COPII-coated membranes function as transport carriers of intracellular procollagen I

Author:

Gorur Amita12,Yuan Lin12,Kenny Samuel J.3,Baba Satoshi1,Xu Ke3ORCID,Schekman Randy12ORCID

Affiliation:

1. Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720

2. Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720

3. Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720

Abstract

The coat protein complex II (COPII) is essential for the transport of large cargo, such as 300-nm procollagen I (PC1) molecules, from the endoplasmic reticulum (ER) to the Golgi. Previous work has shown that the CUL3-KLHL12 complex increases the size of COPII vesicles at ER exit sites to more than 300 nm in diameter and accelerates the secretion of PC1. However, the role of large COPII vesicles as PC1 transport carriers was not unambiguously demonstrated. In this study, using stochastic optical reconstruction microscopy, correlated light electron microscopy, and live-cell imaging, we demonstrate the existence of mobile COPII-coated vesicles that completely encapsulate the cargo PC1 and are physically separated from ER. We also developed a cell-free COPII vesicle budding reaction that reconstitutes the capture of PC1 into large COPII vesicles. This process requires COPII proteins and the GTPase activity of the COPII subunit SAR1. We conclude that large COPII vesicles are bona fide carriers of PC1.

Funder

Gordon and Betty Moore Foundation

National Institutes of Health

Howard Hughes Medical Institute

University of California Berkeley

Miller Institute for Basic Research in Science

Lawrence Berkeley National Laboratory

National Science Foundation

Publisher

Rockefeller University Press

Subject

Cell Biology

Reference60 articles.

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