Herp enhances ER-associated protein degradation by recruiting ubiquilins (Q24318770)

Ubiquilin 1

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Ubiquilin 2

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positive regulation of ER-associated ubiquitin-dependent protein catabolic process

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author name string

Tae-Yeon Kim

1

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Eunmin Kim

2

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Sungjoo Kim Yoon

3

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Jong-Bok Yoon

Biochemical and Biophysical Research Communications

4

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language of work or name

English

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publication date

2 May 2008

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published in

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volume

369

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issue

2

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page(s)

741-6

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cites work

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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins

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The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway

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Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp

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The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway

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The ubiquitin‐like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β‐protein generation

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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

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Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells

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A membrane protein required for dislocation of misfolded proteins from the ER

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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

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Delivery of ubiquitinated substrates to protein-unfolding machines

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ERAD: the long road to destruction

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Ubx2 links the Cdc48 complex to ER-associated protein degradation

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Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation

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Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.

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A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation

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Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane

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Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane

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Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress

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Herp stabilizes neuronal Ca2 homeostasis and mitochondrial function during endoplasmic reticulum stress

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AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation

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Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates

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Role of Herp in the endoplasmic reticulum stress response

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