Three decades of studies to understand the functions of the ubiquitin family.

Methods in Molecular Biology
A Varshavsky

Abstract

Many intracellular proteins are metabolically unstable or can become unstable during their lifetime in a cell. The in vivo half-lives of specific proteins range from less than a minute to many days. Among the functions of intracellular proteolysis are the elimination of misfolded or otherwise abnormal proteins; maintenance of amino acid pools in cells affected by stresses such as starvation; and generation of protein fragments that act as hormones, antigens, or other effectors. One major function of proteolytic pathways is the selective destruction of proteins whose concentrations must vary with time and alterations in the state of a cell. Short in vivo half-lives of such proteins provide a way to generate their spatial gradients and to rapidly adjust their concentration or subunit composition through changes in the rate of their degradation. The regulated (and processive) degradation of intracellular proteins is carried out largely by the ubiquitin-proteasome system (Ub system), in conjunction with autophagy-lysosome pathways. Other contributors to intracellular proteolysis include cytosolic and nuclear proteases, such as caspases, calpains, and separases. They often function as "upstream" components of the Ub system, which de...Continue Reading

Citations

Aug 14, 2012·Transcription·Gary Ee, Norbert Lehming
Dec 29, 2016·Proceedings of the National Academy of Sciences of the United States of America·Peter TsvetkovSusan Lindquist
May 1, 2021·International Journal of Molecular Sciences·Sara Martín-VillanuevaJesús de la Cruz

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