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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae.
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Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC (show CALR ELISA Kits)). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC (show CALR ELISA Kits) cells, and vice versa. For the mechanism, Cdc37 increased CDK4 (show CDK4 ELISA Kits) stability to promote the phosphorylation of RB1 (show RB1 ELISA Kits), which finally promoted the progression of CRC (show CALR ELISA Kits).
During the kinase chaperone cycle, Cdc37 phosphorylated at Y298 acts as a platform for docking of non-receptor tyrosine kinases through their regulatory domains to drive the coupled Hsp90 (show HSP90 ELISA Kits) phosphorylation at Y197 and specifically regulate kinase chaperoning.
findings suggested that this mechanism may be exploited by the Hsp90 (show HSP90 ELISA Kits)-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation
The results suggest a re-evaluation of the role of Cdc37 in the kinase lifecycle, and suggest that such interactions potentially allow kinases to more rapidly respond to key signals while simultaneously protecting unstable kinases from degradation and suppressing unwanted basal activity.
Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 (show HSP90 ELISA Kits) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (show SNRPE ELISA Kits), where induced conformational instability acts as a "flag" for Hsp90 (show HSP90 ELISA Kits) dependence and stable cochaperone association.
Ulk1 (show ULK1 ELISA Kits) promoted the degradation of Hsp90 (show HSP90 ELISA Kits)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (show HSP90 ELISA Kits) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (show ULK1 ELISA Kits) in response to Hsp90 (show HSP90 ELISA Kits) inhibition in cancer cells
The authors find that the interaction between sB-Raf (show RAF1 ELISA Kits) and the Hsp90 chaperone (show HSP90 ELISA Kits) system is based on contacts with the M domain of Hsp90 (show HSP90 ELISA Kits), which contributes in forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide.
Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.
Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.
Results showed that Cdc37 acts as a bridge to direct Hsp90 (show HSP90 ELISA Kits) to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90 (show HSP90 ELISA Kits), with or without binding to Hsp90 (show HSP90 ELISA Kits), the interaction between Cdc37 and Hsp90 (show HSP90 ELISA Kits) appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90 (show HSP90 ELISA Kits)-mediated protein maturation.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (show HSP90 ELISA Kits), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (show HSP90 ELISA Kits)-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha (show MAPK14 ELISA Kits) activity.
CDC37 binds to Akt (show AKT1 ELISA Kits) and HSP90 (show HSP90 ELISA Kits) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (show GSTa2 ELISA Kits) pull-down assay, and the possible interaction model was suggested.
JAK1 (show JAK1 ELISA Kits)/2 are client proteins of Hsp90 alpha (show HSP90AA1 ELISA Kits) and beta; Hsp90 (show HSP90 ELISA Kits) and CDC37 play a critical role in types I and II interferon (show IFNA ELISA Kits) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (show GLI1 ELISA Kits), suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.
Cdc37 has a direct regulatory interaction with endothelial nitric oxide synthase (eNOS (show NOS3 ELISA Kits)) and may play an important role in mediating the eNOS (show NOS3 ELISA Kits) protein complex formation.
The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.
, cdc37 protein
, hsp90 co-chaperone Cdc37
, Hsp90 co-chaperone Cdc37
, hypothetical protein
, CDC37 (cell division cycle 37, S. cerevisiae, homolog)
, CDC37 cell division cycle 37 homolog
, cell division cycle 37 homolog
, hsp90 chaperone protein kinase-targeting subunit
, CDC37 (cell division cycle 37 S. cerevisiae homolog)
, CDC37 cell division cycle 37 protein
, CDC37 homolog
, cell division cycle 37 protein
, cell division cycle control protein 37