| Structural insight into guanylyl cyclase receptor hijacking of the kinase-Hsp90 regulatory mechanism. | Structural insight into guanylyl cyclase receptor hijacking of the kinase-Hsp90 regulatory mechanism.
Caveney NA, Tsutsumi N, Garcia KC., Free PMC Article | 08/4/2023 |
| HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation. | HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
Oberoi J, Guiu XA, Outwin EA, Schellenberger P, Roumeliotis TI, Choudhary JS, Pearl LH., Free PMC Article | 12/17/2022 |
| The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases. | The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases.
Zhang X, Li S, Li Z, Cheng L, Liu Z, Wang C. | 09/3/2022 |
| Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B. | Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B.
Papenfuss M, Lützow S, Wilms G, Babendreyer A, Flaßhoff M, Kunick C, Becker W., Free PMC Article | 03/19/2022 |
| Protein quality control of DYRK family protein kinases by the Hsp90-Cdc37 molecular chaperone. | Protein quality control of DYRK family protein kinases by the Hsp90-Cdc37 molecular chaperone.
Miyata Y, Nishida E. | 12/4/2021 |
| Hsp90 interacts with Cdc37, is phosphorylated by PKA/PKC, and regulates Src phosphorylation in human sperm capacitation. | Hsp90 interacts with Cdc37, is phosphorylated by PKA/PKC, and regulates Src phosphorylation in human sperm capacitation.
Li K, Sun P, Wang Y, Gao T, Zheng D, Liu A, Ni Y. | 11/6/2021 |
| [Cdc37 Expression in Multiple Myeloma and Its Role in Cell Proliferation]. | [Cdc37 Expression in Multiple Myeloma and Its Role in Cell Proliferation].
Zang MR, Liu LT, Deng SH, Qiu LG. | 10/16/2021 |
| The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37. | The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37.
Kowallik S, Kritikos A, Kästle M, Thurm C, Schraven B, Simeoni L., Free PMC Article | 09/18/2021 |
| The CDC37-HSP90 chaperone complex co-translationally degrades the nascent kinase-dead mutant of HIPK2. | The CDC37-HSP90 chaperone complex co-translationally degrades the nascent kinase-dead mutant of HIPK2.
Müller JP, Klempnauer KH. | 07/31/2021 |
| Medium-Throughput Detection of Hsp90/Cdc37 Protein-Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay. | Medium-Throughput Detection of Hsp90/Cdc37 Protein-Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay.
Siddiqui FA, Parkkola H, Manoharan GB, Abankwa D. | 07/17/2021 |
| results demonstrated DDO-5936 as an identified specific small-molecule inhibitor of the Hsp90-Cdc37 PPI that could be used to comprehensively investigate alternative approaches targeting Hsp90 chaperone cycles for cancer therapy. | Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer.
Wang L, Zhang L, Li L, Jiang J, Zheng Z, Shang J, Wang C, Chen W, Bao Q, Xu X, Jiang Z, Zhang J, You Q., Free PMC Article | 05/2/2020 |
| The results suggested that more complicated mechanisms might be necessary to explain the phosphorylation-activated interaction of Cdc37 with various kinases. | Structural characterization of the N-terminal kinase-interacting domain of an Hsp90-cochaperone Cdc37 by CD and solution NMR spectroscopy.
Ihama F, Yamamoto M, Kojima C, Fujiwara T, Matsuzaki K, Miyata Y, Hoshino M. | 11/30/2019 |
| 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 | Functional Role and Hierarchy of the Intermolecular Interactions in Binding of Protein Kinase Clients to the Hsp90-Cdc37 Chaperone: Structure-Based Network Modeling of Allosteric Regulation.
Stetz G, Verkhivker GM. | 01/26/2019 |
| 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. | Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
Bunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M., Free PMC Article | 01/26/2019 |
| 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. | Cdc37 facilitates cell survival of colorectal carcinoma via activating the CDK4 signaling pathway.
Zhu J, Yan F, Tao J, Zhu X, Liu J, Deng S, Zhang X., Free PMC Article | 03/17/2018 |
| 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. | Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation.
Bachman AB, Keramisanou D, Xu W, Beebe K, Moses MA, Vasantha Kumar MV, Gray G, Noor RE, van der Vaart A, Neckers L, Gelis I., Free PMC Article | 02/17/2018 |
| findings suggested that this mechanism may be exploited by the Hsp90-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation | Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.
Czemeres J, Buse K, Verkhivker GM., Free PMC Article | 01/20/2018 |
| 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. | How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.
Verba KA, Agard DA., Free PMC Article | 10/14/2017 |
| Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth. | Computational Discovery of Niclosamide Ethanolamine, a Repurposed Drug Candidate That Reduces Growth of Hepatocellular Carcinoma Cells In Vitro and in Mice by Inhibiting Cell Division Cycle 37 Signaling.
Chen B, Wei W, Ma L, Yang B, Gill RM, Chua MS, Butte AJ, So S., Free PMC Article | 08/19/2017 |
| 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. | Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.
Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I., Free PMC Article | 08/5/2017 |
| 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 | Serine/Threonine Kinase Unc-51-like Kinase-1 (Ulk1) Phosphorylates the Co-chaperone Cell Division Cycle Protein 37 (Cdc37) and Thereby Disrupts the Stability of Cdc37 Client Proteins.
Li R, Yuan F, Fu W, Zhang L, Zhang N, Wang Y, Ma K, Li X, Wang L, Zhu WG, Zhao Y., Free PMC Article | 07/1/2017 |
| 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. | Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro.
Eckl JM, Daake M, Schwartz S, Richter K. | 06/24/2017 |
| Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes. | Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.
Eckl JM, Scherr MJ, Freiburger L, Daake MA, Sattler M, Richter K., Free PMC Article | 05/14/2016 |
| Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth. | Suppressing the CDC37 cochaperone in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.
Wang Z, Wei W, Sun CK, Chua MS, So S. | 12/19/2015 |
| RIP3 activation following the induction of necroptosis requires the activity of an HSP90 and CDC37 cochaperone complex. | A cytosolic heat shock protein 90 and cochaperone CDC37 complex is required for RIP3 activation during necroptosis.
Li D, Xu T, Cao Y, Wang H, Li L, Chen S, Wang X, Shen Z., Free PMC Article | 07/4/2015 |