UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97 (original) (raw)

Abstract.

The highly conserved AAA ATPase Cdc48/p97 acts on ubiquitylated substrate proteins in cellular processes as diverse as the fusion of homotypic membranes and the degradation of misfolded proteins. The ‘Ubiquitin regulatory X’ (UBX) domain-containing proteins constitute the so far largest family of Cdc48/p97 cofactors. UBX proteins are involved in substrate recruitment to Cdc48/p97 and in the temporal and spatial regulation of its activity. In combination with UBX-like proteins and other cofactors, they can assemble into a large variety of Cdc48/p97-cofactor complexes possessing distinct cellular functions. This review gives an overview of the different subfamilies of UBX proteins and their functions, and discusses general principles of Cdc48/p97 regulation by these cofactors.

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Authors and Affiliations

  1. Cell Biology and Biophysics Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117, Heidelberg, Germany
    C. Schuberth
  2. Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany
    A. Buchberger

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  1. C. Schuberth
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  2. A. Buchberger
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Correspondence toC. Schuberth or A. Buchberger.

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Received 8 February 2008; received after revision 12 March 2008; accepted 14 March 2008

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Schuberth, C., Buchberger, A. UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97.Cell. Mol. Life Sci. 65, 2360–2371 (2008). https://doi.org/10.1007/s00018-008-8072-8

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