| http://purl.uniprot.org/citations/28536268 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28536268 | http://www.w3.org/2000/01/rdf-schema#comment | "DNAJB12 (JB12) is an endoplasmic reticulum (ER)-associated Hsp40 family protein that recruits Hsp70 to the ER surface to coordinate the function of ER-associated and cytosolic chaperone systems in protein quality control. Hsp70 is stress-inducible, but paradoxically, we report here that JB12 was degraded by the proteasome during severe ER stress. Destabilized JB12 was degraded by ER-associated degradation complexes that contained HERP, Sel1L, and gp78. JB12 was the only ER-associated chaperone that was destabilized by reductive stress. JB12 knockdown by siRNA led to the induction of caspase processing but not the unfolded protein response. ER stress-induced apoptosis is regulated by the highly labile and ER-associated BCL-2 family member BOK, which is controlled at the level of protein stability by ER-associated degradation components. We found that JB12 was required in human hepatoma cell line 7 (Huh-7) liver cancer cells to maintain BOK at low levels, and BOK was detected in complexes with JB12 and gp78. Depletion of JB12 during reductive stress or by shRNA from Huh-7 cells was associated with accumulation of BOK and activation of Caspase 3, 7, and 9. The absence of JB12 sensitized Huh-7 to death caused by proteotoxic agents and the proapoptotic chemotherapeutic LCL-161. In summary, JB12 is a stress-sensitive Hsp40 whose degradation during severe ER stress provides a mechanism to promote BOK accumulation and induction of apoptosis."xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m117.785113"xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/author | "Cyr D.M."xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/author | "Ren H.Y."xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/author | "Grove D.E."xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/author | "Sopha P."xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/pages | "11792-11803"xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/title | "Endoplasmic reticulum stress-induced degradation of DNAJB12 stimulates BOK accumulation and primes cancer cells for apoptosis."xsd:string |
| http://purl.uniprot.org/citations/28536268 | http://purl.uniprot.org/core/volume | "292"xsd:string |
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