Dataset Information

BAG5 functionally interacts with the autophagy adaptor protein p62

ABSTRACT: Molecular chaperones are critical to maintaining intracellular proteostasis and have been shown to have a protective role against alpha-synuclein mediated toxicity. Co-chaperone proteins regulate the activity of molecular chaperones and connect the chaperone network to protein degradation and cell death pathways. Bcl-2 associated athanogene 5 (BAG5) is a co-chaperone that modulates proteostasis by inhibiting the activity of Hsp70 and several E3 ubiquitin ligases, resulting in enhanced neurodegeneration in models of Parkinson’s disease (PD). Here we identify a novel interaction between BAG5 and p62/sequestosome-1 (SQSTM1), suggesting that BAG5 may bridge the chaperone network to autophagy-mediated protein degradation. The interaction was discovered using affinity purifaction followed by mass spectrometry to identify BAG5 interacting proteins and was validated by subsequent in vitro immunoprecipitation studies.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Erik Friesen

LAB HEAD: Suneil Kalia

PROVIDER: PXD019473 | Pride | 2020-08-05

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	Erik-DARA-IP (peptides_1_0_0.mzid).mzid_Erik-DARA-IP_(peptides_1_0_0.mzid).pride.mgf.gz	Mzid
	Erik-DARA-IP (peptides_1_0_0.mzid).pride.mztab.gz	Mztab
	Erik-DARA-IPpeptides_1_0_0.mzid.mzid.gz	Mzid
	Erik-DARA-IPpeptides_1_0_0.mzid.mzid_Erik-DARA-IP_peptides_1_0_0.mzid.MGF	Mzid
	Erik-GB5-IP (peptides_1_0_0.mzid).mzid_Erik-GB5-IP_(peptides_1_0_0.mzid).pride.mgf.gz	Mzid

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Publications

BAG5 Promotes Alpha-Synuclein Oligomer Formation and Functionally Interacts With the Autophagy Adaptor Protein p62.

Friesen Erik L EL Zhang Yu Tong YT Earnshaw Rebecca R De Snoo Mitch L ML O'Hara Darren M DM Agapova Victoria V Chau Hien H Ngana Sophie S Chen Kevin S KS Kalia Lorraine V LV Kalia Suneil K SK

Frontiers in cell and developmental biology 20200804

Molecular chaperones are critical to maintaining intracellular proteostasis and have been shown to have a protective role against alpha-synuclein-mediated toxicity. Co-chaperone proteins regulate the activity of molecular chaperones and connect the chaperone network to protein degradation and cell death pathways. Bcl-2 associated athanogene 5 (BAG5) is a co-chaperone that modulates proteostasis by inhibiting the activity of Heat shock protein 70 (Hsp70) and several E3 ubiquitin ligases, resultin ...[more]

PMID: 32850835

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