Alzheimer's disease-related protein hGas7b interferes with kinesin motility

Masafumi Hidaka, Tomoe Koga, Aina Gotoh, Mariko Sanada, Keiko Hirose, Takafumi Uchida

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)593-598
Number of pages6
JournalJournal of biochemistry
Volume151
Issue number6
DOIs
Publication statusPublished - 2012 Jun 1

Keywords

  • cryo-EM
  • hGas7b
  • kinesin
  • microtubule
  • motility

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Alzheimer's disease-related protein hGas7b interferes with kinesin motility'. Together they form a unique fingerprint.

Cite this