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Origin and function of ubiquitin-like proteins

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  • Mark Hochstrasser

    (Yale University, 266 Whitney Avenue, PO Box 208114, New Haven, Connecticut 06520, USA.)

Abstract

Eukaryotic proteins can be modified through attachment to various small molecules and proteins. One such modification is conjugation to ubiquitin and ubiquitin-like proteins (UBLs), which controls an enormous range of physiological processes. Bound UBLs mainly regulate the interactions of proteins with other macromolecules, for example binding to the proteasome or recruitment to chromatin. The various UBL systems use related enzymes to attach specific UBLs to proteins (or other molecules), and most of these attachments are transient. There is increasing evidence suggesting that such UBL–protein modification evolved from prokaryotic sulphurtransferase systems or related enzymes. Moreover, proteins similar to UBL-conjugating enzymes and UBL-deconjugating enzymes seem to have already been widespread at the time of the last common ancestor of eukaryotes, suggesting that UBL–protein conjugation did not first evolve in eukaryotes.

Suggested Citation

  • Mark Hochstrasser, 2009. "Origin and function of ubiquitin-like proteins," Nature, Nature, vol. 458(7237), pages 422-429, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7237:d:10.1038_nature07958
    DOI: 10.1038/nature07958
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    Cited by:

    1. Olga Boix & Marion Martinez & Santiago Vidal & Marta Giménez-Alejandre & Lluís Palenzuela & Laura Lorenzo-Sanz & Laura Quevedo & Olivier Moscoso & Jorge Ruiz-Orera & Pilar Ximénez-Embún & Nikaoly Ciri, 2022. "pTINCR microprotein promotes epithelial differentiation and suppresses tumor growth through CDC42 SUMOylation and activation," Nature Communications, Nature, vol. 13(1), pages 1-22, December.
    2. Weiji Weng & Xiaokun Gu & Yang Yang & Qiao Zhang & Qi Deng & Jie Zhou & Jinke Cheng & Michael X. Zhu & Junfeng Feng & Ou Huang & Yong Li, 2023. "N-terminal α-amino SUMOylation of cofilin-1 is critical for its regulation of actin depolymerization," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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