The mitogaligin protein is addressed to the nucleus via a non-classical localization signal

Autor: Fabienne Brulé, Stéphane Charpentier, Lucile Mollet, Thierry Normand, Martine Dubois, Alain Legrand, Patrick Gonzalez, Pauline Robinet
Přispěvatelé: Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut de Mathématiques de Bordeaux (IMB), Université Bordeaux Segalen - Bordeaux 2-Université Sciences et Technologies - Bordeaux 1-Université de Bordeaux (UB)-Institut Polytechnique de Bordeaux (Bordeaux INP)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2009
Předmět:
Zdroj: Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2010, 392 (1), pp.53-57. ⟨10.1016/j.bbrc.2009.12.162⟩
ISSN: 1090-2104
0006-291X
DOI: 10.1016/j.bbrc.2009.12.162⟩
Popis: International audience; Mitogaligin, a protein encoded by galig, an internal cytotoxic gene of the galectin-3 locus, is mostly a mitochondrial protein. Mitochondrial targeting is due to an already identified mitochondrial localization signal. Interaction of mitogaligin with mitochondria leads to cytochrome c cytosolic leakage and ultimately to cell death. We have previously pointed out that mitogaligin can also be directed to the nucleus when the mitochondrial addressing signal is inactivated, indicating a possible dual intracellular localization of the protein. When expressed in the nucleus, mitogaligin exhibits also apoptotic properties leading to cell death. In this report, we show that nuclear addressing of mitogaligin depends on a sequence differing from classical signals containing basic, lysine or proline-tyrosine rich residues. The signal consists of a long sequence of amino acids residues based on a series of a short repetitive degenerated sequence.
Databáze: OpenAIRE