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- Title
Spatial proteomics defines the content of trafficking vesicles captured by golgin tethers.
- Authors
Shin, John J. H.; Crook, Oliver M.; Borgeaud, Alicia C.; Cattin-Ortolá, Jérôme; Peak-Chew, Sew Y.; Breckels, Lisa M.; Gillingham, Alison K.; Chadwick, Jessica; Lilley, Kathryn S.; Munro, Sean
- Abstract
Intracellular traffic between compartments of the secretory and endocytic pathways is mediated by vesicle-based carriers. The proteomes of carriers destined for many organelles are ill-defined because the vesicular intermediates are transient, low-abundance and difficult to purify. Here, we combine vesicle relocalisation with organelle proteomics and Bayesian analysis to define the content of different endosome-derived vesicles destined for the trans-Golgi network (TGN). The golgin coiled-coil proteins golgin-97 and GCC88, shown previously to capture endosome-derived vesicles at the TGN, were individually relocalised to mitochondria and the content of the subsequently re-routed vesicles was determined by organelle proteomics. Our findings reveal 45 integral and 51 peripheral membrane proteins re-routed by golgin-97, evidence for a distinct class of vesicles shared by golgin-97 and GCC88, and various cargoes specific to individual golgins. These results illustrate a general strategy for analysing intracellular sub-proteomes by combining acute cellular re-wiring with high-resolution spatial proteomics. The vesicles that transport proteins between intracellular organelles are small, short-lived, and elusive. Here, the authors show that capture of these vesicles through relocalizing tethers to mitochondria allows their contents to be characterised by organelle proteomics.
- Subjects
PROTEOMICS; CARRIER proteins; MEMBRANE proteins; BAYESIAN analysis; ORGANELLES; COATED vesicles; MITOCHONDRIA; ENDOCYTOSIS
- Publication
Nature Communications, 2020, Vol 11, Issue 1, pN.PAG
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-020-19840-4