Reactome | PINK1 is autophosphorylated

PINK1 is autophosphorylated

Stable Identifier

R-HSA-9834076

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial outer membrane

ReviewStatus

3/5

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PTEN-induced putative kinase 1 (PINK1) is rapidly degraded in healthy mitochondria but the full length form of PINK1 accumulates on the mitochondrial outer membrane (MOM) of damaged mitochondria. Activation of PINK1 at MOM is achieved via dimerization-mediated trans-autophosphorylation of PINK1 at multiple sites including S228 and S402 (Okatsu K et al., 2012, 2013; Aerts L et al., 2015; Rasool S et al., 2018, 2022; Gan ZY et al., 2022). Structural insights suggest that autophosphorylation triggers a conformational change in the N-terminal lobe of PINK1, enabling substrate binding (Gan ZY et al., 2022; Rasool S et al., 2022).

Literature References

PubMed ID	Title	Journal	Year
24189060	A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment Okatsu, K, Uno, M, Koyano, F, Go, E, Kimura, M, Oka, T, Tanaka, K, Matsuda, N	J Biol Chem	2013
25527497	PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402 Aerts, L, Craessaerts, K, De Strooper, B, Morais, VA	J Biol Chem	2015