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Article

Structural insights into ubiquitin phosphorylation by PINK1.

Scientific reports - 10 Jul 2018

Okatsu Kei, Sato Yusuke, Yamano Koji, Matsuda Noriyuki, Negishi Lumi, Takahashi Akiko, Yamagata Atsushi, Goto-Ito Sakurako, Mishima Masaki, Ito Yutaka, Oka Toshihiko, Tanaka Keiji, Fukai Shuya

Abstract excerpt

Mutations of PTEN-induced putative kinase 1 (PINK1) and the E3 ubiquitin (Ub) ligase parkin can cause familial parkinsonism. These two proteins are essential for ubiquitylation of damaged mitochondria and subsequent degradation. PINK1 phosphorylates Ser65 of Ub and the Ub-like (UBL) domain of parkin to allosterically relieve the autoinhibition of parkin. To understand the structural mechanism of the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 29991771
DOI: 10.1038/s41598-018-28656-8
PMCID: PMC6039469

Genes

PINK1
PTEN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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