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. Author manuscript; available in PMC: 2023 Nov 24.
Published in final edited form as: Cell Rep. 2023 Oct 17;42(10):113260. doi: 10.1016/j.celrep.2023.113260

Figure 3. PINK1 autophosphorylation is not necessary for emergence of PINK1 input threshold or input-reciprocal delay behaviors.

Figure 3.

(A) PINK1 domain map. MTS and transmembrane (TM) domain replaced by FKBP domain (Figure 1C). ND: N-terminal domain. CD: C-terminal domain. S228: primary functional PINK1 autophosphorylation site.

(B) Illustration of S228 mutant consequences. S228D: phosphomimicking and non-phosphorylateable. S228A: non-phosphorylateable.

(C) Effects of PINK1 S228 mutations on circuit behavior. Points: aggregate quantification from fixed-cell measurements in Figure S4B.

(D) Statistical analysis of input threshold and delay scaler values for data in (C). Mean, 95% confidence intervals, and statistical significance calculated by bootstrap analysis (B = 10,000; STAR Methods). Bonferroni multiple comparison adjustment. **p < 0.01; ***p < 0.001. See also Figure S4.