Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation

Jennifer K. Dowling; Christine E. Becker; Nollaig M. Bourke; Sinead C. Corr; Dympna J. Connolly; Susan R. Quinn; Paolo P. Pandolfi; Ashley Mansell; Luke A.J. O'Neill

doi:10.1074/jbc.M113.539692

Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation

Jennifer K. Dowling
, Christine E. Becker
, Nollaig M. Bourke
, Sinead C. Corr
, Dympna J. Connolly
, Susan R. Quinn
, Paolo P. Pandolfi
, Ashley Mansell
, Luke A.J. O'Neill

Research output: Contribution to journal › Article › peer-review

Abstract

Background: ASC is the common adaptor of caspase-1 activation in several inflammasomes. Results: A novel interaction between PML and ASC is identified. PML-deficient macrophages display enhanced levels of IL-1β secretion and higher levels of ASC in the cytosol. Conclusion: PML retains ASC in the nucleus limiting inflammasome activation. Significance: Understanding the regulation of inflammasome components will aid in the development of therapeutics to alleviate IL-1β-mediated diseases.

Original language	English
Pages (from-to)	6429-6437
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	289
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M113.539692
Publication status	Published - 7 Mar 2014
Externally published	Yes

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SDG 3 Good Health and Well-being

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10.1074/jbc.M113.539692

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@article{f4d305946e6a4a9882f5d9fd554b58f0,

title = "Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation",

abstract = "Background: ASC is the common adaptor of caspase-1 activation in several inflammasomes. Results: A novel interaction between PML and ASC is identified. PML-deficient macrophages display enhanced levels of IL-1β secretion and higher levels of ASC in the cytosol. Conclusion: PML retains ASC in the nucleus limiting inflammasome activation. Significance: Understanding the regulation of inflammasome components will aid in the development of therapeutics to alleviate IL-1β-mediated diseases.",

author = "Dowling, \{Jennifer K.\} and Becker, \{Christine E.\} and Bourke, \{Nollaig M.\} and Corr, \{Sinead C.\} and Connolly, \{Dympna J.\} and Quinn, \{Susan R.\} and Pandolfi, \{Paolo P.\} and Ashley Mansell and O'Neill, \{Luke A.J.\}",

year = "2014",

month = mar,

day = "7",

doi = "10.1074/jbc.M113.539692",

language = "English",

volume = "289",

pages = "6429--6437",

journal = "Journal of Biological Chemistry",

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publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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TY - JOUR

T1 - Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation

AU - Dowling, Jennifer K.

AU - Becker, Christine E.

AU - Bourke, Nollaig M.

AU - Corr, Sinead C.

AU - Connolly, Dympna J.

AU - Quinn, Susan R.

AU - Pandolfi, Paolo P.

AU - Mansell, Ashley

AU - O'Neill, Luke A.J.

PY - 2014/3/7

Y1 - 2014/3/7

N2 - Background: ASC is the common adaptor of caspase-1 activation in several inflammasomes. Results: A novel interaction between PML and ASC is identified. PML-deficient macrophages display enhanced levels of IL-1β secretion and higher levels of ASC in the cytosol. Conclusion: PML retains ASC in the nucleus limiting inflammasome activation. Significance: Understanding the regulation of inflammasome components will aid in the development of therapeutics to alleviate IL-1β-mediated diseases.

AB - Background: ASC is the common adaptor of caspase-1 activation in several inflammasomes. Results: A novel interaction between PML and ASC is identified. PML-deficient macrophages display enhanced levels of IL-1β secretion and higher levels of ASC in the cytosol. Conclusion: PML retains ASC in the nucleus limiting inflammasome activation. Significance: Understanding the regulation of inflammasome components will aid in the development of therapeutics to alleviate IL-1β-mediated diseases.

UR - https://www.scopus.com/pages/publications/84896780899

U2 - 10.1074/jbc.M113.539692

DO - 10.1074/jbc.M113.539692

M3 - Article

C2 - 24407287

AN - SCOPUS:84896780899

SN - 0021-9258

VL - 289

SP - 6429

EP - 6437

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 10

ER -

Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation

Abstract

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