The Chaperone-assisted E3 Ligase C Terminus of Hsc70-interacting Protein (CHIP) Targets PTEN for Proteasomal Degradation

Ahmed, Syed Feroj; Deb, Satamita; Paul, Indranil; Chatterjee, Anirban; Mandal, Tapashi; Chatterjee, Uttara; Ghosh, Mrinal K.

doi:10.1074/jbc.m111.321083

Cited by 138 publications

(147 citation statements)

References 56 publications

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“…Similar to our results, inhibition of HDAC activity by TSA also alters the function of several other important transcription factors, such as estrogen receptor a and steroidogenic factor 1, through targeting them for proteasomal degradation (45,46). CHIP was identified as an E3 ligase for IRF-1 as well as a number of HSP70-associated proteins, such as ErbB2 and PTEN (47,48); however, it was reported that CHIP acted as the chaperone for IRF-1 in unstressed cells. Only under special conditions in which the interaction between CHIP and IRF-1 gets enhanced will CHIP target IRF-1 for ubiquitination and degradation (41).…”

Section: Discussionsupporting

confidence: 73%

Inhibition of Histone Deacetylase Activity Suppresses IFN-γ Induction of Tripartite Motif 22 via CHIP-Mediated Proteasomal Degradation of IRF-1

Gao

Wang

et al. 2013

The Journal of Immunology

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Tripartite motif (TRIM)22 plays an important role in IFN-mediated antiviral activity. We previously demonstrated that IFN regulatory factor (IRF)-1 was crucial for basal and IFN-induced TRIM22 transcription via binding to a novel cis-element named 5′ extended IFN-stimulating response element. In this study, we investigated the role of histone deacetylase (HDAC) activity in TRIM22 induction by IFN-γ and its underlying mechanism. We found that the HDAC activity, especially that conferred by HDAC6, was required for IFN-γ–induced TRIM22 transcription. Importantly, inhibition of HDAC activity by trichostatin A (TSA) enhanced the hyperacetylation of heat shock protein (HSP)90 and suppressed its chaperone activity for IRF-1. Further study showed that TSA treatment promoted the proteasomal degradation of IRF-1 protein via enhancing the association of IRF-1 with the ubiquitin E3 ligase carboxyl terminus of Hsc70-interacting protein. Moreover, carboxyl terminus of Hsc70-interacting protein was found to be involved in the TSA-mediated inhibitory effect on IFN-γ induction of TRIM22 as well as other IRF-1–dependent IFN-stimulated genes. This study may provide novel insight into the role of HDAC activity in the transcriptional control of IFN-stimulated gene induction.

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Section: Discussionsupporting

confidence: 73%

Inhibition of Histone Deacetylase Activity Suppresses IFN-γ Induction of Tripartite Motif 22 via CHIP-Mediated Proteasomal Degradation of IRF-1

Gao

Wang

et al. 2013

The Journal of Immunology

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“…Since in a previous study, Ahmed et al (2012) reported that the chaperone-assisted E3 ligase C terminus of Hsc70-interacting protein (CHIP), the chaperone associated E3 ligase, induces ubiquitination and regulates the proteasomal turnover of PTEN, we investigated if Hsp27 interacts significantly with CHIP (Fig. 5d).…”

Section: Resultsmentioning

confidence: 99%

Downregulation of Hsp27 (HSPB1) in MCF-7 human breast cancer cells induces upregulation of PTEN

Cayado-Gutiérrez

Moncalero

Rosales

et al. 2013

Cell Stress and Chaperones

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“…Some ubiquitin ligases (CHIP) link chaperones and the 26S proteasome machinery by ubiquitinating chaperone substrates and channeling them toward the proteasome (76)(77)(78). Chaperones are among the proteins increased to the highest levels (ϳ16.7-to 27-fold) in the MAM of HCMV-infected cells (37).…”

Section: Discussionmentioning

confidence: 99%

Human Cytomegalovirus Inhibits Apoptosis by Proteasome-Mediated Degradation of Bax at Endoplasmic Reticulum-Mitochondrion Contacts

Zhang

Hildreth

Colberg-Poley

2013

J Virol

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Human cytomegalovirus (HCMV) encodes the UL37 exon 1 protein (pUL37x1), which is the potent viral mitochondrion-localized inhibitor of apoptosis (vMIA), to increase survival of infected cells. HCMV vMIA traffics from the endoplasmic reticulum (ER) to ER subdomains, which are physically linked to mitochondria known as mitochondrion-associated membranes (MAM), and to mitochondria. The antiapoptotic function of vMIA is thought to primarily result from its ability to inhibit Bax-mediated permeabilization of the outer mitochondrial membrane (OMM). Here, we establish that vMIA retargets Bax to the MAM as well as to the OMM from immediate early through late times of infection. However, MAM localization of Bax results in its increased ubiquitination and proteasome-mediated degradation. Surprisingly, HCMV infection does not increase OMM-associated degradation (OMMAD) of Bax, even though the ER and mitochondria are physically connected at the MAM. It was recently found that lipid rafts at the plasma membrane can connect extrinsic and intrinsic apoptotic pathways and can serve as sites of apoptosome assembly. In transfected permissive human fibroblasts, vMIA mediates, through its cholesterol affinity, association of Bax and apoptosome components with MAM lipid rafts. While Bax association with MAM lipid rafts was detected in HCMV-infected cells, association of apoptosome components was not. These results establish that Bax recruitment to the MAM and its MAMassociated degradation (MAMAD) are a newly described antiapoptotic mechanism used by HCMV infection to increase cell survival for its growth.

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The Chaperone-assisted E3 Ligase C Terminus of Hsc70-interacting Protein (CHIP) Targets PTEN for Proteasomal Degradation

Cited by 138 publications

References 56 publications

Inhibition of Histone Deacetylase Activity Suppresses IFN-γ Induction of Tripartite Motif 22 via CHIP-Mediated Proteasomal Degradation of IRF-1

Inhibition of Histone Deacetylase Activity Suppresses IFN-γ Induction of Tripartite Motif 22 via CHIP-Mediated Proteasomal Degradation of IRF-1

Downregulation of Hsp27 (HSPB1) in MCF-7 human breast cancer cells induces upregulation of PTEN

Human Cytomegalovirus Inhibits Apoptosis by Proteasome-Mediated Degradation of Bax at Endoplasmic Reticulum-Mitochondrion Contacts

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