Phosphorylation and isoform expression of microtubule-associated protein tau are regulated independently in the mouse brain

Abstract

Event Abstract Back to Event Phosphorylation and isoform expression of microtubule-associated protein tau are regulated independently in the mouse brain Dilina Tuerde1*, Taeko Kimura1, Tomohiro Miyasaka2, Akiko Asada1, Kanae Ando1, Taro Saito1 and Shin-Ichi Hisanaga1* 1 Tokyo Metropolitan University, Department of Biological Sciences, Japan 2 Doshisha University, Faculty of Life and Medical Sciences Neuropathology, Japan Tau is a microtubule-associated protein, mainly expressed in axon of neurons. There are 6 isoforms in tau, which are produced by alternative mRNA splicing of N-terminal insertions and C-terminal microtubule-binding repeats. The C-terminal splicing produces 3-repeat (3R) and 4-repeart (4R) tau with different microtubule-binding ability. It is shown that isoforms and phosphorylation of tau change during neuronal development. In mouse brain 3R tau isoforms are expressed in embryonic and early postnatal days and replaced with 4R tau until postnatal day 20 (P20). Early postnatal tau resembles that of Alzheimer`s disease in their high phosphorylation states. Thus, it is important to understand the mechanism of highly phosphorylated postnatal tau. However, it is not entirely known how the changes in isoforms and phosphorylation of tau are regulated and related to each other. In order to address this question, we used Phos-tag SDS-PAGE, in which phosphorylated proteins are shifted upward remarkably depending on the number and site of phosphorylation. Phosphorylation of tau drops with the decrease in 3R tau expression during postnatal day 5 (P5) to 18 (P18). In contrast, 4R tau, whose expression began at around P9 and was not highly phosphorylated even when 3R tau was phosphorylated. Phosphorylation of 4R tau changed around P24, one week after 3R tau completed the change in phosphorylation. We also examined phosphorylation of human 3R tau which was knocked in mouse tau locus. Human 3R tau changed phosphorylation states at P20, slightly delayed after mouse tau even though its expression levels did not change. We also studied phosphorylation of tau in several brain regions, cerebral cortex, cerebellum, hippocampus and olfactory bulb. Tau was phosphorylated higher in olfactory bulb than other areas with stronger expression of 3R tau. Keywords: Brain, Phosphorylation, in vivo, neurone, protein Conference: 14th Meeting of the Asian-Pacific Society for Neurochemistry, Kuala Lumpur, Malaysia, 27 Aug - 30 Aug, 2016. Presentation Type: Poster Presentation Session Topic: 14th Meeting of the Asian-Pacific Society for Neurochemistry Citation: Tuerde D, Kimura T, Miyasaka T, Asada A, Ando K, Saito T and Hisanaga S (2016). Phosphorylation and isoform expression of microtubule-associated protein tau are regulated independently in the mouse brain. Conference Abstract: 14th Meeting of the Asian-Pacific Society for Neurochemistry. doi: 10.3389/conf.fncel.2016.36.00125 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 04 Aug 2016; Published Online: 11 Aug 2016. * Correspondence: Ms. Dilina Tuerde, Tokyo Metropolitan University, Department of Biological Sciences, Hachioji-shi, Tokyo, Japan, dilnara0616@gmail.com Dr. Shin-Ichi Hisanaga, Tokyo Metropolitan University, Department of Biological Sciences, Hachioji-shi, Tokyo, Japan, Shin-ichi.Hisanaga@frontiersin.org Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Dilina Tuerde Taeko Kimura Tomohiro Miyasaka Akiko Asada Kanae Ando Taro Saito Shin-Ichi Hisanaga Google Dilina Tuerde Taeko Kimura Tomohiro Miyasaka Akiko Asada Kanae Ando Taro Saito Shin-Ichi Hisanaga Google Scholar Dilina Tuerde Taeko Kimura Tomohiro Miyasaka Akiko Asada Kanae Ando Taro Saito Shin-Ichi Hisanaga PubMed Dilina Tuerde Taeko Kimura Tomohiro Miyasaka Akiko Asada Kanae Ando Taro Saito Shin-Ichi Hisanaga Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.