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)peer-review

64 Citations (Scopus)
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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
Issue number3
Early online date26 Dec 2018
Publication statusPublished - 4 Mar 2019


  • Trafficking
  • Organelles


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