@article {Twomeyeaax1033,
	title = {Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding},
	journal = {Science},
	year = {2019},
	publisher = {American Association for the Advancement of Science},
	abstract = {The Cdc48 ATPase (p97 or VCP in mammals) and its cofactor Ufd1/Npl4 extract poly-ubiquitinated proteins from membranes or macromolecular complexes for subsequent degradation by the proteasome. How Cdc48 processes its diverse and often well-folded substrates is unclear. Here, we report cryo-EM structures of the Cdc48 ATPase in complex with Ufd1/Npl4 and poly-ubiquitinated substrate. The structures show that the Cdc48 complex initiates substrate processing by unfolding a ubiquitin molecule. The unfolded ubiquitin molecule binds to Npl4 and projects its N-terminal segment through both hexameric ATPase rings. Pore loops of the second ring form a staircase that acts as a conveyer belt to move the polypeptide through the central pore. Inducing the unfolding of ubiquitin allows the Cdc48 ATPase complex to process a broad range of substrates.},
	issn = {0036-8075},
	doi = {10.1126/science.aax1033},
	url = {https://science.sciencemag.org/content/early/2019/06/26/science.aax1033},
	author = {Twomey, Edward C. and Ji, Zhejian and Wales, Thomas E. and Bodnar, Nicholas O. and Ficarro, Scott B. and Marto, Jarrod A. and Engen, John R. and Rapoport, Tom A.}
}
