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The p97-FAF1 protein complex reveals a common mode of p97 adaptor binding.


ABSTRACT: 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-?B 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 ? 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.

SUBMITTER: Ewens CA 

PROVIDER: S-EPMC4002113 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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The p97-FAF1 protein complex reveals a common mode of p97 adaptor binding.

Ewens Caroline A CA   Panico Silvia S   Kloppsteck Patrik P   McKeown Ciaran C   Ebong Ima-Obong IO   Robinson Carol C   Zhang Xiaodong X   Freemont Paul S PS  

The Journal of biological chemistry 20140311 17


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  ...[more]

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