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ERAD substrates
300px Definition: -
Wiki Content
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E3 ubiquitin ligase
300px Function: -
HRD3 / SEL1L
300px Function: adaptor of E3 ubiquitin ligase complex HRD1 in ER membrane, HRD3 in yeast, SEL1L in metazoans; recruits misfolded proteins to E3 ligase and also recruits other adaptors, such as lectins Yos9p/OS-9 -
HRD1
300px Function: -
Doa10 (Doa10p)
300px E3 ubiquitin ligase complex for substrates with misfolded cytosolic domains only other ERAD-active E3 in yeast besides Hrd1p, Has broad substrate specificity, encompassing membrane proteins, as well as soluble cytosolic and nuclear proteins -
ERAD Wiki
ERAD Write a description about your topic. Let your readers know what your topic is about and add some general information about it. -
HMG-CoA reductase (Hmg2p)
300px yeast HMG-CoA reductase (Hmg2p) is the rate limiting enzyme in cholesterol synthesis example of physiological regulation of protein abundance via ERAD, when cholesterol levels are high, Hmg2p undergoes a lipid-induced structural change -
Derlin (Der1p, DER1)
300px Function: members of E3 complexes, yeast Der1p: multi-pass transmembrane protein that interacts with Hrd1p and Hrd3p as well as with substrates, dispensable for degradation of many substrates, contain a motif shared with rhomboid -
Htm1 (Htm1p)
300px Htm1p forms a disulfide-stabilized complex with Pdi1p which is necessary for both maximal Htm1p activity as well as its stability (Gauss et al., 2011; Mol Cell; Sakoh-Nakatogawa et al., 2009; JBC) -
ERdj5
300px interacts with EDEM1 and BiP, can reduce disulfide bonds of aberrantly linked proteins, accelerates ERAD when overexpressed (Ushioda et al., 2008; Science), substrate-binding J domain and disulfide-reactive thioredoxin domain are both critical -
UPR (unfolded protein response)
300px Definition:
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