title: Alzheimer's disease-related protein hGas7b interferes with kinesin motility.
abstract: In the previous study, we reported the important properties of hGas7b (i) that binds to phospho-tau and facilitates microtubule polymerization and (ii) the level of hGas7b is very low in the brains of patients with Alzheimer's disease. These results led us to study the function of hGas7b in detail. We focused on the effect of hGas7b on microtubule dynamics in the absence of tau, on the assumption of healthy tau decrease in the brains of Alzheimer's disease. hGas7b binds to microtubule directly without tau, although this binding does not enhance microtubule polymerization. Excess hGas7b interferes with kinesin motility on microtubules. These results suggest that regulation to maintain an appropriate concentration of hGas7b is required for healthy neurotransmission.
authors.affiliation: Molecular Enzymology, Department of Molecular Cell Science, Graduate School of Agricultural Science, Tohoku University, Aoba, Sendai, Japan.
authors.forename: Masafumi
authors.initials: M
authors.lastname: Hidaka
authors.forename: Tomoe
authors.initials: T
authors.lastname: Koga
authors.forename: Aina
authors.initials: A
authors.lastname: Gotoh
authors.forename: Mariko
authors.initials: M
authors.lastname: Sanada
authors.forename: Keiko
authors.initials: K
authors.lastname: Hirose
authors.forename: Takafumi
authors.initials: T
authors.lastname: Uchida
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D016547:Kinesins / Q000378:metabolism*; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D058105:Polymerization
chemical_list: C114909:GAS7 protein, human; D009419:Nerve Tissue Proteins; D016547:Kinesins