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Ubiquitin fusion degradation

Lindsten K, de Vrij FM, Verhoef LG et al. (2002) Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J Cell Biol 157(3), 417-427. [Pg.95]

Wojcik C, Rowicka M, Kudlicki A et al. (2006) Valosin-containing protein (p97) is a regulator of ER stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells. Mol Biol Cell 17(11), 4606-4618. [Pg.215]

UbcS 16 abnormal proteins, sporulation, resistance to stress conditions, degradation of MATa2 and ubiquitin-fusion proteins, endocytosis of membrane proteins... [Pg.103]

Mitochondrial dynamics (fission, fusion, migration) has been reported to play an important role in neurotransmission, synaptic stability, and maintenance and neuronal survival. PBMKl and Parkin are closely associated within the regulation of mitochondrial dynamics and function (Bueler, 2009). Mutations in DJ-1, Parkin, and PINK 1 render animals more susceptible to oxidative stress and mitochondrial toxins implicated in sporadic PD. DJ-1, Parkin, and PINKl form a complex (termed PPD complex) to promote ubiquitination and degradation of Parkin substrates, including Parkin itself and synphilin-1. In addition, mutant proteins may retard the transport of nuclear-encoded mitochondrial proteins to mitochondria, interact with mitochondrial proteins and disrupt the electron transport chain, induce free radicals, cause... [Pg.352]

Other DUBs have been found to associate with membranes and regulate membrane-associated cellular processes, although they appear not to be membrane anchored like UBP16. The ability of DOA4 to remove ubiquitin from membrane-bound endocytic substrates promotes their degradation in the vacuole or lysosome [71]. DUBs are also important for membrane fusion events as shown by the fact that an OTU domain DUB, VCIP135 (VCP/p47 complex-interacting protein of... [Pg.202]


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See also in sourсe #XX -- [ Pg.17 ]




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