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

Full description

Saved in:
Bibliographic Details
Published inThe Journal of biological chemistry Vol. 285; no. 11; pp. 8155 - 8162
Main Authors Seeger, Mark A., Rice, Sarah E.
Format Journal Article
LanguageEnglish
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
Online AccessGet full text

Cover

More Information
Summary: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. Binding is largely electrostatic in nature, and is facilitated by a region of basic amino acids in the tail and the acidic E-hook at the C terminus of tubulin. The tail binds to a site on tubulin that is independent of the head domain-binding site but overlaps with the binding site of the microtubule-associated protein Tau. Surprisingly, the kinesin tail domain stimulates microtubule assembly and stability in a manner similar to Tau. The biological function of this strong kinesin tail-microtubule interaction remains to be seen, but it is likely to play an important role in kinesin regulation due to the close proximity of the microtubule-binding region to the conserved regulatory and cargo-binding domains of the tail.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M109.068247