ER-to-Golgi trafficking of procollagen in the absence of large carriers

Janine McCaughey, Nicola L Stevenson, Stephen Cross, David J Stephens*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)

16 Citations (Scopus)
272 Downloads (Pure)

Abstract

Secretion and assembly of collagen are fundamental to the function of the extracellular matrix. Defects in the assembly of a collagen matrix lead to pathologies including fibrosis and osteogenesis imperfecta. Owing to the size of fibril-forming procollagen molecules it is assumed that they are transported from the endoplasmic reticulum to the Golgi in specialized large COPII-dependent carriers. Here, analyzing endogenous procollagen and a new engineered GFP-tagged form, we show that transport to the Golgi occurs in the absence of large (>350 nm) carriers. Large GFP-positive structures were observed occasionally, but these were nondynamic, are not COPII positive, and are labeled with markers of the ER. We propose a short-loop model of COPII-dependent ER-to-Golgi traffic that, while consistent with models of ERGIC-dependent expansion of COPII carriers, does not invoke long-range trafficking of large vesicular structures. Our findings provide an important insight into the process of procollagen trafficking and reveal a short-loop pathway from the ER to the Golgi, without the use of large carriers.

Original languageEnglish
Pages (from-to)929-948
Number of pages20
JournalJournal of Cell Biology
Volume218
Issue number3
Early online date26 Dec 2018
DOIs
Publication statusPublished - 4 Mar 2019

Keywords

  • Trafficking
  • Organelles

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