Lumenal protein multimerization in the distal secretory pathway/secretory granules

Curr Opin Cell Biol. 2002 Aug;14(4):448-53. doi: 10.1016/s0955-0674(02)00344-7.

Abstract

Differences in protein solubility appear to play an important role in lumenal protein trafficking through Golgi/post-Golgi compartments. Recent advances indicate that multimeric protein assembly is one of the factors regulating the efficiency of protein storage within secretory granules, by mechanisms that, with slight modification, might be considered to represent the culmination of a process of Golgi cisternal maturation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Carrier Proteins / metabolism
  • Cell Compartmentation
  • Cytoplasmic Granules / metabolism*
  • Cytoplasmic Granules / ultrastructure
  • Golgi Apparatus / metabolism*
  • Humans
  • Intracellular Membranes / metabolism
  • Models, Biological
  • Protein Precursors / metabolism
  • Protein Processing, Post-Translational
  • Protein Transport
  • Proteins / metabolism*
  • Solubility
  • trans-Golgi Network / metabolism

Substances

  • Carrier Proteins
  • Protein Precursors
  • Proteins