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2. HDAC3 is a molecular brake of the metabolic switch supporting white adipose tissue browning

Author

Alessandra Ferrari, Raffaella Longo, Erika Fiorino, Rui Silva, Nico Mitro, Gaia Cermenati, Federica Gilardi, Béatrice Desvergne, Annapaola Andolfo, Cinzia Magagnotti, Donatella Caruso, Emma De Fabiani, Scott W. Hiebert, and Maurizio Crestani

Subjects
Science
Abstract

Histone deacetylases, such as HDAC3, have been shown to alter cellular metabolism in various tissues. Here the authors show that HDAC3 regulates WAT metabolism by activating a futile cycle of fatty acid synthesis and oxidation, which supports WAT browning.

Published
2017
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3. Author Correction: Direct stimulation of ERBB2 highlights a novel cytostatic signaling pathway driven by the receptor Thr701 phosphorylation

Author

Chiara Brombin, Paola Bagnato, Annapaola Andolfo, Giuseppina De Feudis, Andrea Rabellino, Andrea Raimondi, Tiziana Daniele, Matthias Brand, Giovanni Tonon, Marco Gaviraghi, Alberta Locatelli, Carlo Tacchetti, Davide Mazza, Yosef Yarden, Luca Gianni, and Daniela Tosoni

Subjects
Receptor, ErbB-2, Science, Cell Line, Tumor, Medicine, Humans, Phosphorylation, Receptor, Author Correction, Extracellular Signal-Regulated MAP Kinases, Direct stimulation, Cell Proliferation, Multidisciplinary, business.industry, Receptor Protein-Tyrosine Kinases, Cytostatic Agents, Cell biology, Cell Transformation, Neoplastic, Signal transduction, business, Dimerization, Proto-Oncogene Proteins c-akt, Signal Transduction
Abstract

ERBB2 is a ligand-less tyrosine kinase receptor expressed at very low levels in normal tissues; when overexpressed, it is involved in malignant transformation and tumorigenesis in several carcinomas. In cancer cells, ERBB2 represents the preferred partner of other members of the ERBB receptor family, leading to stronger oncogenic signals, by promoting both ERK and AKT activation. The identification of the specific signaling downstream of ERBB2 has been impaired by the lack of a ligand and of an efficient way to selectively activate the receptor. In this paper, we found that antibodies (Abs) targeting different epitopes on the ERBB2 extracellular domain foster the activation of ERBB2 homodimers, and surprisingly induce a unique cytostatic signaling cascade promoting an ERK-dependent ERBB2 Thr

Published
2021

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