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Proximity labeling reveals dynamic changes in the SQSTM1 protein network

ABSTRACT: Sequestosome1 (SQSTM1) is an autophagy receptor that mediates degradation of intracellular cargo, including protein aggregates, through multiple protein interactions. These interactions form the SQSTM1 protein network that are mediated by SQSTM1 functional interaction domains, which include LIR, PB1, UBA and KIR. Despite various attempts to unravel the complexity of the SQSTM1 protein network, our understanding of the relationship of various components in cellular physiology and disease states continues to evolve. To investigate the SQSTM1 protein interaction network, we performed proximity profile labeling by fusing TurboID with the human protein SQSTM1 (TurboID::SQSTM1). This chimeric protein displayed well-established SQSTM1 features including: production of SQSTM1 intracellular bodies, binding to known SQSTM1 interacting partners via defined functional SQSTM1 interacting domains and capture of novel SQSTM1 interactors. Strikingly, aggregated tau protein altered the protein interaction network of SQSTM1 to include many stress associated proteins. Overall, our work reveals the dynamic landscape of the SQSTM1 protein network and offers a resource to study SQSTM1 function in cellular physiology and disease state.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Alejandro Rondon Ortiz

LAB HEAD: Ben Wolozin

PROVIDER: PXD047725 | Pride | 2024-08-06

REPOSITORIES: Pride

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			Action	DRS
	FIG1-20220817_ARO_LYS_TurboID-1.raw	Raw
	FIG1-20220817_ARO_LYS_TurboID-2.raw	Raw
	FIG1-20220817_ARO_LYS_TurboID-3.raw	Raw
	FIG1-20220817_ARO_LYS_TurboID-4.raw	Raw
	FIG1-20220817_ARO_p62_P62-1.raw	Raw

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