Endogenous HMGB1 regulates autophagy

Tang, Daolin; Kang, Rui; Livesey, Kristen M.; Cheh, Chun-Wei; Farkas, Adam M.; Loughran, Patricia; Hoppe, George; Bianchi, Marco E.; Tracey, Kevin J.; Zeh, Herbert J.; Lotze, Michael T.

doi:10.1084/jem20710oia27

Cited by 163 publications

(284 citation statements)

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“…41 High mobility group box-1 (HMGB1), a chromatinassociated nuclear protein competes with BCL2 for interaction with BECN1 to promote autophagy. 47 The damage-associated molecular pattern and BNIP3 (BCL2/adenovirus E1B 19kDa interacting protein 3) or other proteins inhibit the BCL2-BECN1 complex to promote autophagy. 48 Significant recent compelling evidence suggests that cellular BCL2 plays a pivotal role in the selection of cell fate as well as on the emerging consequences.…”

Section: Discussionmentioning

confidence: 99%

PAWR-mediated suppression of BCL2 promotes switching of 3-azido withaferin A (3-AWA)-induced autophagy to apoptosis in prostate cancer cells

Rah¹,

Rasool²,

Nayak³

et al. 2015

Autophagy

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Section: Discussionmentioning

confidence: 99%

PAWR-mediated suppression of BCL2 promotes switching of 3-azido withaferin A (3-AWA)-induced autophagy to apoptosis in prostate cancer cells

Rah¹,

Rasool²,

Nayak³

et al. 2015

Autophagy

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“…Extracellular HMGB1 functions as a proinflammatory cytokine-like molecule by direct binding to TLR4 or indirectly binding with other molecules (41). In addition, HMGB1 can play an intracytoplasmic role as a regulator between macroautophagy and apoptosis (11,(42)(43)(44) and a sentinel molecule for viral nucleic acid sensing (45).…”

Section: Discussionmentioning

confidence: 99%

“…1C). Aggregation of a fragment of the Htt protein directly causes free radical production in vivo (36), and oxidative potential is important for the nucleocytoplasmic translocation of HMGB1 (11). To test whether ROS scavenging inhibits the translocation of HMGB1, NAC, a precursor of glutathione that acts as a scavenger for the OH radical, and Mito-tempo, a mitochondria-targeted antioxidant with superoxide and alkyl radical-scavenging properties, were treated.…”

Section: Hmgb1 Reduces Physical Stress-induced Protein Denaturation Imentioning

confidence: 99%

“…PolyQ aggregates tend to be eliminated by autophagy or lysosomal pathway (21), and HMGB1 is an important autophagy regulator (11). Therefore, we performed PLA to check the possibility that HMGB1-associated aggregates might be localized in autophagosomes.…”

Section: Administration Of Exogenous Rhmgb1 Protein Reduces the Formamentioning

confidence: 99%

“…HMGB1 was also shown to act as a late mediator of endotoxemia and sepsis in animal models and human patients (7)(8)(9)(10). HMGB1 moves to the cytoplasm via a redox-dependent mechanism and plays a role as a regulator between macroautophagy and apoptosis in the cytoplasm by binding to beclin-1 and dissociating from bcl-2 (11).…”

mentioning

confidence: 99%

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Chaperone-like Activity of High-Mobility Group Box 1 Protein and Its Role in Reducing the Formation of Polyglutamine Aggregates

Min

et al. 2013

The Journal of Immunology

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High-mobility group box 1 protein (HMGB1), which mainly exists in the nucleus, has recently been shown to function as a sentinel molecule for viral nucleic acid sensing and an autophagy regulator in the cytoplasm. In this study, we studied the chaperone-like activity of HMGB1 and found that HMGB1 inhibited the chemically induced aggregation of insulin and lysozyme, as well as the heat-induced aggregation of citrate synthase. HMGB1 also restored the heat-induced suppression of cytoplasmic luciferase activity as a reporter protein in hamster lung fibroblast O23 cells with expression of HMGB1. Next, we demonstrated that HMGB1 inhibited the formation of aggregates and toxicity caused by expanded polyglutamine (polyQ), one of the main causes of Huntington disease. HMGB1 directly interacted with polyQ on immunofluorescence and coimmunoprecipitation assay, whereas the overexpression of HMGB1 or exogenous administration of recombinant HMGB1 protein remarkably reduced polyQ aggregates in SHSY5Y cells and hmgb1−/− mouse embryonic fibroblasts upon filter trap and immunofluorescence assay. Finally, overexpressed HMGB1 proteins in mouse embryonic primary striatal neurons also bound to polyQ and decreased the formation of polyQ aggregates. To this end, we have demonstrated that HMGB1 exhibits chaperone-like activity and a possible therapeutic candidate in polyQ disease.

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The self‐association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors

et al. 2017

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Edited by Miguel De la RosaHigh mobility group box 1 (HMGB1), a chromatin protein, interacts with DNA and controls gene expression. However, when HMGB1 is released from apoptotic or damaged cells, it triggers proinflammatory reactions by interacting with various receptors, mainly receptor for advanced glycation end-products (RAGE) and toll-like receptors (TLRs). The self-association of HMGB1 has been found to be crucial for its DNA-related biological functions. It is influenced by several factors, such as ionic strength, pH, specific divalent metal cations, redox environment and acetylation. This self-association may also play a role in the interaction with RAGE and TLRs and the concomitant inflammatory responses. Future studies should address the potential role of HMGB1 self-association on its interactions with DNA, RAGE and TLRs, as well as the influence of physicochemical factors in different cellular environments on these interactions.

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Endogenous HMGB1 regulates autophagy

Cited by 163 publications

References 1 publication

PAWR-mediated suppression of BCL2 promotes switching of 3-azido withaferin A (3-AWA)-induced autophagy to apoptosis in prostate cancer cells

PAWR-mediated suppression of BCL2 promotes switching of 3-azido withaferin A (3-AWA)-induced autophagy to apoptosis in prostate cancer cells

Chaperone-like Activity of High-Mobility Group Box 1 Protein and Its Role in Reducing the Formation of Polyglutamine Aggregates

The self‐association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors

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