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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Shin JJH,Crook OM,Borgeaud AC,Cattin-Ortolá J,Peak-Chew SY,Breckels LM,Gillingham AK,Chadwick J,Lilley KS,Munro Sdoi
10.1038/s41467-020-19840-4subject
Has Abstractpub_date
2020-11-25 00:00:00pages
5987issue
1issn
2041-1723pii
10.1038/s41467-020-19840-4journal_volume
11pub_type
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