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Mapping of a N-terminal alpha-helix domain required for human PINK1 stabilisation, Serine228 autophosphorylation and activation in cells

ABSTRACT: Comparative hydrogen deuterium exchange mass spectrometry of WT and I507A mutant for above titled manuscript.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: James Ault

LAB HEAD: Miratul Muqit

PROVIDER: PXD030382 | Pride | 2022-02-17

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	108-end_apo-I507A.DnX	Other
	I507A.zip	Other
	WT.zip	Other
	temp_cluster_dundee.csv	Csv
	temp_state_dundee.csv	Csv

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Publications

Mapping of a N-terminal α-helix domain required for human PINK1 stabilization, Serine228 autophosphorylation and activation in cells.

Kakade Poonam P Ojha Hina H Raimi Olawale G OG Shaw Andrew A Waddell Andrew D AD Ault James R JR Burel Sophie S Brockmann Kathrin K Kumar Atul A Ahangar Mohd Syed MS Krysztofinska Ewelina M EM Macartney Thomas T Bayliss Richard R Fitzgerald Julia C JC Muqit Miratul M K MMK

Open biology 20220119 1

Autosomal recessive mutations in the <i>PINK1</i> gene are causal for Parkinson's disease (PD). PINK1 encodes a mitochondrial localized protein kinase that is a master-regulator of mitochondrial quality control pathways. Structural studies to date have elaborated the mechanism of how mutations located within the kinase domain disrupt PINK1 function; however, the molecular mechanism of PINK1 mutations located upstream and downstream of the kinase domain is unknown. We have employed mutagenesis st ...[more]

PMID: 35042401

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