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Article Addendum
Causal Links Between Protein Folding in the ER and Events Along the Secretory Pathway
Masato Takeuchi, Yukio Kimata and Kenji Kohno
volume 2 | issue 4
October/November/December 2006Pages: 319 - 320
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
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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.
Addendum to:
Masato Takeuchi, Yukio Kimata, Aiko Hirata, Masahiro Oka and Kenji Kohno
J Biochem 2006; 139:597-605
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.