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Comment
. 1998 Mar 17;95(6):2727-30.
doi: 10.1073/pnas.95.6.2727.

The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death

A Ciechanover  1 , A L Schwartz
Affiliations
Comment

The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death

A Ciechanover et al. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
(A) The ubiquitin-proteasome pathway. Conjugation of ubiquitin to the target protein: 1) activation of ubiquitin by E1. 2) Transfer of the activated ubiquitin moiety to a member of the E2 family of enzymes. 3) Formation of a binary complex between E3 and the protein substrate. 4) Formation of a ternary E2-E3-protein substrate complex. 5) Transfer of the activated ubiquitin moiety from E2 to E3. 6) Synthesis of protein substrate-anchored polyubiquitin chain. 7) Recycling of E2 and E3. Degradation of the polyubiquitin-conjugated substrate by the proteasome: 8) Transfer of the protein substrate-ubiquitin adduct to the symmetrical 19S-20S-19S proteasome. 9) Transfer of the protein substrate-ubiquitin adduct to the putative asymmetrical 19S-20S-PA28 proteasome. 10) Generation of large peptides by the symmetrical 19S-20S-19S proteasome. 11) “Trimming” of the large peptides into precise antigenic epitopes in a two-step mechanism by the asymmetrical 19S-20S-PA28 or the symmetrical PA28-20S-PA28 proteasomes. 12) Generation of free amino acids by the symmetrical or asymmetrical PA28-containing proteasomes. 13) Recycling of ubiquitin by ubiquitin C-terminal hydrolases (isopeptidases). Ub-R denotes ubiquitin chain receptor (binding) subunit of the 19S complex. (B) The (αβ)3 structure of the PA28 complex.
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