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Enzymatic Machinery of Ubiquitin and Ubiquitin-Like Modification Systems in Chondrocyte Homeostasis and Osteoarthritis

  • Osteoarthritis (M Goldring and T Griffin, Section Editors)
  • Published:
Current Rheumatology Reports Aims and scope Submit manuscript

Abstract

Purpose of Review

To date, a vast amount of information regarding ubiquitination (Ub) and ubiquitylation-like (Ubl) modification–related mechanisms has been reported in the context of skeletal cell homeostasis and diseases. In this review, we mainly focus on recent findings regarding the contribution of enzymatic machinery that directly adds or removes Ub and Ubl modifications from protein targets in chondrocyte homeostasis and osteoarthritis (OA) development.

Recent Findings

Mechanisms that promote homeostasis of articular chondrocytes are crucial for maintaining the integrity of articular joints to prevent osteoarthritis development. Articular chondrocytes are postmitotic cells that continuously produce and remodel cartilage matrix. In addition, the long lifespan of chondrocytes makes them susceptible to accumulating cellular damage. Ub and the evolutionarily conserved Ubl modifications, such as SUMOylation, ATGylation, and UFMylation, play important roles in promoting chondrocyte homeostasis, including regulating cell signaling and protein stability, resolving cellular stresses and inflammation, and maintaining differentiation and survival of chondrocytes.

Summary

Uncovering new components/functions of Ub/Ubl modification machinery may provide novel drug targets to treat OA.

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The paper is supported by funding NIH/NIA R01AG061086 and the Arthritis National Research Foundation (ANRF).

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  1. Department of Cell Biology, Van Andel Institute, 333 Bostwick Ave NE, Grand Rapids, MI, 49503, USA

    Ye Liu, Vladimir Molchanov & Tao Yang

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  1. Ye Liu
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Liu, Y., Molchanov, V. & Yang, T. Enzymatic Machinery of Ubiquitin and Ubiquitin-Like Modification Systems in Chondrocyte Homeostasis and Osteoarthritis. Curr Rheumatol Rep 23, 62 (2021). https://doi.org/10.1007/s11926-021-01022-w

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