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TitleThe p97-FAF1 protein complex reveals a common mode of p97 adaptor binding.
Journal, issue, pagesJ Biol Chem, Vol. 289, Issue 17, Page 12077-12084, Year 2014
Publish dateApr 25, 2014
AuthorsCaroline A Ewens / Silvia Panico / Patrik Kloppsteck / Ciaran McKeown / Ima-Obong Ebong / Carol Robinson / Xiaodong Zhang / Paul S Freemont /
PubMed Abstractp97, also known as valosin-containing protein, is a versatile participant in the ubiquitin-proteasome system. p97 interacts with a large network of adaptor proteins to process ubiquitylated ...p97, also known as valosin-containing protein, is a versatile participant in the ubiquitin-proteasome system. p97 interacts with a large network of adaptor proteins to process ubiquitylated substrates in different cellular pathways, including endoplasmic reticulum-associated degradation and transcription factor activation. p97 and its adaptor Fas-associated factor-1 (FAF1) both have roles in the ubiquitin-proteasome system during NF-κB activation, although the mechanisms are unknown. FAF1 itself also has emerging roles in other cell-cycle pathways and displays altered expression levels in various cancer cell lines. We have performed a detailed study the p97-FAF1 interaction. We show that FAF1 binds p97 stably and in a stoichiometry of 3 to 6. Cryo-EM analysis of p97-FAF1 yielded a 17 Å reconstruction of the complex with FAF1 above the p97 ring. Characteristics of p97-FAF1 uncovered in this study reveal common features in the interactions of p97, providing mechanistic insight into how p97 mediates diverse functionalities.
External linksJ Biol Chem / PubMed:24619421 / PubMed Central
MethodsEM (single particle)
Resolution17.0 Å
Structure data

EMDB-2319:
Cryo-EM of full-length p97-FAF1 protein complex
Method: EM (single particle) / Resolution: 17.0 Å

Source
  • Mus musculus (house mouse)

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