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Updated: Aug 6, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
Causal links between protein folding in the ER and events along the secretory pathway
Masato Takeuchi1, Yukio Kimata, Kenji Kohno
1Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
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.
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