Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c.

Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Research Abstract Details 

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Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Abstract Text:

Jawdat Al-Bassam,Benoit Roger,Shelley Halpain,Ronald A Milligan,

Microtubule based motors like conventional kinesin (Kinesin-1) and Unc104 (Kinesin-3), and classical microtubule associated proteins (MAPs), including MAP2, are intimately involved in neurite formation and organelle transport. The processive motility of both these kinesins involves weak microtubule interactions in the ADP-bound states. Using cosedimentation assays, we have investigated these weak interactions and characterized their inhibition by MAP2c. We show that Unc104 binds microtubules with five-fold weaker affinity and two-fold higher stoichiometry compared with conventional kinesin. Unc104 and conventional kinesin binding affinities are primarily dependent on positively charged residues in the Unc104 K-loop and conventional kinesin neck coiled-coil and removal of these residues affects Unc104 and conventional kinesin differently. We observed that MAP2c acts primarily as a competitive inhibitor of Unc104 but a mixed inhibitor of conventional kinesin. Our data suggest a specific model in which MAP2c differentially interferes with each kinesin motor by inhibiting its weak attachment to the tubulin C-termini. This is reminiscent of the defects we have observed in Unc104 and kinesin mutants in which the positively charged residues in K-loop and neck coiled-coil domains were removed.

Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Publishing Authors By Initials

J Al-Bassam,B Roger,S Halpain,RA Milligan,

For similar proteins: nerve tissue proteins research abstracts see: proteins: nerve tissue proteins research

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Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Cell motility and the cytoskeleton

VOLUME: 64

Page Numbers: 377-89

Journal Abbreviation:

ISSN: 0886-1544

DAY: 3

MONTH: May

YEAR: 2007

Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8605339

Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Keywords Mesh Terms:

KEYWORDS: Nerve Tissue Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Information

Substance Name: Kinesin

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c.

AFFILIATION: Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Country: United States

AGENCY: United States NIMH

GRANT: MH50861

ACRONYM: MH

MEDLINETA: Cell Motil Cytoskeleton

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