IndraLab

Statements

MYSM1 dephosphorylates RIPK2. 4 / 4
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"As a deubiquitinase, MYSM1 may not directly dephosphorylate RIPK2; instead, it likely recruits other phosphatases during inflammation."
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"Dephosphorylated and deubiquitinated RIPK2 downstream of MYSM1 maintains articular cartilage homeostasis by antagonizing NF-κB and MAPK signaling in OA.As a deubiquitinase, MYSM1 may not directly dephosphorylate RIPK2; instead, it likely recruits other phosphatases during inflammation."
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"These results suggest that the phosphorylation of RIPK2 is essential for RIPK2 ubiquitination, and MYSM1 reduces the phosphorylation and ubiquitination of RIPK2 with the assistance of PP2A (Fig. 7)."
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"Interestingly, MYSM1 notably enhanced the role of PP2A in dephosphorylating RIPK2, as indicated by the pS176 levels (Fig. 6j, k)."
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