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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. Zusätzlich bieten wir Ihnen CDC37 Antikörper (185) und CDC37 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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Human CDC37 Protein expressed in Baculovirus infected Insect Cells - ABIN2003178
Roiniotis, Masendycz, Ho, Scholz: Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37. in Biochemistry 2005
Show all 2 Pubmed References
Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC (zeige CALR Proteine)). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC (zeige CALR Proteine) cells, and vice versa. For the mechanism, Cdc37 increased CDK4 (zeige CDK4 Proteine) stability to promote the phosphorylation of RB1 (zeige RB1 Proteine), which finally promoted the progression of CRC (zeige CALR Proteine).
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 (zeige HSP90 Proteine) phosphorylation at Y197 and specifically regulate kinase chaperoning.
findings suggested that this mechanism may be exploited by the Hsp90 (zeige HSP90 Proteine)-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 (zeige HSP90 Proteine) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (zeige SNRPE Proteine), where induced conformational instability acts as a "flag" for Hsp90 (zeige HSP90 Proteine) dependence and stable cochaperone association.
Ulk1 (zeige ULK1 Proteine) promoted the degradation of Hsp90 (zeige HSP90 Proteine)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (zeige HSP90 Proteine) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (zeige ULK1 Proteine) in response to Hsp90 (zeige HSP90 Proteine) inhibition in cancer cells
The authors find that the interaction between sB-Raf (zeige RAF1 Proteine) and the Hsp90 chaperone (zeige HSP90 Proteine) system is based on contacts with the M domain of Hsp90 (zeige HSP90 Proteine), 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 (zeige HSP90 Proteine) to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90 (zeige HSP90 Proteine), with or without binding to Hsp90 (zeige HSP90 Proteine), the interaction between Cdc37 and Hsp90 (zeige HSP90 Proteine) appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90 (zeige HSP90 Proteine)-mediated protein maturation.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (zeige HSP90 Proteine), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (zeige HSP90 Proteine)-Cdc37 complex acta (zeige ACTC1 Proteine) as an endogenous regulator of noncanonical p38alpha (zeige MAPK14 Proteine) activity.
CDC37 binds to Akt (zeige AKT1 Proteine) and HSP90 (zeige HSP90 Proteine) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (zeige GSTa2 Proteine) pull-down assay, and the possible interaction model was suggested.
JAK1 (zeige JAK1 Proteine)/2 are client proteins of Hsp90 alpha (zeige HSP90AA1 Proteine) and beta; Hsp90 (zeige HSP90 Proteine) and CDC37 play a critical role in types I and II interferon (zeige IFNA Proteine) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (zeige GLI1 Proteine), 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 (zeige NOS3 Proteine)) and may play an important role in mediating the eNOS (zeige NOS3 Proteine) 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