GSBS Student Publications

Title

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

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Physiology

Date

3-22-2002

Document Type

Article

Medical Subject Headings

Adaptor Proteins, Signal Transducing; *Adaptor Proteins, Vesicular Transport; Adenosine Triphosphatases; Animals; Genes, Tumor Suppressor; Humans; Kinetics; Mice; Microfilaments; Movement; Myosin Heavy Chains; Protein Structure, Tertiary; Proteins; Signal Transduction; Two-Hybrid System Techniques; Yeasts

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.

Rights and Permissions

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

DOI of Published Version

10.1006/bbrc.2002.6636

Related Resources

Link to article in PubMed

Journal Title

Biochemical and biophysical research communications

PubMed ID

11906161

Link to Full Text

Share

COinS