Extended Data Fig. 3: MS-identified RYR1 phosphorylation and the predicted kinases and nearby ubiquitylation sites. | Nature Cell Biology

Extended Data Fig. 3: MS-identified RYR1 phosphorylation and the predicted kinases and nearby ubiquitylation sites.

From: Cancer-cell-secreted miR-122 suppresses O-GlcNAcylation to promote skeletal muscle proteolysis

Extended Data Fig. 3: MS-identified RYR1 phosphorylation and the predicted kinases and nearby ubiquitylation sites.

(a) IF of C2C12 myotubes showing colocalization of exogenously expressed HA-tagged RYR1 and an ER marker PDI. DAPI stains the nuclei. Bar=100 μm. (b) MS-identified phosphorylation in immunoprecipitated, endogenous RYR1 from C2C12 with OGT knockdown but not from control C2C12. (c) Scansite 4.0 analysis predicting kinases that can potentially phosphorylate the identified threonine. (d) PhosphoSitePlus analysis showing published phosphorylation and ubiquitylation sites in the surrounding region in human and mouse RYR1.

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