division of Biological Sciences, Section of Cell and Developmental Biology, University of California at San Diego, 2129 Bonner Hall, MC 0368,9500 Gilman Drive, La Jolla, CA 92093-0368, USA (e-mail: tama@ucsd.edu)
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2003-09-01
Volume
116
Issue
17
Pages
3453-3461
ISSN
  • 1477-9137
  • 0021-9533
DOI
10.1242/jcs.00669
Cited by
161
References
2
Language
en

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