Title

DOC-2/DAB2 is the binding partner of myosin VI

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Physiology

Publication Date

2002-03-22

Document Type

Article

Disciplines

Life Sciences | Medicine and Health Sciences

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.

DOI of Published Version

10.1006/bbrc.2002.6636

Source

Biochem Biophys Res Commun. 2002 Mar 29;292(2):300-7. Link to article on publisher's site

Journal/Book/Conference Title

Biochemical and biophysical research communications

Related Resources

Link to article in PubMed

PubMed ID

11906161

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