The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack Journal Article

   


Authors: Miesenböck, G.; Rothman, J. E.
Article Title: The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack
Abstract: To explore how far into the Golgi stack the capacity to retrieve KDEL proteins extends, we have introduced an exogenous probe (the peptide YHPNSTCSEKDEL) into the TGN of living cells. For this purpose, a CHO cell line expressing a c-myc-tagged version of the transmembrane protein TGN38- which cycles between the TGN and the cell surface-was generated. The cells internalized peptides that were disulfide bonded to anti-myc antibodies and accumulated the peptide-antibody complexes in the TGN. Peptides released from these complexes underwent retrograde transport to the ER, as evidenced by the transfer of N-linked carbohydrate to their acceptor site. The KDEL-tagged glycopeptides (~10% of the endocytosed load) behaved like endogenous ER residents: they stayed intracellular, and their oligosaccharide side chains remained sensitive to endoglycosidase H. An option thus exists to extract ER residents even at the most distant pole of the Golgi stack, suggesting that sorting of resident from exported ER proteins may occur in a multistage process akin to fractional distillation.
Keywords: controlled study; unclassified drug; nonhuman; animal cell; complex formation; animalia; monoclonal antibody; endoplasmic reticulum; membrane protein; protein transport; mesna; oncogene c myc; endocytosis; glycopeptide; golgi complex; cho cell; protein glycosylation; transferase; polyclonal antibody; disulfide bond; tunicamycin; concanavalin a; dithiothreitol; oligosaccharyltransferase; priority journal; article; glycosidase
Journal Title: Journal of Cell Biology
Volume: 129
Issue: 2
ISSN: 0021-9525
Publisher: Rockefeller University Press  
Date Published: 1995-04-15
Start Page: 309
End Page: 319
Language: English
DOI: 10.1083/jcb.129.2.309
PUBMED: 7721936
PROVIDER: scopus
PMCID: PMC2199920
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028920154&doi=10.1083%2fjcb.129.2.309&partnerID=40&md5=afc28a2fe905190f810062267d644309
Notes: Article -- Export Date: 28 August 2018 -- Source: Scopus
Altmetric
What is Altmetric?
Citation Impact
What is Dimensions Citation Badge?
BMJ Impact Analytics
MSK Authors
  1. James E Rothman
    120 Rothman
  2. Gero A Miesenboeck
    17 Miesenboeck
Related MSK Work