Swarupa Panda
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Swarupa Panda has a total of 2 co-authors. Here are the top co-authors by number of shared publications:
- Amitha Kamath
Department of Ageing Research, Manipal School of Life Science, Manipal Academy of higher Education, Manipal, India
1 shared publication - Nelson Ong'Ondo Gekara
Institute of Medical Microbiology and Hygiene, Medical Center - University of Freiburg, Faculty of Medicine, Freiburg, Germany
1 shared publication
Latest Publications
- Open Access
K27-linked ubiquitination restrains the NOD2-RIP2 signaling pathway
Nucleotide-binding oligomerization domain 2 (NOD2) signaling is a critical arm of host defense and immune homeostasis but requires strict regulation to prevent self-injury. Central to this regulation is the polyubiquitination of the adaptor protein RIP2, yet the precise ubiquitin linkages and their dynamic control remain incompletely understood. Here, we identify K27-linked polyubiquitination of RIP2 by the E3 ligase XIAP as a novel inhibitory signal that attenuates RIP2 complex assembly and downstream NF-κB activation, thereby fine-tuning NOD2-induced inflammatory signaling. We show that XIAP-mediated K63-linked ubiquitination promotes NOD2-RIP2 activation, whereas K27-linked ubiquitination impairs the recruitment of TAK1 and NEMO to the NOD2-RIP2 complex, dampening downstream signaling and cytokine production. We further demonstrate that this regulation is counterbalanced by the deubiquitinase MYSM1, which selectively removes K27-, K63-. and M1-polyubiquitin chains via its SWIRM-MPN domains to restore balanced signaling. Together, these findings define a dynamic XIAP-RIP2-MYSM1 axis in which opposing ubiquitin linkages fine-tune NOD2 responses, establishing a molecular rheostat for immune signaling with implications for inflammatory disease pathogenesis and opportunities for targeted therapeutic intervention.
Open AccessK27-linked ubiquitination restrains the NOD2-RIP2 signaling pathway
Nucleotide-binding oligomerization domain 2 (NOD2) signaling is a critical arm of host defense and immune homeostasis but requires strict regulation to prevent self-injury. Central to this regulation is the polyubiquitination of the adaptor protein RIP2, yet the precise ubiquitin linkages and their dynamic control remain incompletely understood. Here, we identify K27-linked polyubiquitination of RIP2 by the E3 ligase XIAP as a novel inhibitory signal that attenuates RIP2 complex assembly and downstream NF-κB activation, thereby fine-tuning NOD2-induced inflammatory signaling. We show that XIAP-mediated K63-linked ubiquitination promotes NOD2-RIP2 activation, whereas K27-linked ubiquitination impairs the recruitment of TAK1 and NEMO to the NOD2-RIP2 complex, dampening downstream signaling and cytokine production. We further demonstrate that this regulation is counterbalanced by the deubiquitinase MYSM1, which selectively removes K27-, K63-. and M1-polyubiquitin chains via its SWIRM-MPN domains to restore balanced signaling. Together, these findings define a dynamic XIAP-RIP2-MYSM1 axis in which opposing ubiquitin linkages fine-tune NOD2 responses, establishing a molecular rheostat for immune signaling with implications for inflammatory disease pathogenesis and opportunities for targeted therapeutic intervention.