Phospho-CDC37 (S13) Recombinant Monoclonal Antibody

1. 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. PMID: 29288563
2. 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. PMID: 29343704
3. findings suggested that this mechanism may be exploited by the Hsp90-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation PMID: 29267381
4. 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. PMID: 28784328
5. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth. PMID: 28284560
6. 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. PMID: 27105117
7. 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 PMID: 28073914
8. 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. PMID: 27620500
9. Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes. PMID: 26511315
10. Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth. PMID: 25098386
11. 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 PMID: 24869908
12. 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. PMID: 25619116
13. 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 PMID: 24292678
14. 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. PMID: 24927996
15. CDC37 is a crucial HSP90-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors PMID: 23584476
16. SGK3 stability and kinase activation are regulated by the Hsp90-Cdc37 chaperone complex. PMID: 24379398
17. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. PMID: 23569206
18. ERK5 interacts with the Hsp90-Cdc37 chaperone in resting cells, and inhibition of Hsp90 or Cdc37 results in ERK5 ubiquitylation and proteasomal degradation. PMID: 23428871
19. an essential role for surface Cdc37 in concert with HSP90 on the cell surface during cancer cell invasion processes PMID: 22912728
20. A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle. PMID: 22727666
21. Data show that part of the normal clearance cascade for TDP-43 involves the Cdc37/Hsp90 complex. PMID: 22674575
22. Cdc37-mediated direct interaction between Hsp90/Cdc37 and an IRE1alpha cytosolic motif is important to maintain basal IRE1alpha activity and contributes to normal protein homeostasis and unfolded protein response under physiological stimulation. PMID: 22199355
23. The primary mechanisms by which apigenin kill multiple myeloma cells is by targeting the trinity of CK2-Cdc37-Hsp90. PMID: 21871133
24. the Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics PMID: 21367866
25. Hsp90-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha activity. PMID: 20299663
26. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. PMID: 11864612
27. role in regulating Hsp90 ATPase activity PMID: 11916974
28. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells PMID: 12176997
29. Results show that Cdc37 and heat shock protein 90 bind specifically to the kinase domain of LKB1. PMID: 12489981
30. phosphorylation of Cdc37 on Ser13 is critical for its ability to coordinate Hsp90 nucleotide-mediated conformational switching and kinase binding PMID: 12930845
31. Heteromeric comlpexes containing the molecular chaperones Hsp90 and Cdc37/p50 interacts with the kinase domain of LKB1. PMID: 14668798
32. the interaction of Cdc37 with its client protein kinases requires amino acid residues within a motif that is present in many protein kinases PMID: 14701845
33. Hsp90/p50cdc37 is required for mixed-lineage kinase (MLK) 3 signaling PMID: 15001580
34. the Hsp90.Cdc37 molecular chaperone module has a central role in interleukin-1 receptor-associated-kinase-dependent signaling by toll-like receptors PMID: 15647277
35. Cdc37 is found to heterodimerize with heat-shock protein 90 (Hsp90)-associating relative of Cdc37 (Harc) in vitro. PMID: 15850399
36. Nuclear magnetic resonance study of binding to to HSP90. PMID: 16132836
37. results suggest that a region of Cdc37 other than the client-binding site may be responsible for discriminating client protein kinases from others PMID: 16156789
38. JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways PMID: 16280321
39. N-terminal glycine-rich loop of protein kinases is essential for physically associating with Cdc37. PMID: 16611982
40. The data shows the expression and purification of an Hsp90-Cdc37-Cdk4 complex, defining its stoichiometry, and determining its 3D structure by single-particle electron microscopy. PMID: 16949366
41. these observations support the hypothesis that there is a specific coordination between the activation of the cytosolic Ah receptor and the c-Src- and cdc37-containing HSP90 complex. PMID: 17223712
42. The present data denote Hsp90-Cdc37 as a transiently acting essential regulatory component of IKK signaling. PMID: 17728246
43. identify Pink1 as a novel Cdc37/Hsp90 client kinase PMID: 18003639
44. Cdc37 is essential for maintaining prostate tumor cell growth and may represent a novel target in the search for multitargeted therapies. PMID: 18089825
45. These data reveal a cyclic regulatory mechanism for Cdc37, in which its constitutive phosphorylation is reversed by targeted dephosphorylation in Hsp90 complexes. PMID: 18922470
46. CDC37 in concert with HSP90 plays an essential role in maintaining oncogenic protein kinase clients including ERBB2, CRAF, CDK4, CDK6, & phosphorylated AKT. PMID: 18931700
47. The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. PMID: 19073599
48. C-terminal tail and determinants in the alphaE-helix of the catalytic domain allows the chaperones Hsp90 and Cdc37 to bind newly synthesized PKC beta II, a required event in the processing of PKC by phosphorylation PMID: 19091746
49. celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex. PMID: 19858214

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HGNC: 1735

OMIM: 605065

KEGG: hsa:11140

STRING: 9606.ENSP00000222005

UniGene: Hs.160958