Causal links between protein folding in the ER and events along the secretory pathway

Autophagy. 2006 Oct-Dec;2(4):323-4. doi: 10.4161/auto.3089. Epub 2006 Oct 13.

Abstract

The 70-kDa heat shock protein (Hsp70) family comprises the most abundant and important group of molecular chaperones. Hsp70s cooperate with a number of cofactors, which define their functions. We recently reported that a yeast protein, Rot1, is a putative cofactor of BiP, an endoplasmic reticulum (ER)-localized Hsp70. Rot1 is an essential ER membrane protein and may be involved in protein folding. Mutation of the ROT1 gene caused defects in cell wall synthesis and lysis of autophagic bodies. We suggest that Rot1 is required for folding of proteins engaged in these cellular processes.

MeSH terms

  • Cathepsin A / chemistry
  • Cathepsin A / metabolism
  • Endoplasmic Reticulum / metabolism*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • HSP70 Heat-Shock Proteins / metabolism*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Protein Folding*

Substances

  • Fungal Proteins
  • HSP70 Heat-Shock Proteins
  • Membrane Proteins
  • Cathepsin A