RING Fingers and Relatives: Determinators of Protein Fate

Lorick, Kevin L.; Tsai, Ya Chea; Yang, Yili; Weissman, Allan M.

doi:10.1002/9783527619320.ch4

Cited by 3 publications

(4 citation statements)

References 374 publications

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“…While some E2s from higher eukaryotes match the names of their yeast counterparts, in many cases they do not. Table clarifies some of the confusion (Lorick et al, , b). Accession numbers provided are current GenBank reference sequences where available.…”

Section: Generation Of Ubiquitin‐conjugating Enzymes (E2s)mentioning

confidence: 92%

“…Such multi‐subunit E3s include the SCF complexes, the anaphase‐promoting complex, or cyclosome, and the CBC E3s (Iwai et al, 1999; Skowyra et al, 1999; Chan et al, 2001). For most RING‐finger proteins, it is currently thought that the RING finger and substrate‐recognition element are encoded on a single polypeptide (Lorick et al, ).…”

Section: In Vitro Production Of Ubiquitin‐protein Ligases (E3s)mentioning

confidence: 99%

“…There is evidence to suggest, however, that they are not merely docking sites for E2s. (Lorick et al, ).…”

Section: Commentarymentioning

confidence: 99%

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Studies of the Ubiquitin Proteasome System

et al. 2006

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A concept that has arisen over the last decade is that proteins can, in general, be covalently modified by polypeptides, resulting in alterations in their fate and function. The first‐identified and most well studied of these modifying polypeptides is ubiquitin. Although targeting for proteasomal degradation is the best studied outcome of ubiquitylation, we now understand that modification of proteins with ubiquitin has numerous other cellular roles that alter protein function and that are unrelated to proteasomal degradation. Ubiquitylation is a complex process that is regulated at the level of both addition and removal of ubiquitin from target proteins. This unit includes a number of different basic protocols that will facilitate the study of components of the ubiquitin system and substrate ubiquitylation both in vitro and in cells. Because another protein modifier, NEDD8, itself regulates aspects of the ubiquitin system, basic protocols on neddylation are also included in this unit.

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Section: Generation Of Ubiquitin‐conjugating Enzymes (E2s)mentioning

confidence: 92%

Section: In Vitro Production Of Ubiquitin‐protein Ligases (E3s)mentioning

confidence: 99%

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Studies of the Ubiquitin Proteasome System

et al. 2006

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“…Ubiquitin ligases (E3s) have a central role in the process of protein modification with UBIQ (known as 'ubiquitination' or 'ubiquitylation'); they recognize specific substrates and facilitate UBIQ transfer from the E2 onto the substrate. Although the precise number of human E3s is unknown, about 500 or more have been proposed to exist [ 2 - 5 ], supportive of the broad role for the ubiquitin system in regulating diverse cellular processes. Ubiquitin-like proteins (UBLs) have also been identified with varying degrees of identity to UBIQ and are conjugated onto proteins through similar enzymatic cascades as UBIQ.…”

Section: Broad Overview Of Familymentioning

confidence: 99%

The ubiquitin system, disease, and drug discovery

2008

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The ubiquitin system of protein modification has emerged as a crucial mechanism involved in the regulation of a wide array of cellular processes. As our knowledge of the pathways in this system has grown, so have the ties between the protein ubiquitin and human disease. The power of the ubiquitin system for therapeutic benefit blossomed with the approval of the proteasome inhibitor Velcade in 2003 by the FDA. Current drug discovery activities in the ubiquitin system seek to (i) expand the development of new proteasome inhibitors with distinct mechanisms of action and improved bioavailability, and (ii) validate new targets. This review summarizes our current understanding of the role of the ubiquitin system in various human diseases ranging from cancer, viral infection and neurodegenerative disorders to muscle wasting, diabetes and inflammation.

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Protein Degradation

Mayer

Ciechanover²,

Rechsteiner

2005

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RING Fingers and Relatives: Determinators of Protein Fate

Cited by 3 publications

References 374 publications

Studies of the Ubiquitin Proteasome System

Studies of the Ubiquitin Proteasome System

The ubiquitin system, disease, and drug discovery

Protein Degradation

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