Microtubule-binding Properties of Dynactin P150 Expedient for Dynein Motility.
From: Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Komaba 3-8-1, Meguro-ku, Tokyo 153-8902, Japan.
Biochemical and biophysical research communications
- Publish Date: Feb 2006
- ISSN: 0006-291X
- Volume: 340
- Issue: 1
- Pages: 23-8
- Medium: Print
- Language: English
- Citation (JAMA): Kobayashi Takuya, Shiroguchi Katsuyuki, Edamatsu Masaki, et al. Microtubule-binding Properties of Dynactin P150 Expedient for Dynein Motility.. Biochem. Biophys. Res. Commun. Feb 2006;340:23-8
Abstract
Dynactin is a hetero-oligomeric protein complex that has an important role in dynein-based intracellular transport. The expressed N-terminal fragments of dynactin p150 bound to microtubules in the ratio of one to one tubulin dimer, independent from the binding of dynein stalk head. Single molecule observation revealed that these fragments moved around on microtubules by Brownian motion. When the dynein-dynactin complex moves on microtubules, p150 can support dynein to maintain contact with microtubules and does not interfere with the motility of dynein, and thus, the dynein-dynactin complex can efficiently achieve long-distance carriage of the cargo.
Mesh Headings (Keywords): Binding Sites, Dynein ATPase, Microtubule-Associated Proteins, Microtubules, Molecular Motor Proteins, Motion, Protein Binding, Protein Conformation, Structure-Activity Relationship
Check for Full Text / PubMed Unique Identifier (PMID): 16343429
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