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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

DOC-2/DAB2 Is the Binding Partner of Myosin VI

Inoue, Akira, Sato, Osamu, Homma, Kazuaki, Ikebe, Mitsuo·2002·Biochemical and Biophysical Research Communications
DOI 10.1006/bbrc.2002.6636
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Abstract

Myosin VI is a molecular motor that moves processively along actin filaments and is believed to play a role in cargo movement in cells. Here we found that DOC-2/DAB2, a signaling molecule inhibiting the Ras cascade, binds to myosin VI at the globular tail domain. DOC-2/DAB2 binds stoichiometrically to myosin VI with one molecule per one myosin VI heavy chain. The C-terminal 122 amino acid residues of DOC-2/DAB2, containing the Grb2 binding site, is identified to be critical for the binding to myosin VI. Actin gliding assay revealed that the binding of DOC-2/DAB2 to myosin VI can support the actin filament gliding by myosin VI, suggesting that it can function as a myosin VI anchoring molecule. The C-terminal domain but not the N-terminal domain of DOC-2/DAB2 functions as a myosin VI anchoring site. The present findings suggest that myosin VI plays a role in transporting DOC-2/DAB2, a Ras cascade signaling molecule, thus involved in Ras signaling pathways.

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  • Dab2 probably plays an important role in targeting myosin VI to clathrin-coated vesicles.

    “Myosin VI is a component of some clathrin-coated vesicles (Buss et al., 2001) and Dab2 probably plays an important role in targeting this motor to the vesicle.”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Inoue et al., 2002

  • 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 Inoue et al., 2002

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Metadata

Authors
Inoue, A., Sato, O., Homma, K., & Ikebe, M.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2002-03
Volume
292
Issue
2
Pages
300-307
ISSN
0006-291X
DOI
10.1006/bbrc.2002.6636
Cited by
65
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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