SEC23-SEC31 the interface plays critical role for export of procollagen from the endoplasmic reticulum

Sun Don Kim, Kanika Bajaj Pahuja, Mariella Ravazzola, Joonsik Yoon, Simeon A. Boyadjiev, Susan Hammamoto, Randy Schekman, Lelio Orci, Jinoh Kim

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


COPII proteins are essential for exporting most cargo molecules from the endoplasmic reticulum. The membrane-facing surface of the COPII proteins (especially SEC23-SEC24) interacts directly or indirectly with the cargo molecules destined for exit. As we characterized the SEC23A mutations at the SEC31 binding site identified from patients with cranio-lenticulo-sutural dysplasia, we discovered that the SEC23-SEC31 interface can also influence cargo selection. Remarkably, M702V SEC23A does not compromise COPII assembly, vesicle size, and packaging of cargo molecules into COPII vesicles that we have tested but induces accumulation of procollagen in the endoplasmic reticulum when expressed in normal fibroblasts. We observed that M702V SEC23A activates SAR1B GTPase more than wildtype SEC23A when SEC13-SEC31 is present, indicating that M702V SEC23A causes premature dissociation of COPII from the membrane. Our results indicate that a longer stay of COPII proteins on the membrane is required to cargo procollagen than other molecules and suggest that the SEC23-SEC31 interface plays a critical role in capturing various cargo molecules.

Original languageEnglish (US)
Pages (from-to)10134-10144
Number of pages11
JournalJournal of Biological Chemistry
Issue number13
StatePublished - Mar 23 2012
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology


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