Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA.

作者：Yoshimitsu Kanai, Reika Deja Takemura, Takeshi Oshima, Hajime Mori, Yasuo Ihara, Masashi Yanagisawa, Tsutomu Masaki, Nobutaka Hirokawa · 发表于：The Journal of Cell Biology · 年份：1989 · DOI：10.1083/jcb.109.3.1173 · 被引用次数：359 · 研究领域：Alzheimer's disease research and treatments、Protein Structure and Dynamics、Prion Diseases and Protein Misfolding

Tau proteins are a class of low molecular mass microtubule-associated proteins that are specifically expressed in the nervous system. A cDNA clone of adult rat tau was isolated and sequenced. To analyze functions of tau proteins in vivo, we carried out transfection experiments. A fibroblast cell line, which was transfected with the cDNA, expressed three bands of tau, while six bands were expressed in rat brain. After dephosphorylation, one of the three bands disappeared, demonstrating directly that phosphorylation was involved in the multiplicity of tau. Morphologically, we observed a thick bundle formation of microtubules in the transiently and stably tau-gene-transfected cells. In addition, we found that the production of tubulin was prominently enhanced in the stably transfected cells. Thus, we suppose that tau proteins promote polymerization of tubulin, form bundles of microtubules in vivo, and play important roles in growing and maintaining nerve cell processes.