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p(HGNC:CDC37)

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Entity

Name
CDC37
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 5

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

In-Edges 26

complex(a(MESH:"Protein Kinases"), p(HGNC:CDC37)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:ABL2), p(HGNC:CDC37)) hasComponent p(HGNC:CDC37) View Subject | View Object

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p(HGNC:FKBP5) association p(HGNC:CDC37) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

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complex(p(HGNC:AHSA1), p(HGNC:CDC37)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:ARAF), p(HGNC:CDC37)) hasComponent p(HGNC:CDC37) View Subject | View Object

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p(INTERPRO:"Cdc37, N-terminal domain") increases act(p(HGNC:CDC37)) View Subject | View Object

CDC37L1 lacks the very N terminus of CDC37, which is required for kinase interaction and the cellular function of CDC37 (Shao et al., 2003), and is able to mediate strong interaction with ARAF when fused to CDC37L1 (Figure S3B) PubMed:25036637

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complex(p(HGNC:AURKB), p(HGNC:CDC37)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:CDK1)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:CDK11A)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:CDK4)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:CHUK)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:FER)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:IKBKG)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(HGNC:RAF1)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(INTERPRO:"Heat shock protein Hsp90 family")) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(FPLX:HSP90), p(HGNC:CDC37)) hasComponent p(HGNC:CDC37) View Subject | View Object

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complex(p(HGNC:CDC37), p(SFAM:"HSP90 Family")) hasComponent p(HGNC:CDC37) View Subject | View Object

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act(p(SFAM:"HSP90 Family")) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

This coordination of kinase triage decisions by Hsp90 requires the co-chaperone Cdc37 (cell division cycle protein 37). The Hsp90/Cdc37 machine is essential for the maturation of a number of kinases, including Akt PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Thr, 231)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Ser, 404)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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act(p(HGNC:CDK5)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Western blot analysis for a panel of tau kinases showed that only the levels of endogenous Cdk5 and Akt were significantly reduced by Cdc37 siRNA; the levels of GSK3-Beta and Mark2 (microtubule affinity regulating kinase 2) were largely unchanged PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Ser, 199)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Ser, 202)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Ser, 262)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Ser, 356)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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p(HGNC:MAPT, pmod(Ph, Ser, 396)) positiveCorrelation p(HGNC:CDC37) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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Out-Edges 31

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(INTERPRO:"Heat shock protein Hsp90 family")) View Subject | View Object

For example, we identified several protein kinases that copurified with CDC37, a known kinase-specific Hsp90 cochaperone (Taipale et al., 2012) PubMed:25036637

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p(HGNC:CDC37) directlyIncreases complex(p(HGNC:AHSA1), p(HGNC:CDC37)) View Subject | View Object

For example, CDC37L1 interacted with the bridging factor HOP, whereas CDC37 copurified with AHA1 (Figure 3B), but even more strikingly, CDC37L1 did not associate with any kinases in AP-MS (Figures 2 and 3B) PubMed:25036637

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p(HGNC:CDC37) directlyIncreases complex(p(HGNC:AURKB), p(HGNC:CDC37)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

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p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:CDK11A)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:CDK1)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:IKBKG)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:CDK4)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:FER)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:CHUK)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:CDC37), p(HGNC:RAF1)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:ABL2), p(HGNC:CDC37)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(p(HGNC:ARAF), p(HGNC:CDC37)) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) association p(HGNC:FKBP5) View Subject | View Object

First, FKBP51 interacted with a subset of the kinases that interacted with CDC37 (Figure 3B) PubMed:25036637

Appears in Networks:

p(HGNC:CDC37) directlyIncreases complex(a(MESH:"Protein Kinases"), p(HGNC:CDC37)) View Subject | View Object

As expected, CDC37 interacted virtually exclusively with kinases (p < 0.0001, Mann-Whitney test; Figure 7A) PubMed:25036637

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p(HGNC:CDC37) regulates act(p(FPLX:HSP90)) View Subject | View Object

As in the case of Hsp70, cochaperones of Hsp90, such as Aha1, cdc37 and TPR domain-containing proteins, regulate its ATPase activity and control its conformational transitions (reviewed in [84]). PubMed:21882945

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p(HGNC:CDC37) increases complex(a(MESH:"Protein Kinases"), p(FPLX:HSP90)) View Subject | View Object

For example, the co-chaperones cdc37, a peptidyl-prolyl cis-trans isomerase (PPIase) family member, and p23 are all critical for the transfer of kinases to Hsp90 and maturation of the active protein [76,105] PubMed:21882945

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p(HGNC:CDC37) increases p(HGNC:MAPT) View Subject | View Object

Interestingly, overexpression of Cdc37 preserves tau, and its suppression reduces tau (Jinwal et al., 2012). PubMed:29311797

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Annotations
MeSH
Cerebral Cortex

p(HGNC:CDC37) positiveCorrelation act(p(SFAM:"HSP90 Family")) View Subject | View Object

This coordination of kinase triage decisions by Hsp90 requires the co-chaperone Cdc37 (cell division cycle protein 37). The Hsp90/Cdc37 machine is essential for the maturation of a number of kinases, including Akt PubMed:21367866

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p(HGNC:CDC37) isA complex(p(HGNC:CDC37), p(SFAM:"HSP90 Family")) View Subject | View Object

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p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Thr, 231)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

Appears in Networks:

p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 199)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

Appears in Networks:

p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 202)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

Appears in Networks:

p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 396)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

Appears in Networks:

p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 404)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

Appears in Networks:

p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 262)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

Appears in Networks:

p(HGNC:CDC37) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 356)) View Subject | View Object

Quantification of the Western blot showed that Cdc37 knockdown reduced phospho-Thr-231, phospho-Ser-199/Ser-202, phospho-Ser-396/Ser-404, and phospho-Ser-262/Ser-356 tau. PubMed:21367866

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p(HGNC:CDC37) decreases deg(p(HGNC:MAPT)) View Subject | View Object

Previous work showed that Hsp90 inhibition with 17-AAG reduced phospho-tau levels in vivo (16, 23). We speculated that Cdc37 might modulate Hsp90 inhibitor efficacy for phosphotau. M17 cells were transfected with Cdc37 siRNA and then treated with 1 μM 17-AAG for 24 h. Indeed, reducing Cdc37 synergized with Hsp90 inhibition to reduce tau levels more potently than either condition alone (Fig. 6A). PubMed:21367866

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p(HGNC:CDC37) positiveCorrelation act(p(HGNC:CDK5)) View Subject | View Object

Western blot analysis for a panel of tau kinases showed that only the levels of endogenous Cdk5 and Akt were significantly reduced by Cdc37 siRNA; the levels of GSK3-Beta and Mark2 (microtubule affinity regulating kinase 2) were largely unchanged PubMed:21367866

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p(HGNC:CDC37) causesNoChange p(HGNC:GSK3B) View Subject | View Object

Western blot analysis for a panel of tau kinases showed that only the levels of endogenous Cdk5 and Akt were significantly reduced by Cdc37 siRNA; the levels of GSK3-Beta and Mark2 (microtubule affinity regulating kinase 2) were largely unchanged PubMed:21367866

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p(HGNC:CDC37) causesNoChange p(HGNC:MARK2) View Subject | View Object

Western blot analysis for a panel of tau kinases showed that only the levels of endogenous Cdk5 and Akt were significantly reduced by Cdc37 siRNA; the levels of GSK3-Beta and Mark2 (microtubule affinity regulating kinase 2) were largely unchanged PubMed:21367866

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p(HGNC:CDC37) decreases act(p(FPLX:HSP90), ma(GO:"ATPase activity")) View Subject | View Object

Cochaperones HOP (Sti1) and Cdc37 (p50) stabilize the open conformation of the Hsp90 dimer (81, 174, 175, 188), inhibit ATP hydrolysis, and facilitate substrate protein binding. PubMed:23746257

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.