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• W2805364370 abstract "Abstract Secretion and assembly of collagen is 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 specialised large COPII-dependent carriers. Here, analysing endogenous procollagen and a new engineered GFP-tagged form, we show that transport to the Golgi occurs in the absence of large carriers. Large GFP-positive structures are observed occasionally but these are non-dynamic, are not COPII-positive, and label 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. Summary Trafficking of procollagen is essential for normal cell function. Here, imaging of GFP-tagged type I procollagen reveals that it is transported from the endoplasmic reticulum to the Golgi, without the use of large carriers." @default.
• W2805364370 created "2018-06-13" @default.
• W2805364370 creator A5004412496 @default.
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• W2805364370 creator A5087111646 @default.
• W2805364370 date "2018-06-05" @default.
• W2805364370 modified "2023-10-14" @default.
• W2805364370 title "ER-to-Golgi trafficking of procollagen in the absence of large carriers" @default.
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• W2805364370 doi "https://doi.org/10.1101/339804" @default.
• W2805364370 hasPublicationYear "2018" @default.
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