Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding (Q27931158)

GOA release 2020-03-11

1 reference

Masato Takeuchi

1

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Yukio Kimata

2

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Aiko Hirata

3

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Masahiro Oka

4

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Kenji Kohno

The Hsp70 and Hsp60 chaperone machines

5

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language of work or name

English

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publication date

March 2006

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published in

Journal of Biochemistry

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1 December 2016

139

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issue

3

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page(s)

597-605

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cites work

1 reference

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Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

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Chaperones get in touch: the Hip-Hop connection

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The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae

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BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast

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The action of molecular chaperones in the early secretory pathway

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Setting the standards: quality control in the secretory pathway

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Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation

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A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum

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Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.

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Coordinated activation of Hsp70 chaperones

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LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum

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The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates

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Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum

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Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.

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Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae

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The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum

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Cell wall integrity modulates RHO1 activity via the exchange factor ROM2

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Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.

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IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast

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Mutation of the yeast epsilon-COP gene ANU2 causes abnormal nuclear morphology and defects in intracellular vesicular transport

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Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction

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Formation process of autophagosome is traced with Apg8/Aut7p in yeast

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Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole

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Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast

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