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TitleActivation mechanism of PINK1.
Journal, issue, pagesNature, Vol. 602, Issue 7896, Page 328-335, Year 2022
Publish dateDec 21, 2021
AuthorsZhong Yan Gan / Sylvie Callegari / Simon A Cobbold / Thomas R Cotton / Michael J Mlodzianoski / Alexander F Schubert / Niall D Geoghegan / Kelly L Rogers / Andrew Leis / Grant Dewson / Alisa Glukhova / David Komander /
PubMed AbstractMutations in the protein kinase PINK1 lead to defects in mitophagy and cause autosomal recessive early onset Parkinson's disease. PINK1 has many unique features that enable it to phosphorylate ...Mutations in the protein kinase PINK1 lead to defects in mitophagy and cause autosomal recessive early onset Parkinson's disease. PINK1 has many unique features that enable it to phosphorylate ubiquitin and the ubiquitin-like domain of Parkin. Structural analysis of PINK1 from diverse insect species with and without ubiquitin provided snapshots of distinct structural states yet did not explain how PINK1 is activated. Here we elucidate the activation mechanism of PINK1 using crystallography and cryo-electron microscopy (cryo-EM). A crystal structure of unphosphorylated Pediculus humanus corporis (Ph; human body louse) PINK1 resolves an N-terminal helix, revealing the orientation of unphosphorylated yet active PINK1 on the mitochondria. We further provide a cryo-EM structure of a symmetric PhPINK1 dimer trapped during the process of trans-autophosphorylation, as well as a cryo-EM structure of phosphorylated PhPINK1 undergoing a conformational change to an active ubiquitin kinase state. Structures and phosphorylation studies further identify a role for regulatory PINK1 oxidation. Together, our research delineates the complete activation mechanism of PINK1, illuminates how PINK1 interacts with the mitochondrial outer membrane and reveals how PINK1 activity may be modulated by mitochondrial reactive oxygen species.
External linksNature / PubMed:34933320 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.35 - 3.53 Å
Structure data

EMDB-25677:
Structure of dimeric phosphorylated Pediculus humanus (Ph) PINK1
Method: EM (single particle) / Resolution: 3.07 Å

25678

7t4k

EMDB-25678, PDB-7t4k:
Structure of dimeric phosphorylated Pediculus humanus (Ph) PINK1 with kinked alpha-C helix in chain B
Method: EM (single particle) / Resolution: 3.25 Å

25679

7t4l

EMDB-25679, PDB-7t4l:
Structure of dimeric phosphorylated Pediculus humanus (Ph) PINK1 with extended alpha-C helix in chain B
Method: EM (single particle) / Resolution: 3.28 Å

25680

7t4m

EMDB-25680, PDB-7t4m:
Structure of dodecameric unphosphorylated Pediculus humanus (Ph) PINK1 D357A mutant
Method: EM (single particle) / Resolution: 2.48 Å

25681

7t4n

EMDB-25681, PDB-7t4n:
Structure of dimeric unphosphorylated Pediculus humanus (Ph) PINK1 D357A mutant
Method: EM (single particle) / Resolution: 2.35 Å

PDB-7t3x:
Structure of unphosphorylated Pediculus humanus (Ph) PINK1 D334A mutant
Method: X-RAY DIFFRACTION / Resolution: 3.53 Å

Source
  • pediculus humanus corporis (human body louse)
KeywordsTRANSFERASE / PINK1 / Kinase / Mitophagy / Parkinson's Disease / Ubiquitin / Phosphorylation / Phospho-ubiquitin

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