Ubiquitylation

Ubiquitylation is the post-translational modification process by which ubiquitin is attached via an isopeptide bond to lysine residues on a protein. Ubiquitylation consists of three steps, activation by ubiquitin-activating enzymes (E1 enzymes), conjugation by ubiquitin-conjugating enzymes (E2s) and attachment to the substrate protein by ubiquitin ligases (E3s).

Latest Research and Reviews

  • Research | | open

    How intracellular cAMP activate PKA is well-characterized, but PKA inactivation remains poorly understood. Here, Rinaldi et al. show that CHIP/HSP70 ubiquitinates the catalytic subunit of PKA, with implications for the human disease spinocerebellar ataxia 16, as patients often have CHIP mutations.

    • Laura Rinaldi
    • , Rossella Delle Donne
    • , Bruno Catalanotti
    • , Omar Torres-Quesada
    • , Florian Enzler
    • , Federica Moraca
    • , Robert Nisticò
    • , Francesco Chiuso
    • , Sonia Piccinin
    • , Verena Bachmann
    • , Herbert H Lindner
    • , Corrado Garbi
    • , Antonella Scorziello
    • , Nicola Antonino Russo
    • , Matthis Synofzik
    • , Ulrich Stelzl
    • , Lucio Annunziato
    • , Eduard Stefan
    •  & Antonio Feliciello
  • Research |

    Many tumors evade immunosurveillance by down-modulating expression of antigen-processing machinery and MHC molecules. Yang et al. report triple-negative tumor cell expression of the lncRNA LINK-A enhances degradation of antigen peptide-loading complex molecules and intrinsic tumor suppressors, which contribute to tumor persistence.

    • Qingsong Hu
    • , Youqiong Ye
    • , Li-Chuan Chan
    • , Yajuan Li
    • , Ke Liang
    • , Aifu Lin
    • , Sergey D. Egranov
    • , Yaohua Zhang
    • , Weiya Xia
    • , Jing Gong
    • , Yinghong Pan
    • , Sujash S. Chatterjee
    • , Jun Yao
    • , Kurt W. Evans
    • , Tina K. Nguyen
    • , Peter K. Park
    • , Jiewei Liu
    • , Cristian Coarfa
    • , Sri Ramya Donepudi
    • , Vasanta Putluri
    • , Nagireddy Putluri
    • , Arun Sreekumar
    • , Chandrashekar R. Ambati
    • , David H. Hawke
    • , Jeffrey R. Marks
    • , Preethi H. Gunaratne
    • , Abigail S. Caudle
    • , Aysegul A. Sahin
    • , Gabriel N. Hortobagyi
    • , Funda Meric-Bernstam
    • , Lieping Chen
    • , Dihua Yu
    • , Mien-Chie Hung
    • , Michael A. Curran
    • , Leng Han
    • , Chunru Lin
    •  & Liuqing Yang
    Nature Immunology 20, 835-851
  • Research | | open

    Wwp2 is an HECT-type E3 ubiquitin ligase abundantly expressed in articular cartilage. Here, the authors show that in mice, loss of Wwp2 leads to upregulated Runx2-Adamts5 signaling in articular cartilage and development of osteoarthritis, and that disease severity is reduced by injection of Wwp2 mRNA

    • Sho Mokuda
    • , Ryo Nakamichi
    • , Tokio Matsuzaki
    • , Yoshiaki Ito
    • , Tempei Sato
    • , Kohei Miyata
    • , Masafumi Inui
    • , Merissa Olmer
    • , Eiji Sugiyama
    • , Martin Lotz
    •  & Hiroshi Asahara
  • Research | | open

    Post-translational protein modifications can affect lifespan and aging but age-dependent ubiquitylation changes have not yet been systematically characterized. Here, the authors analyze age-related proteome and ubiquitylome dynamics in Drosophila and identify increasing H2A ubiquitylation as a conserved aging marker.

    • Lu Yang
    • , Zaijun Ma
    • , Han Wang
    • , Kongyan Niu
    • , Ye Cao
    • , Le Sun
    • , Yang Geng
    • , Bo Yang
    • , Feng Gao
    • , Zuolong Chen
    • , Zhen Wu
    • , Qingqing Li
    • , Yong Shen
    • , Xumin Zhang
    • , Hong Jiang
    • , Yelin Chen
    • , Rui Liu
    • , Nan Liu
    •  & Yaoyang Zhang

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