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A di-acidic motif targets cytoplasmic proteins for unconventional protein secretion

View ORCID ProfileDavid Cruz-Garcia, View ORCID ProfileNathalie Brouwers, View ORCID ProfileJuan M. Duran, View ORCID ProfileAmy J. Curwin, View ORCID ProfileVivek Malhotra
doi: https://doi.org/10.1101/122028
David Cruz-Garcia
1Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain
2Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain
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Nathalie Brouwers
1Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain
2Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain
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Juan M. Duran
1Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain
2Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain
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Amy J. Curwin
1Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain
2Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain
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Vivek Malhotra
1Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain
2Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain
3Institució Catalana de Recerca i Estudis Avançats (ICREA), 08010 Barcelona, Spain
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  • For correspondence: vivek.malhotra@crg.eu
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Abstract

We previously reported that Acb1, a cytoplasmic protein in Saccharomyces cerevisiae that cannot enter the endoplasmic reticulum (ER), was secreted upon nutrient starvation by a Vps4 independent, but ESCRT-I, -II and -III and Grh1 dependent pathway (Curwin et al., 2016). Here, we report that the same conditions result in secretion of another signal sequence lacking protein, superoxide dismutase 1 (SOD1). Similar to Acb1, SOD1 export requires Grh1 and a subset of ESCRT components. Importantly, our analysis reveals the existence of a conserved di-acidic motif (Asp-Glu) in SOD1 and Acb1 that is required for their respective export. This sequence is different from the di-acidic motif (Asp-X-Glu) necessary for export of transmembrane proteins from the ER. We propose that the Asp-Glu sequence acts as a targeting motif for the entry of SOD1 and Acb1, and likely many other proteins, upon nutrient starvation into a common albeit ER-Golgi independent pathway of secretion.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted March 29, 2017.
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A di-acidic motif targets cytoplasmic proteins for unconventional protein secretion
David Cruz-Garcia, Nathalie Brouwers, Juan M. Duran, Amy J. Curwin, Vivek Malhotra
bioRxiv 122028; doi: https://doi.org/10.1101/122028
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A di-acidic motif targets cytoplasmic proteins for unconventional protein secretion
David Cruz-Garcia, Nathalie Brouwers, Juan M. Duran, Amy J. Curwin, Vivek Malhotra
bioRxiv 122028; doi: https://doi.org/10.1101/122028

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