Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Name Email address

Details on Person PTEN-induced putative kinase 1 (PINK1) is rapidly degraded i...

Class:IdSummation:9834075
_displayNamePTEN-induced putative kinase 1 (PINK1) is rapidly degraded i...
_timestamp2023-10-16 22:23:20
created[InstanceEdit:9834059] Shamovsky, Veronica, 2023-05-05
literatureReference[LiteratureReference:9835099] Activation mechanism of PINK1
[LiteratureReference:9835089] Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex
[LiteratureReference:9835091] PINK1 autophosphorylation is required for ubiquitin recognition
[LiteratureReference:9834925] PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
[LiteratureReference:9834922] A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment
[LiteratureReference:9834065] PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402
modified[InstanceEdit:9835108] Shamovsky, Veronica, 2023-05-11
[InstanceEdit:9838806] Shamovsky, Veronica, 2023-06-26
[InstanceEdit:9843343] Shamovsky, Veronica, 2023-09-06
[InstanceEdit:9851289] Shamovsky, Veronica, 2023-10-16
textPTEN-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).
(summation)[Reaction:9834076] PINK1 is autophosphorylated [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by PTEN-induced putative kinase 1 (PINK1) is rapidly degraded i... (9834075)
Follow Reactome