Fig. 5: Fortilin binds CTNNA3, an anti-apoptotic protein, protects it against phosphorylation-induced ubiquitination and proteasomal degradation. | Communications Biology

Fig. 5: Fortilin binds CTNNA3, an anti-apoptotic protein, protects it against phosphorylation-induced ubiquitination and proteasomal degradation.

From: Fortilin binds CTNNA3 and protects it against phosphorylation, ubiquitination, and proteasomal degradation to guard cells against apoptosis

Fig. 5

FT fortilin, P phosphorus, Ub ubiquitin molecule. The figure represents a proposed model of the positive regulation by fortilin of CTNNA3. Under normal conditions, fortilin binds CTNNA3 and protects CTNNA3 against its phosphorylation, ubiquitination, and proteasome-mediated degradation, thereby maintaining cellular integrity (left panel, Fortilin (+)). Reduction of fortilin levels within the cell disrupts this protective mechanism, leading to increased phosphorylation, ubiquitination, and proteasome-mediated degradation of CTNNA3, resulting in increased apoptosis (right panel, Fortilin (–)).

Back to article page