Causal links between protein folding in the ER and events along the secretory pathway.
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.
Takeuchi
Masato
M
Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Kimata
Yukio
Y
Kohno
Kenji
K
D043402:Cathepsin A / Q000737:chemistry / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding
D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D008565:Membrane Proteins; D043402:Cathepsin A