Dendritic Cell IL-1α and IL-1β Are Polyubiquitinated and Degraded by the Proteasome

Ainscough, Joseph S.; Gerberick, G. Frank; Zahedi-Nejad, Maryam; López-Castejón, Gloria; Brough, David; Kimber, Ian; Dearman, Rebecca J.

doi:10.1074/jbc.m114.595686

Cited by 54 publications

(49 citation statements)

References 56 publications

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“…Ϫ/Ϫ cells likely reflects the pro-IL-1␤ ubiquitination and proteosomal clearance pathway recently described by Ainscough et al (33). We also verified the absence of ASC oligomerization in response to both acute and sustained nigericin stimulation in Nlrp3…”

Section: Decrease In Pro-il-1␤ Levels In Nlrp3supporting

confidence: 67%

Caspase-8 as an Effector and Regulator of NLRP3 Inflammasome Signaling

Antonopoulos

Russo

Sanadi³

et al. 2015

Journal of Biological Chemistry

181

145

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Background: NLRP3 inflammasomes regulate caspase-1-dependent IL-1␤ release and pyroptotic death in dendritic cells (DC) and macrophages. Results: Caspase-8 mediates IL-1␤ production and apoptosis by NLRP3 inflammasomes in caspase-1-deficient DC and facilitates pyroptosis in wild type DC. Conclusion: Caspase-8 is activated within NLRP3 inflammasome signaling platforms. Significance: In addition to caspase-1, NLRP3 inflammasomes engage caspase-8 as an important effector of innate immune signaling responses.

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Section: Decrease In Pro-il-1␤ Levels In Nlrp3supporting

confidence: 67%

Caspase-8 as an Effector and Regulator of NLRP3 Inflammasome Signaling

Antonopoulos

Russo

Sanadi³

et al. 2015

Journal of Biological Chemistry

181

145

View full text Add to dashboard Cite

show abstract

“…Over time, plasma-membrane-bound pro-IL-1α can be released via cleavage with extracellular proteases 39,54,57 . The excess of intracellular pro-IL-1α is subjected to proteosomal degradation through ubiquitin-dependent mechanisms 58 .…”

Section: Il-1α Biogenesismentioning

confidence: 99%

Interleukin 1α and the inflammatory process

2016

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Inflammation occurs after disruption of tissue homeostasis by cell stress, injury or infection and ultimately involves the recruitment and retention of cells of hematopoietic origin, which arrive at the affected sites to resolve damage and initiate repair. Interleukin 1α (IL-1α) and IL-1β are equally potent inflammatory cytokines that activate the inflammatory process, and their deregulated signaling causes devastating diseases manifested by severe acute or chronic inflammation. Although much attention has been given to understanding the biogenesis of IL-1β, the biogenesis of IL-1α and its distinctive role in the inflammatory process remain poorly defined. In this review we examine key aspects of IL-1α biology and regulation and discuss its emerging importance in the initiation and maintenance of inflammation that underlie the pathology of many human diseases.

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“…Secreted mature IL-1β is not ubiquitinated, suggesting that deubiquitination occurs just before or during processing by the inflammasome. 53 One high-risk strain of human papillomavirus (HPV16) exploits this biology to evade the innate immune response. HPV16 harboring the E6 oncogene encodes the ubiquitin ligase E6-AP, which increases the ubiquitination and proteasomal degradation of pro-IL-1β.…”

Section: Il-1βmentioning

confidence: 99%