Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum

Chung Ling Lu, Steven Ortmeier, Jon Brudvig, Tamara Moretti, Jacob Cain, Simeon A. Boyadjiev, Jill M. Weimer, Jinoh Kim

Research output: Contribution to journalArticlepeer-review

Abstract

SEC24 is mainly involved in cargo sorting during COPII vesicle assembly. There are four SEC24 paralogs (A–D) in vertebrates, which are classified into two subgroups (SEC24A/B and SEC24C/D). Pathological mutations in SEC24D cause osteogenesis imperfecta with craniofacial dysplasia in humans. sec24d mutant fish also recapitulate the phenotypes. Consistent with the skeletal phenotypes, the secretion of collagen was severely defective in mutant fish, emphasizing the importance of SEC24D in collagen secretion. However, SEC24D patient-derived fibroblasts show only a mild secretion phenotype, suggesting tissue-specificity in the secretion process. Using Sec24d KO mice and cultured cells, we show that SEC24A and SEC24B also contribute to endoplasmic reticulum (ER) export of procollagen. In contrast, fibronectin 1 requires either SEC24C or SEC24D for ER export. On the basis of our results, we propose that procollagen interacts with multiple SEC24 paralogs for efficient export from the ER, and that this is the basis for tissue-specific phenotypes resulting from SEC24 paralog deficiency.

Original languageEnglish (US)
JournalTraffic
DOIs
StateAccepted/In press - 2021
Externally publishedYes

Keywords

  • collagen
  • COPII
  • endoplasmic reticulum
  • SEC24
  • secretion
  • tissue specificity

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint

Dive into the research topics of 'Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum'. Together they form a unique fingerprint.

Cite this