期刊
JOURNAL OF CELL BIOLOGY
卷 216, 期 9, 页码 2691-2700出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201704056
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资金
- Spanish Ministry of Economy and Competitiveness through the program Centro de Excelencia Severo Ochoa [SEV-2012-0208]
- Centres de Recerca de Catalunya Program/Generalitat de Catalunya
- Spanish Ministry of Economy and Competitiveness [BFU2013-44188-P, CSD2009-00016]
- European Research Council [268692]
- European Union
- European Research Council (ERC) [268692] Funding Source: European Research Council (ERC)
The nutrient starvation-specific unconventional secretion of Acb1 in Saccharomyces cerevisiae requires ESCRT-I, -II, and -III and Grh1. In this study, we report that another signal sequence lacking cytoplasmic protein, superoxide dismutase 1 (SOD1), and its mutant form linked to amyotrophic lateral sclerosis (ALS), is also secreted by yeast upon nutrient starvation in a Grh1- and ESCRT-I-, -II-, and -III-dependent process. Our analyses reveal that a conserved diacidic motif (Asp-Glu) in these proteins is necessary for their export. Importantly, secretion of wild-type human SOD1 and the ALS-linked mutant in human cells also require the diacidic residues. Altogether, these findings reveal information encoded within the cytoplasmic proteins required for their unconventional secretion and provide a means to unravel the significance of the cytoplasmic versus the secreted form of mutant SOD1 in the pathology of ALS. We also propose how cells, based on a signal-induced change in cytoplasmic physiology, select a small pool of a subset of cytoplasmic proteins for unconventional secretion.
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