Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation

Cell. 1998 Dec 23;95(7):993-1003. doi: 10.1016/s0092-8674(00)81723-7.


Newly synthesized procollagen type I (PC) assembles into 300 nm rigid, rod-like triple helices in the lumen of the endoplasmic reticulum. This oligomeric complex moves to the Golgi and forms large electron-dense aggregates. We have monitored the transport of PC along the secretory pathway. We show that PC moves across the Golgi stacks without ever leaving the lumen of the Golgi cisternae. During transport from the endoplasmic reticulum to the Golgi, PC is found within tubular-saccular structures greater than 300 nm in length. Thus, supermolecular cargoes such as PC do not utilize the conventional vesicle-mediated transport to traverse the Golgi stacks. Our results imply that PC moves in the anterograde direction across the Golgi complex by a process involving progressive maturation of Golgi cisternae.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2,2'-Dipyridyl / pharmacology
  • Animals
  • Biological Transport / drug effects
  • Chick Embryo
  • Cytoplasmic Granules / metabolism
  • Endoplasmic Reticulum / chemistry
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / ultrastructure
  • Fibroblasts
  • Fluorescent Antibody Technique
  • Golgi Apparatus / chemistry
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • Intracellular Membranes / metabolism
  • Microscopy, Electron
  • Organelles / metabolism
  • Procollagen / chemistry
  • Procollagen / metabolism*
  • Procollagen / ultrastructure
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Rats
  • Tendons
  • Time Factors


  • Procollagen
  • 2,2'-Dipyridyl