Over the last few years, the widely distributed family of reticulons (RTNs) is receiving renewed interest because of the implication of RTN4/Nogo in neurite regeneration. Four genes were identified in mammals and are referred to as RTN1, 2, 3 and the neurite outgrowth inhibitor RTN4/Nogo. In the present paper, we describe the existence of five new isoforms of RTN3 that differ in their N-termini, and analysed their tissue distribution and expression in neurons. We redefined the structure of human and murine rtn3 genes, and identified two supplementary exons that may generate up to seven putative isoforms arising by alternative splicing or differential promoter usage. We confirmed the presence of five of these isoforms at the mRNA and protein levels, and showed their preferential expression in the central nervous system. We analysed rtn3 expression in the cerebellum further, and observed increased levels of several of the RTN3 isoforms during cerebellum development and during in vitro maturation of cerebellar granule cells. This pattern of expression paralleled that shown by RTN4/Nogo isoforms. Specifically, RTN3A1 expression was down-regulated upon cell death of cerebellar granule neurons triggered by potassium deprivation. Altogether, our results demonstrate that the rtn3 gene generates multiple isoforms varying in their N-termini, and that their expression is tightly regulated in neurons. These findings suggest that RTN3 isoforms may contribute, by as yet unknown mechanisms, to neuronal survival and plasticity.
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Research Article|
December 14 2004
Tissue specificity and regulation of the N-terminal diversity of reticulon 3
Franck DI SCALA;
Franck DI SCALA
1
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
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Luc DUPUIS;
Luc DUPUIS
1
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
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Christian GAIDDON;
Christian GAIDDON
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
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Marc DE TAPIA;
Marc DE TAPIA
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
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Natasa JOKIC;
Natasa JOKIC
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
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Jose-Luis GONZALEZ DE AGUILAR;
Jose-Luis GONZALEZ DE AGUILAR
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
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Jean-Sébastien RAUL;
Jean-Sébastien RAUL
†Institut de Médecine Légale, 11 rue Humann, 67085 Strasbourg Cedex, France
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Bertrand LUDES;
Bertrand LUDES
†Institut de Médecine Légale, 11 rue Humann, 67085 Strasbourg Cedex, France
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Jean-Philippe LOEFFLER
Jean-Philippe LOEFFLER
2
*Laboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France
2To whom correspondence should be addressed (email loeffler@neurochem.u-strasbg.fr).
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Publisher: Portland Press Ltd
Received:
March 19 2004
Revision Received:
September 01 2004
Accepted:
September 07 2004
Accepted Manuscript online:
September 07 2004
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 385 (1): 125–134.
Article history
Received:
March 19 2004
Revision Received:
September 01 2004
Accepted:
September 07 2004
Accepted Manuscript online:
September 07 2004
Citation
Franck DI SCALA, Luc DUPUIS, Christian GAIDDON, Marc DE TAPIA, Natasa JOKIC, Jose-Luis GONZALEZ DE AGUILAR, Jean-Sébastien RAUL, Bertrand LUDES, Jean-Philippe LOEFFLER; Tissue specificity and regulation of the N-terminal diversity of reticulon 3. Biochem J 1 January 2005; 385 (1): 125–134. doi: https://doi.org/10.1042/BJ20040458
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