IndraLab

Statements


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"We subsequently explored whether PINK1 directly binds to USP20 in the absence or presence of CCCP treatment."

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"Cell lysates were immunoprecipitated with anti-Flag antiserum, and immunoblotting with anti-Myc antibodies revealed that ectopically expressed USP20 binds to PINK1 (Fig.  xref A)."

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"Co-IP analysis revealed that ectopically expressed PINK1 interacts with USP20 in the basal state."

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"The model confidence score (pLDDT) of AlphaFold3-prediction and the average distance between both the N-lobe and C-lobe of PINK1 and USP20 (approximately 3–4 Å) supports a direct physical interaction between PINK1 and USP20 (Supple Fig. xref )."

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"To validate the endogenous interaction, we additionally conducted a Proximity Ligation Assay (PLA), which demonstrated that endogenous PINK1 interacts with USP20 in the cytosol (Fig.  xref H)."

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"Overall, our data indicates that USP20 binds to PINK1 in the cytosol of mammalian cells."

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"PINK1 Kinase Domain Interacts with the Catalytic Domain of USP20."

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"Future studies in neuronal and in vivo models are warranted to validate these findings and further elucidate the physiological and pathological relevance of the USP20PINK1 axis."

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"PINK1 interacts with USP20 when the intact kinase domain of PINK1 is present (Fig.  xref D)."

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"However, deletion of the N-lobe of the kinase domain abolished the PINK1 binding to USP20."

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"The predicted complex structure is further supported by examining the interaction of different PINK1 domains with USP20 (Fig.  xref E)."

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"PINK1 Interacts with USP20 in Mammalian Cells."