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Mouse lysosome - LC-DIA-IM-MS - Quantitative proteome analysis of mouse liver lysosomes provides evidence for mannose 6-phosphate-independent targeting mechanisms of acid hydrolases in mucolipidosis II

ABSTRACT: Quantitative profiling of new lysosomal proteins of unknown function. Mouse models with loss-of-function were analysed in order to identify putative substrates or to reveal impaired pathological pathways. Interaction partners were sought to elucidate the function of the non-transporter proteins.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Hans Vissers

LAB HEAD: Dr. Markus Damme

PROVIDER: PXD001556 | Pride | 2017-01-09

REPOSITORIES: Pride

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			Action	DRS
	GNPTAB_01_01.mzML	Mzml
	GNPTAB_01_01_Pride.pride.mgf.gz	Mgf
	GNPTAB_01_01_Pride.pride.mztab.gz	Mztab
	GNPTAB_01_01_Pride.xml.gz	Xml
	GNPTAB_01_02.mzML	Mzml

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Publications

Quantitative Proteome Analysis of Mouse Liver Lysosomes Provides Evidence for Mannose 6-phosphate-independent Targeting Mechanisms of Acid Hydrolases in Mucolipidosis II.

Markmann Sandra S Krambeck Svenja S Hughes Christopher J CJ Mirzaian Mina M Aerts Johannes M F G JM Saftig Paul P Schweizer Michaela M Vissers Johannes P C JP Braulke Thomas T Damme Markus M

Molecular & cellular proteomics : MCP 20170106 3

The efficient receptor-mediated targeting of soluble lysosomal proteins to lysosomes requires the modification with mannose 6-phosphate (M6P) residues. Although the absence of M6P results in misrouting and hypersecretion of lysosomal enzymes in many cells, normal levels of lysosomal enzymes have been reported in liver of patients lacking the M6P-generating phosphotransferase (PT). The identity of lysosomal proteins depending on M6P has not yet been comprehensively analyzed. In this study we puri ...[more]

PMID: 28062798

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