p(HGNC:STIP1)
Hsp90 and Hop are both involved in the CMA system; PubMed:29311797
For instance, CyP40, FKBP52, PP5, Hop, p23, and Aha1 are all repressed in the aged brain. PubMed:29311797
Hsp90 and Hop are both involved in the CMA system; PubMed:29311797
This functional screen identified 18 genes (Figure 3D), corresponding to ten ATP-dependent chaperones, HSC70 (hsp-1), HSP90 (daf-21), and eight subunits of the CCT/TRiC chaperonin complex; the co-chaperones, HSP40 (dnj-12) and CDC37 (cdc-37); and the TPR-domain pro- tein STI1 that upon knockdown significantly enhanced A b 42 pro- teotoxicity (Figure 3D). PubMed:25437566
Two subnetworks emerged within this central network, corresponding to known Hsp90 and Hsp70 chaperone complexes (Figure 2, blue and orange squares, respectively). These two subnetworks were bridged by a unique set of cochaperones (Figure 2, tan squares). Among these were the wellknown bridging factors HOP/STIP1, TPR2/DNAJC7, and CHIP/ STUB1, validating our approach (Brychzy et al., 2003; Schmid et al., 2012; Xu et al., 2002). Other bridging factors in this first tier of organization included members of the Hsp40 chaperone family (DNAJB1 and DNAJB6), HSP70-binding protein 1 (HSPBP1), the TPR domain protein EDRF1, and the E3 ligase NRDP1/RNF41 PubMed:25036637
A previous study found that when Hop was depleted using siRNA, there was an accumulation of tau (Jinwal et al., 2013). PubMed:29311797
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.