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Determining the Structural Basis of Cofactor and Substrate Interactions with Cdc48

Published online by Cambridge University Press:  30 July 2020

Ian Cooney
Affiliation:
University of Utah, Midvale, Utah, United States
Han Han
Affiliation:
University of Utah, Salt Lake City, Utah, United States
Chris Hill
Affiliation:
University of Utah, Salt Lake City, Utah, United States
Peter Shen
Affiliation:
University of Utah, Salt Lake City, Utah, United States

Abstract

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Type
3D Structures: From Macromolecular Assemblies to Whole Cells (3DEM FIG)
Copyright
Copyright © Microscopy Society of America 2020

References

Ye, Y, Tang, WK, Zhang, T, Xia, D. A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase. Front Mol Biosci. 2017;4:39.10.3389/fmolb.2017.00039CrossRefGoogle ScholarPubMed
Wiehl, CC, Dalal, S, Pestronk, A, Hanson, PI. Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation. Human Molecular Genetics. 2006;15(2):189-99. Epub 2005/12/01.10.1093/hmg/ddi426CrossRefGoogle Scholar
Qiu, L, Pashkova, N, Walker, JR, Winistorfer, S, Allali-Hassani, A, Akutsu, M, Piper, R, Dhe-Paganon S. Structure and function of the PLAA/Ufd3-p97/Cdc48 complex. J Biol Chem. 2010;285(1):365-72. doi: 10.1074/jbc.M109.044685. Epub 2009/11/02.CrossRefGoogle ScholarPubMed
Banerjee, S, Bartesaghi, A, Merk, A, Rao, P, Bulfer, SL, Yan, Y, Green, N, Mroczkowski, B, Neitz, RJ, Wipf, P, Falconieri, V, Deshaies, RJ, Milne, JL, Huryn, D, Arkin, M, Subramaniam, S. A resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition. Science. 2016;351(6275):871-5. Epub 2016/01/28.10.1126/science.aad7974CrossRefGoogle ScholarPubMed
Bodnar, NO, Kim, KH, Ji, Z, Wales, TE, Svetlov, V, Nudler, E, Engen, JR, Walz, T, Rapoport, TA. Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nature Structural Molecular Biology. 2018;25(7):616-622. Epub 2018/07/02.10.1038/s41594-018-0085-xCrossRefGoogle ScholarPubMed
Cheng, YL, Chen, RH. Assembly and quality control of the protein phosphatase 1 holoenzyme involves the Cdc48-Shp1 chaperone. Journal of Cell Science. 2015;128(6):1180-92. Epub 2015/01/22.10.1242/jcs.165159CrossRefGoogle ScholarPubMed
Cooney, I., Han, H., Stewart, M.G., Carson, R.H., Hansen, D.T., Iwasa, J.H., Price, J.C., Hill, C.P. and Shen, P.S. Structure of the Cdc48 segregase in the act of unfolding an authentic substrate. Science. 2019;365(6452):502-505. Epub 2019/06/27. doi: 10.1126/science.aax0486CrossRefGoogle ScholarPubMed
Han, H, Monroe, N, Sundquist, WI, Shen, PS, Hill, CP. The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets. Elife. 2017;6:e31324.10.7554/eLife.31324CrossRefGoogle ScholarPubMed