The ubiquitin-mediated proteolytic pathway

enzymology and mechanisms of recognition of the proteolytic substrates.

Research output: Contribution to journalReview articleResearchpeer-review

8 Citations (Scopus)

Abstract

Degradation of proteins by the ubiquitin system involves two discrete steps. Initially, ubiquitin is covalently linked in an ATP-dependent mode to the protein substrate. The protein moiety of the conjugate is subsequently degraded by a specific protease into peptides and free amino acids with the release of free and reutilizable ubiquitin. The degradation process also requires energy. In this review we shall discuss the mechanisms involved in ubiquitin activation, selection of substrates for conjugation, and subsequent degradation of ubiquitin-conjugated proteins. In addition, we shall briefly summarize what is currently known of the role of the ubiquitin system in protein degradation in vitro and in vivo.

Original languageEnglish
Pages (from-to)415-422
Number of pages8
JournalSeminars in cell biology
Volume1
Issue number6
StatePublished - 1 Dec 1990

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Ubiquitin
Proteolysis
Proteins
Peptide Hydrolases
Adenosine Triphosphate
Amino Acids
Peptides

Cite this

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title = "The ubiquitin-mediated proteolytic pathway: enzymology and mechanisms of recognition of the proteolytic substrates.",
abstract = "Degradation of proteins by the ubiquitin system involves two discrete steps. Initially, ubiquitin is covalently linked in an ATP-dependent mode to the protein substrate. The protein moiety of the conjugate is subsequently degraded by a specific protease into peptides and free amino acids with the release of free and reutilizable ubiquitin. The degradation process also requires energy. In this review we shall discuss the mechanisms involved in ubiquitin activation, selection of substrates for conjugation, and subsequent degradation of ubiquitin-conjugated proteins. In addition, we shall briefly summarize what is currently known of the role of the ubiquitin system in protein degradation in vitro and in vivo.",
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The ubiquitin-mediated proteolytic pathway : enzymology and mechanisms of recognition of the proteolytic substrates. / Ciechanover, Aaron; Gonen, H.

In: Seminars in cell biology, Vol. 1, No. 6, 01.12.1990, p. 415-422.

Research output: Contribution to journalReview articleResearchpeer-review

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N2 - Degradation of proteins by the ubiquitin system involves two discrete steps. Initially, ubiquitin is covalently linked in an ATP-dependent mode to the protein substrate. The protein moiety of the conjugate is subsequently degraded by a specific protease into peptides and free amino acids with the release of free and reutilizable ubiquitin. The degradation process also requires energy. In this review we shall discuss the mechanisms involved in ubiquitin activation, selection of substrates for conjugation, and subsequent degradation of ubiquitin-conjugated proteins. In addition, we shall briefly summarize what is currently known of the role of the ubiquitin system in protein degradation in vitro and in vivo.

AB - Degradation of proteins by the ubiquitin system involves two discrete steps. Initially, ubiquitin is covalently linked in an ATP-dependent mode to the protein substrate. The protein moiety of the conjugate is subsequently degraded by a specific protease into peptides and free amino acids with the release of free and reutilizable ubiquitin. The degradation process also requires energy. In this review we shall discuss the mechanisms involved in ubiquitin activation, selection of substrates for conjugation, and subsequent degradation of ubiquitin-conjugated proteins. In addition, we shall briefly summarize what is currently known of the role of the ubiquitin system in protein degradation in vitro and in vivo.

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