Dynamic Nucleotide-dependent Interactions of Cysteine- and Histidine-rich Domain (CHORD)-containing Hsp90 Cochaperones Chp-1 and Melusin with Cochaperones PP5 and Sgt1

Hong, Tae-Joon; Kim, Sang-Kyu; Wi, Ah Ram; Lee, Peter; Kang, Miae; Jeong, Jong Ju; Hahn, Jinyong

doi:10.1074/jbc.m112.398636

Cited by 17 publications

(19 citation statements)

References 43 publications

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“…CacyBP/SIP (chaperone and Hsp90-cochaperone) is in line with literature data indicating that cochaperones such as Sgt1, CHP-1, melusin and PP5 can also interact with each other (Hong et al, 2013).…”

supporting

confidence: 89%

Interaction of CacyBP/SIP with NPM1 and its influence on NPM1 localization and function in oxidative stress

Rosińska

Filipek

2018

Journal Cellular Physiology

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Calcyclin (S100A6) binding protein/Siah-1 interacting protein (CacyBP/SIP) is mainly a cytoplasmic protein; however, some literature data suggested its presence in the nucleus. In this work we examined more precisely the nuclear localization and function of CacyBP/SIP. By applying mass spectrometry, we have identified several nuclear proteins, among them is nucleophosmin (NPM1), that may interact with CacyBP/SIP. Subsequent assays revealed that CacyBP/SIP forms complexes with NPM1 in the cell and that the interaction between these two proteins is direct. Interestingly, although CacyBP/SIP exhibits phosphatase activity, we have found that its overexpression favors phosphorylation of NPM1 on S125. In turn, the RNA immunoprecipitation assay indicated that the altered CacyBP/SIP level has an impact on the amount of 28S and 18S rRNA bound to NPM1. The overexpression of CacyBP/SIP resulted in a significant increase in the binding of 28S and 18S rRNA to NPM1, whereas silencing of CacyBP/SIP expression decreased 28S rRNA binding and had no effect on the binding of 18S rRNA. Further studies have shown that under oxidative stress, CacyBP/SIP overexpression alters NPM1 distribution in cell nuclei. In addition, staining for a nucleolar marker, fibrillarin, revealed that CacyBP/SIP is indispensable for maintaining the nucleolar structure. These results are in agreement with data obtained by western blot analysis, which show that upon oxidative stress the NPM1 level decreases but that CacyBP/SIP overexpression counteracts the effect of stress. Altogether, our results show for the first time that CacyBP/SIP binds to and affects the properties of a nuclear protein, NPM1, and that it is indispensable for preserving the structure of nucleoli under oxidative stress.

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supporting

confidence: 89%

Interaction of CacyBP/SIP with NPM1 and its influence on NPM1 localization and function in oxidative stress

Rosińska

Filipek

2018

Journal Cellular Physiology

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“…CHORDC1 is a HSP90 cochaperone (39 -41), and whether this interaction is involved in HBV replication was also investigated. H186A mutation of CHORDC1 was shown to have a weaker nucleotide-dependent interaction with HSP90 compared with wild-type CHORDC1 (45). However, neither H186A mutation of CHORDC1 nor knockdown of HSP90 expression by siRNA (46) could efficiently attenuate the enhancement of HBV production by CHORDC1 (data not shown).…”

Section: Discussionmentioning

confidence: 92%

MicroRNA-26b Inhibits Hepatitis B Virus Transcription and Replication by Targeting the Host Factor CHORDC1 Protein

Zhao¹,

Xu²,

Zhou³

et al. 2014

Journal of Biological Chemistry

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Background: Disordered miR-26b expression has been linked to the development of many diseases induced by hepatitis B virus (HBV). Results: miR-26b inhibits HBV replication, and HBV infection suppresses miR-26b expression. Conclusion: miR-26b acts as a host restriction factor to attenuate HBV transcription and replication. Significance: The functional interplay between HBV infection and miR-26b may influence the outcome of viral proliferation and virus-induced diseases.

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“…Previous studies in mammalian cells have shown that Morgana and Hsp90 co-immunoprecipitate (Hahn, 2005;Wu et al, 2005;Ferretti et al, 2010;Gano and Simon, 2010;Michowski et al, 2010;Hong et al, 2013). This interaction is conserved, as the Drosophila homologue (Hsp83) was purified with similar abundance to Mora itself (Fig.…”

Section: Morgana Interacts With the Hsp90-r2tp-ttt Super-complex And mentioning

confidence: 63%

“…These domains are functionally associated with CHORD-containing proteins and Sgt1 (CS) domains, which can exist either within the same protein or in separate proteins. Two such mammalian proteins, Morgana (also known as CHORDC1 and CHP1) and Melusin (also known as ITGB1BP2), contain both CHORD and C-terminal CS domains (Brancaccio et al, 2003;Ferretti et al, 2010), interact with the cytosolic forms of the heat-shock protein Hsp90 (Hsp90α and Hsp90β, collectively referred to as Hsp90) and have been proposed to act as Hsp90 co-chaperones (Hahn, 2005;Wu et al, 2005;Sbroggiò et al, 2008;Ferretti et al, 2010;Gano and Simon, 2010;Michowski et al, 2010;Hong et al, 2013;Bohush et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Drosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerisation

Palumbo

Tariq

Borgal

et al. 2020

Journal of Cell Science

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Morgana (Mora, also known as CHORD in flies) and its mammalian homologue, called CHORDC1 or CHP1, is a highly conserved cysteine and histidine-rich domain (CHORD)-containing protein that has been proposed to function as an Hsp90 co-chaperone. Morgana deregulation promotes carcinogenesis in both mice and humans while, in Drosophila, loss of mora causes lethality and a complex mitotic phenotype that is rescued by a human morgana transgene. Here, we show that Drosophila Mora localises to mitotic spindles and co-purifies with the Hsp90-R2TP-TTT supercomplex and with additional well-known Hsp90 co-chaperones. Acute inhibition of Mora function in the early embryo results in a dramatic reduction in centrosomal microtubule stability, leading to small spindles nucleated from mitotic chromatin. Purified Mora binds to microtubules directly and promotes microtubule polymerisation in vitro, suggesting that Mora directly regulates spindle dynamics independently of its Hsp90 co-chaperone role.

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Dynamic Nucleotide-dependent Interactions of Cysteine- and Histidine-rich Domain (CHORD)-containing Hsp90 Cochaperones Chp-1 and Melusin with Cochaperones PP5 and Sgt1

Cited by 17 publications

References 43 publications

Interaction of CacyBP/SIP with NPM1 and its influence on NPM1 localization and function in oxidative stress

Interaction of CacyBP/SIP with NPM1 and its influence on NPM1 localization and function in oxidative stress

MicroRNA-26b Inhibits Hepatitis B Virus Transcription and Replication by Targeting the Host Factor CHORDC1 Protein

Drosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerisation

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