Fig. 8: Model of the regulation of FILIP1-mediated FLNc degradation. | Communications Biology

Fig. 8: Model of the regulation of FILIP1-mediated FLNc degradation.

From: Phosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C

Fig. 8

a Differentiation-dependent expression of FILIP1, FLNc and FLNa in skeletal muscle cells. b Akt- and PKCα-dependent dual-site phosphorylation occurs in the extended basophilic motif located in the unique insert in domain 20 of FLNc. Dual-site phosphorylation reduces binding to FILIP1 and ensures stability and high dynamics of FLNc in muscle cells. Activation of protein phosphatases (PP) may result in the dephosphorylation of FLNc and thus, FILIP binding promoting the removal of nonphosphorylated FLNc of low mobility and dynamics by the Bag3-machinery and chaperone-assisted selective autophagy (CASA). Ub, ubiquitin.

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