Characterization of the Teb4 ubiquitin ligase of type 2 deiodinase

Abstract

Event Abstract Back to Event Characterization of the Teb4 ubiquitin ligase of type 2 deiodinase Peter Egri1, Gabor Wittmann1, Csaba Fekete1, 2 and Balázs Gereben1* 1 Institute of Experimental Medicine, Hungarian Academy of Sciences, Hungary 2 Tufts-Medical Center, Diabetes, and Metabolism, United States Thyroid hormone, a highly potent differentiation factor plays a crucial role in the development and function of the central nervous system. In order to bind its receptor, the pro-hormone thyroxine (T4) has to be converted to T3 by the type 2 deiodinase selenoenzyme (D2). T3 generation by D2 is down-regulated via the ubiquitin/proteasomal system and Doa10 has recently been suggested as a D2 ubiquitin ligase (E3) in yeast. We studied the distribution of the mammalian Doa10 ortholog, TEB4 in rat tissues and in D2 expressing cells of the brain, namely tanycytes and astrocytes. TEB4 mRNA was detected both in D2 expressing and in non-expressing tissues including the brain, pituitary, liver, kidney, skeletal muscle, heart and brown adipose tissue, but not in the thyroid. This distribution was similar to that of the other D2 ubiquitin ligase WSB1. In the brain, in situ hybridization detected TEB4 expression in tanycytes in the wall of the third ventricle in the mediobasal hypothalamus. TEB4 expression in astrocytes was region-specific; GFAP positive astrocytes expressed TEB4 in the cerebellum, but not in other brain regions. However, strong TEB4 hybridization signal was observed in GFAP-negative cells in different brain regions. Our data demonstrated that similarly to WSB1, the morphological basis for TEB4 mediated regulation of T3 generation is present in hypothalamic tanycytes. However, D2 ubiquitination in astrocytes by TEB4 and WSB1 seems region-specific in the brain. In addition, the expression of TEB4 in non-D2 expressing cells suggests that D2 is not the only substrate of this E3 protein. Conference: 12th Meeting of the Hungarian Neuroscience Society, Budapest, Hungary, 22 Jan - 24 Jan, 2009. Presentation Type: Poster Presentation Topic: Homeostatic regulatory mechanisms Citation: Egri P, Wittmann G, Fekete C and Gereben B (2009). Characterization of the Teb4 ubiquitin ligase of type 2 deiodinase. Front. Syst. Neurosci. Conference Abstract: 12th Meeting of the Hungarian Neuroscience Society. doi: 10.3389/conf.neuro.01.2009.04.009 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: 25 Feb 2009; Published Online: 25 Feb 2009. * Correspondence: Balázs Gereben, Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary, gereben@koki.hu 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 Peter Egri Gabor Wittmann Csaba Fekete Balázs Gereben Google Peter Egri Gabor Wittmann Csaba Fekete Balázs Gereben Google Scholar Peter Egri Gabor Wittmann Csaba Fekete Balázs Gereben PubMed Peter Egri Gabor Wittmann Csaba Fekete Balázs Gereben 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.