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. 1984 May;37(1):57-66.
doi: 10.1016/0092-8674(84)90300-3.

Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85

A Ciechanover, D Finley, A Varshavsky

Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85

A Ciechanover et al. Cell. 1984 May.

Abstract

We have shown that covalent conjugation of ubiquitin to proteins is temperature-sensitive in the mouse cell cycle mutant ts85 due to a specifically thermolabile ubiquitin-activating enzyme (accompanying paper). We show here that degradation of short-lived proteins is also temperature sensitive in ts85 , in contrast to wild-type and revertant cells. While more than 70% of the prelabeled abnormal proteins (containing amino acid analogs) or puromycyl peptides are degraded within 4 hr at the permissive temperature in both ts85 and wild-type cells, less than 15% are degraded in ts85 cells at the nonpermissive temperature. Degradation of abnormal proteins and puromycyl peptides in both ts85 cells and wild-type cells is nonlysosomal and ATP-dependent. Immunochemical analysis shows a strong and specific reduction in the levels of in vivo labeled ubiquitin-protein conjugates at the nonpermissive temperature in ts85 cells. Degradation of normal, short-lived proteins is also specifically temperature sensitive in ts85 . We suggest that the contribution of ubiquitin-independent pathways to the degradation of short-lived proteins in this higher eucaryotic cell is no more than 10%, and possibly less.

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Comment in

  • Back to the future with ubiquitin.
    Pickart CM. Pickart CM. Cell. 2004 Jan 23;116(2):181-90. doi: 10.1016/s0092-8674(03)01074-2. Cell. 2004. PMID: 14744430 Review.
  • Ubiquitin as a central cellular regulator.
    Finley D, Ciechanover A, Varshavsky A. Finley D, et al. Cell. 2004 Jan 23;116(2 Suppl):S29-32, 2 p following S32. doi: 10.1016/s0092-8674(03)00971-1. Cell. 2004. PMID: 15055578 No abstract available.

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