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PINK1-TOM-TIM23 complex SDA XL-MS

ABSTRACT: 3xFLAG-tagged human wild-type PINK1 was expressed and immunoprecipitated with anti-FLAG beads. Chemical cross-linking MS (XL-MS) analysis using SDA and UV exposure was performed followed by in solution trypsin digestion and MS analysis.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Prof. David Komander

PROVIDER: PXD058526 | JPOST Repository | Thu May 29 00:00:00 GMT+01:00 2025

REPOSITORIES: jPOST

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			Action	DRS
	Human_Proteome_reviewed_May2021_P4563_mito_proteins.fasta	Fasta
	P4700_01.mgf	Mgf
	P4700_01.raw	Raw
	P4700_02.mgf	Mgf
	P4700_02.raw	Raw

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Publications

Structure of human PINK1 at a mitochondrial TOM-VDAC array.

Callegari Sylvie S Kirk Nicholas S NS Gan Zhong Yan ZY Dite Toby T Cobbold Simon A SA Leis Andrew A Dagley Laura F LF Glukhova Alisa A Komander David D

Science (New York, N.Y.) 20250313 6744

Mutations in the ubiquitin kinase PINK1 cause early-onset Parkinson's disease, but how PINK1 is stabilized at depolarized mitochondrial translocase complexes has remained poorly understood. We determined a 3.1-angstrom resolution cryo-electron microscopy structure of dimeric human PINK1 stabilized at an endogenous array of mitochondrial translocase of the outer membrane (TOM) and voltage-dependent anion channel (VDAC) complexes. Symmetric arrangement of two TOM core complexes around a central VD ...[more]

PMID: 40080546

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