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Article

Ubiquitin is phosphorylated by PINK1 to activate parkin.

Nature - 5 Jun 2014

Koyano Fumika, Okatsu Kei, Kosako Hidetaka, Tamura Yasushi, Go Etsu, Kimura Mayumi, Kimura Yoko, Tsuchiya Hikaru, Yoshihara Hidehito, Hirokawa Takatsugu, Endo Toshiya, Fon Edward A, Trempe Jean-François, Saeki Yasushi, Tanaka Keiji, Matsuda Noriyuki

Abstract excerpt

PINK1 (PTEN induced putative kinase 1) and PARKIN (also known as PARK2) have been identified as the causal genes responsible for hereditary recessive early-onset Parkinsonism. PINK1 is a Ser/Thr kinase that specifically accumulates on depolarized mitochondria, whereas parkin is an E3 ubiquitin ligase that catalyses ubiquitin transfer to mitochondrial substrates. PINK1 acts as an upstream factor for parkin and is...

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Source

Identifiers

PMID: 24784582
DOI: 10.1038/nature13392

Genes

PINK1
PTEN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Ubiquitin is phosphorylated by PINK1 to activate parkin.PMID 24784582Read ↗

PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagySemantic proximity Read ↗

Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.Semantic proximity Read ↗

PINK1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease.Semantic proximity Read ↗

Phosphorylation of Parkin at serine 65 is essential for its activation in vivoSemantic proximity Read ↗

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation.Semantic proximity Read ↗

PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control.Semantic proximity Read ↗

Mechanism of phospho-ubiquitin-induced PARKIN activation.Semantic proximity Read ↗

Ubiquitin phosphorylation in Parkinson’s disease: Implications for pathogenesis and treatmentSemantic proximity Read ↗

A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment.Semantic proximity Read ↗

Structure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation.Semantic proximity Read ↗

The principal <scp>PINK1</scp> and Parkin cellular events triggered in response to dissipation of mitochondrial membrane potential occur in primary neuronsSemantic proximity Read ↗

A Ubl/ubiquitin switch in the activation of ParkinSemantic proximity Read ↗

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