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ZAAT ER clearance resulted from enhancing ERdj3-mediated ZAAT degradation by silencing ERdj3 while simultaneously enhancing autophagy. In this context, ERdj3 suppression may eliminate the toxic gain of function associated with polymerization of ZAAT
These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating endplasmic reticulum and extracellular proteostasis in the presence and absence of endplasmic reticulum stress.
BiP (zeige GDF10 ELISA Kits) facilitates Sec61 (zeige SEC61A1 ELISA Kits) channel closure (i.e. limits ER Ca(2 (zeige CA2 ELISA Kits)+) leakage) via the Sec61 (zeige SEC61A1 ELISA Kits) channel with the help of ERj3 and ERj6
Depleting ERdj3 reduced the rate of mutant GCase (zeige GBA ELISA Kits) degradation in patient-derived fibroblasts, while increasing folding, trafficking, and function by directing GCase (zeige GBA ELISA Kits) to the profolding ER calnexin (zeige CANX ELISA Kits) pathway.
regulated co-secretion of ERdj3 with misfolded clients directly links ER and extracellular proteostasis during conditions of ER stress.
ERdj3 mutant bound to unfolded endoplasmic reticulum proteins under steady state conditions in much greater amounts than wild-type.
ERdjs appear to play the dual roles of increasing BiP (zeige GDF10 ELISA Kits) affinity for clients and regulating delivery of clients to BiP (zeige GDF10 ELISA Kits).
These data identify ERdj3 as a host protein involved with the cholera toxin intoxication process and provide new molecular details regarding cholera toxin A1-chaperone interactions.
In addition, BiP (zeige GDF10 ELISA Kits) formed a complex with SV40 capsids in the endoplasmic reticulum in a DNAJB11-dependent fashion.
Hsp90 (zeige HSP90 ELISA Kits) and Hsp40 (zeige DNAJB1 ELISA Kits)/Erdj3 were essential for K1's anti-apoptotic function.
DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus\; a glycine/phenylalanine (G/F)-rich region\; and a C-terminal cysteine-rich region (Ohtsuka and Hata, 2000
DnaJ (Hsp40) homolog, subfamily B, member 11
, dnaJ homolog subfamily B member 11
, dnaJ homolog subfamily B member 11-like
, APOBEC1-binding protein 2
, DnaJ protein 9
, ER-associated DNAJ protein 3
, ER-associated Hsp40 co-chaperone
, PWP1-interacting protein 4
, dnaJ protein homolog 9
, human DnaJ protein 9
, ER-associated dnaJ protein 3
, liver regeneration-related protein LRRGT00084