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Deciphering the tissue specificity of the protein secretory pathway in humans

View ORCID ProfileAmir Feizi, Francesco Gatto, View ORCID ProfileMathias Uhlen, Jens Nielsen
doi: https://doi.org/10.1101/070870
Amir Feizi
1Department of Biology and Biological Engineering, Kemivägen 10, Chalmers University of Technology, SE41296 Gothenburg, Sweden
2Novo Nordisk Foundation Center for Biosustainability, Chalmers University of Technology, SE41296 Gothenburg, Sweden
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Francesco Gatto
1Department of Biology and Biological Engineering, Kemivägen 10, Chalmers University of Technology, SE41296 Gothenburg, Sweden
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Mathias Uhlen
2Novo Nordisk Foundation Center for Biosustainability, Chalmers University of Technology, SE41296 Gothenburg, Sweden
3Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK2970 Hørsholm, Denmark
4Science for Life Laboratory, Royal Institute of Technology, SE-17121 Stockholm, Sweden
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Jens Nielsen
1Department of Biology and Biological Engineering, Kemivägen 10, Chalmers University of Technology, SE41296 Gothenburg, Sweden
2Novo Nordisk Foundation Center for Biosustainability, Chalmers University of Technology, SE41296 Gothenburg, Sweden
3Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK2970 Hørsholm, Denmark
4Science for Life Laboratory, Royal Institute of Technology, SE-17121 Stockholm, Sweden
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Abstract

Proteins that are components of the secretory machinery form a cellular pathway of paramount importance for physiological regulation, development and function of human tissues. Consistently, most secretory pathway components are ubiquitously expressed in all tissues. At the same time, recent studies identified that the largest fraction of tissue-specific proteins consists of secreted and membrane proteins and not intracellular proteins. This suggests that the secretory pathway is distinctively regulated in a tissue-specific fashion. However, a systematic analysis on how the protein secretory pathway is tuned in different tissues is lacking, and it is even largely unexplored if the secretome and membrane proteome differs in, for example, posttranslation modifications across tissues. Here, analyzing publically available transcriptome data across 30 human tissues, we discovered the expression level of key components previously categorized as housekeeping proteins were specifically over-expressed in a certain tissue compared with the average expression of their corresponding secretory pathway subsystem (e.g. protein folding). These extreme genes define an exceptional fine-tuning in specific subnetworks, which neatly differentiated for example the pancreas and liver from 30 other tissues. Moreover, the subnetwork expression tuning correlated with the nature and number of post translational modification sites in the pancreas or liver-specific secretome and membrane proteome. These patterns were recurrently observed also in other tissues, like the blood, the brain and the skeletal muscle. These findings conciliate both the housekeeping and tissue-specific nature of the protein secretory pathway, which we attribute to a fine-tuned regulation of defined subnetworks in order to support the diversity of secreted proteins and their modifications.

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Posted August 24, 2016.
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Deciphering the tissue specificity of the protein secretory pathway in humans
Amir Feizi, Francesco Gatto, Mathias Uhlen, Jens Nielsen
bioRxiv 070870; doi: https://doi.org/10.1101/070870
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Deciphering the tissue specificity of the protein secretory pathway in humans
Amir Feizi, Francesco Gatto, Mathias Uhlen, Jens Nielsen
bioRxiv 070870; doi: https://doi.org/10.1101/070870

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