Proteomics of protein trafficking by in vivo tissue-specific labeling

Author:

Droujinine Ilia A.ORCID,Meyer Amanda S.ORCID,Wang DanORCID,Udeshi Namrata D.ORCID,Hu YanhuiORCID,Rocco David,McMahon Jill A.,Yang Rui,Guo JinJin,Mu Luye,Carey Dominique K.,Svinkina Tanya,Zeng Rebecca,Branon Tess,Tabatabai Areya,Bosch Justin A.,Asara John M.,Ting Alice Y.ORCID,Carr Steven A.,McMahon Andrew P.,Perrimon NorbertORCID

Abstract

AbstractConventional approaches to identify secreted factors that regulate homeostasis are limited in their abilities to identify the tissues/cells of origin and destination. We established a platform to identify secreted protein trafficking between organs using an engineered biotin ligase (BirA*G3) that biotinylates, promiscuously, proteins in a subcellular compartment of one tissue. Subsequently, biotinylated proteins are affinity-enriched and identified from distal organs using quantitative mass spectrometry. Applying this approach inDrosophila, we identify 51 muscle-secreted proteins from heads and 269 fat body-secreted proteins from legs/muscles, including CG2145 (human ortholog ENDOU) that binds directly to muscles and promotes activity. In addition, in mice, we identify 291 serum proteins secreted from conditional BirA*G3 embryo stem cell-derived teratomas, including low-abundance proteins with hormonal properties. Our findings indicate that the communication network of secreted proteins is vast. This approach has broad potential across different model systems to identify cell-specific secretomes and mediators of interorgan communication in health or disease.

Funder

Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada

U.S. Department of Health & Human Services | National Institutes of Health

Howard Hughes Medical Institute

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

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