XIAP controls RIPK2 signaling by preventing its deposition in speck-like structures Article Swipe
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· 2019
· Open Access
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· DOI: https://doi.org/10.26508/lsa.201900346
The receptor interacting serine/threonine kinase 2 (RIPK2) is essential for linking activation of the pattern recognition receptors NOD1 and NOD2 to cellular signaling events. Recently, it was shown that RIPK2 can form higher order molecular structures in vitro. Here, we demonstrate that RIPK2 forms detergent insoluble complexes in the cytosol of host cells upon infection with invasive enteropathogenic bacteria. Formation of these structures occurred after NF-κB activation and depended on the caspase activation and recruitment domain of NOD1 or NOD2. Complex formation upon activation required RIPK2 autophosphorylation at Y474 and was influenced by phosphorylation at S176. We found that the E3 ligase X-linked inhibitor of apoptosis (XIAP) counteracts complex formation of RIPK2, accordingly mutation of the XIAP ubiquitylation sites in RIPK2 enhanced complex formation. Taken together, our work reveals novel roles of XIAP in the regulation of RIPK2 and expands our knowledge on the function of RIPK2 posttranslational modifications in NOD1/2 signaling.
Related Topics
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.26508/lsa.201900346
- https://www.life-science-alliance.org/content/lsa/2/4/e201900346.full.pdf
- OA Status
- gold
- Cited By
- 27
- References
- 65
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2965988115
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W2965988115Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.26508/lsa.201900346Digital Object Identifier
- Title
-
XIAP controls RIPK2 signaling by preventing its deposition in speck-like structuresWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2019Year of publication
- Publication date
-
2019-07-26Full publication date if available
- Authors
-
Kornelia Ellwanger, Selina Briese, Christine Arnold, Ioannis Kienes, Valentin J. Heim, Ueli Nachbur, Thomas A. KuferList of authors in order
- Landing page
-
https://doi.org/10.26508/lsa.201900346Publisher landing page
- PDF URL
-
https://www.life-science-alliance.org/content/lsa/2/4/e201900346.full.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.life-science-alliance.org/content/lsa/2/4/e201900346.full.pdfDirect OA link when available
- Concepts
-
XIAP, Autophosphorylation, Cell biology, Ubiquitin ligase, Chemistry, Signal transduction, Inhibitor of apoptosis, NOD2, Phosphorylation, Biology, Receptor, Protein kinase A, Biochemistry, Apoptosis, Caspase, Ubiquitin, Programmed cell death, Gene, Innate immune systemTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
27Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 7, 2023: 5, 2022: 4, 2021: 3, 2020: 6Per-year citation counts (last 5 years)
- References (count)
-
65Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| citation_normalized_percentile.value | 0.80822983 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |