Microtubule-associated Protein-like Binding of the Kinesin-1 Tail to Microtubules

• Published in: The Journal of biological chemistry Vol. 285; no. 11; pp. 8155 - 8162
• Main Authors: Seeger, Mark A., Rice, Sarah E.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 12.03.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Allosteric Regulation; Biophysics; Circular Dichroism; Cytoskeleton/Microtubules; Electrochemistry; Enzymes/Allosteric Regulation; Fluorescence Polarization; Humans; Kinesin - chemistry; Kinesin - genetics; Kinesin - metabolism; Methods/Electron Microscopy; Methods/Fluorescence; Microscopy, Electron; Microtubule-Associated Proteins - metabolism; Microtubules - metabolism; Molecular Biophysics; Molecular Motors/Kinesin; Mutagenesis; Protein Binding - physiology; Protein Structure, Tertiary; tau Proteins - metabolism; Enzymes/Allosteric Regulation; Molecular Motors/Kinesin; Biophysics; Methods/Electron Microscopy; Methods/Fluorescence; Cytoskeleton/Microtubules

The kinesin-1 molecular motor contains an ATP-dependent microtubule-binding site in its N-terminal head domain and an ATP-independent microtubule-binding site in its C-terminal tail domain. Here we demonstrate that a kinesin-1 tail fragment associates with microtubules with submicromolar affinity. B...