Intracellular mechanisms of molecular recognition and sorting for transport of large extracellular matrix molecules

Yoshihiro Ishikawa, Shinya Ito, Kazuhiro Nagata, Lynn Y. Sakai, Hans Peter Bächinger

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

Extracellular matrix (ECM) proteins are biosynthesized in the rough endoplasmic reticulum (rER) and transported via the Golgi apparatus to the extracellular space. The coat protein complex II (COPII) transport vesicles are approximately 60-90 nm in diameter. However, several ECM molecules are much larger, up to several hundreds of nanometers. Therefore, special COPII vesicles are required to coat and transport these molecules. Transmembrane Protein Transport and Golgi Organization 1 (TANGO1) facilitates loading of collagens into special vesicles. The Src homology 3 (SH3) domain of TANGO1 was proposed to recognize collagen molecules, but how the SH3 domain recognizes various types of collagen is not understood. Moreover, how are large noncollagenous ECM molecules transported from the rER to the Golgi? Here we identify heat shock protein (Hsp) 47 as a guide molecule directing collagens to special vesicles by interacting with the SH3 domain of TANGO1. We also consider whether the collagen secretory model applies to other large ECM molecules.

Original languageEnglish (US)
Pages (from-to)E6036-E6044
JournalProceedings of the National Academy of Sciences of the United States of America
Volume113
Issue number41
DOIs
StatePublished - Oct 11 2016

Keywords

  • COPII vesicles
  • Collagen
  • Hsp47
  • Secretion
  • TANGO1

ASJC Scopus subject areas

  • General

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