Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.

doi:10.1038/ncomms13047

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Article

Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.

Nature communications - 20 Oct 2016

Arumughan Anup, Roske Yvette, Barth Carolin, Forero Laura Lleras, Bravo-Rodriguez Kenny, Redel Alexandra, Kostova Simona, McShane Erik, Opitz Robert, Faelber Katja, Rau Kirstin, Mielke Thorsten, Daumke Oliver, Selbach Matthias, Sanchez-Garcia Elsa, Rocks Oliver, Panáková Daniela, Heinemann Udo, Wanker Erich E

Abstract excerpt

Interaction mapping is a powerful strategy to elucidate the biological function of protein assemblies and their regulators. Here, we report the generation of a quantitative interaction network, directly linking 14 human proteins to the AAA+ ATPase p97, an essential hexameric protein with multiple cellular functions. We show that the high-affinity interacting protein ASPL efficiently promotes p97 hexamer...

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PMID: 27762274
DOI: 10.1038/ncomms13047
PMCID: PMC5080433

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Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.PMID 27762274Read ↗

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