anti-Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) Antikörper

Fruit Fly (Drosophila melanogaster) Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) Interaktionspartner

1. loss of function leads to defects in mitosis and male meiosis

Human Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) Interaktionspartner

1. results of this integrative computational study are compared with a wide range of structural, biochemical, and cell-based experiments, offering a robust network-centric model of allosteric regulation and client kinase recognition by the Hsp90-Cdc37 chaperone machine

2. Results found that several disease-linked mutations convert FGFR3 to a stronger client of Hsp90/Cdc37. Enhanced interaction with Cdc37 is underpinned by a weakened N-lobe network. Cdc37 binding to unrelated kinases induces their common, extensive remodeling. Kinase remodeling and the kinase/Cdc37 architecture allow recognition by Hsp90.

3. Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC cells, and vice versa. For the mechanism, Cdc37 increased CDK4 stability to promote the phosphorylation of RB1, which finally promoted the progression of CRC.

4. 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 phosphorylation at Y197 and specifically regulate kinase chaperoning.

5. findings suggested that this mechanism may be exploited by the Hsp90-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation

6. 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.

7. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth.

8. Cdc37 performs a quality control of protein kinases, including b-raf, where induced conformational instability acts as a "flag" for Hsp90 dependence and stable cochaperone association.

9. Ulk1 promoted the degradation of Hsp90-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 in response to Hsp90 inhibition in cancer cells

10. The authors find that the interaction between sB-Raf and the Hsp90 chaperone system is based on contacts with the M domain of Hsp90, which contributes in forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide.

11. Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.

12. Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.

13. RIP3 activation following the induction of necroptosis requires the activity of an HSP90 and CDC37 cochaperone complex.

14. Correlation between PDZK1, Cdc37, Akt and breast cancer malignancy: the role of PDZK1 in cell growth through Akt stabilization by increasing and interacting with Cdc37

15. The N-terminal tail serves as an intramolecular chaperone ensuring that CDC37 assumes one of two interconvertible states in a manner impacting the interaction of the client binding N-domain and the MC-domains, involved in dimerization and HSP90 binding.

16. CDC37 has an important role in chaperoning protein kinases; it stabilizes kinase clients by a mechanism that is not dependent on a substantial direct interaction between CDC37 and HSP90, but requires HSP90 activity

17. As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.

18. CDC37 is a crucial HSP90-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors

19. SGK3 stability and kinase activation are regulated by the Hsp90-Cdc37 chaperone complex.

20. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.

Mouse (Murine) Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) Interaktionspartner

1. Results showed that Cdc37 acts as a bridge to direct Hsp90 to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90, with or without binding to Hsp90, the interaction between Cdc37 and Hsp90 appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90-mediated protein maturation.

2. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth.

3. A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle.

4. Hsp90-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha activity.

5. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells

6. The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase pull-down assay, and the possible interaction model was suggested.

7. JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways

8. This growth inhibition is partially rescued by expression of ectopic Gli1, suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.

Cow (Bovine) Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) Interaktionspartner

1. Cdc37 has a direct regulatory interaction with endothelial nitric oxide synthase (eNOS) and may play an important role in mediating the eNOS protein complex formation.