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Human Polyclonal DNAJB11 Primary Antibody for ICC, IF - ABIN4305581
Wen, Damania: Hsp90 and Hsp40/Erdj3 are required for the expression and anti-apoptotic function of KSHV K1. in Oncogene 2010
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 (show GDF10 Antibodies) facilitates Sec61 (show SEC61A1 Antibodies) channel closure (i.e. limits ER Ca(2 (show CA2 Antibodies)+) leakage) via the Sec61 (show SEC61A1 Antibodies) channel with the help of ERj3 and ERj6
Depleting ERdj3 reduced the rate of mutant GCase (show GBA Antibodies) degradation in patient-derived fibroblasts, while increasing folding, trafficking, and function by directing GCase (show GBA Antibodies) to the profolding ER calnexin (show CANX Antibodies) 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 (show GDF10 Antibodies) affinity for clients and regulating delivery of clients to BiP (show GDF10 Antibodies).
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 (show GDF10 Antibodies) formed a complex with SV40 capsids in the endoplasmic reticulum in a DNAJB11-dependent fashion.
Hsp90 (show HSP90 Antibodies) and Hsp40 (show DNAJB1 Antibodies)/Erdj3 were essential for K1's anti-apoptotic function.
The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (show NYX Antibodies) (SlrP (show OPTC Antibodies)), targets the human chaperone ERdj3.
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