Post-translational modifications articles within Nature Communications

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  • Article |

    Methyltransferases modify cellular proteins in addition to DNA and histones. These authors identify a new family of lysine-specific methyltransferases and show that a member of this family, which is associated with tumour metastasis, methylates the ATP-dependent protein chaperone VCP/p97.

    • Stefan Kernstock
    • , Erna Davydova
    •  & Pål Ø. Falnes

  • Article
    | Open Access

    The kinase PINK1 is mutated in Parkinson's disease and accumulates in defective mitochondria, where it recruits Parkin. Here, PINK1 is shown to be autophosphorylated and this is required for the localization of PINK1 to mitochondria with a reduced membrane potential, and for the recruitment of Parkin.

    • Kei Okatsu
    • , Toshihiko Oka
    •  & Noriyuki Matsuda

  • Article
    | Open Access

    Protein L-isoaspartyl methyltransferase (PIMT) is a carboxyl methyltransferase, but its role in regulating the tumour suppressor p53 is unclear. Here, PIMT is shown to methylate p53, obstructing the tumour suppressor function of p53 through reduced protein levels and stability.

    • Jae-Cheol Lee
    • , Sung-Ung Kang
    •  & Jeung-Whan Han

  • Article
    | Open Access

    Tyrosyl DNA phosphodiesterase 1 (TDP1) repairs DNA breaks and is mutated in the disease Spinocerebellar Ataxia with Axonal Neuropathy. Here TDP1 is shown to be post-translationally modified by sumoylation of lysine 111, and cells carrying a mutation at this residue are inefficient at single-strand DNA break repair.

    • Jessica J.R. Hudson
    • , Shih-Chieh Chiang
    •  & Sherif F. El-Khamisy

  • Article |

    The Golgi membrane is fragmented during mitosis and is subsequently fused following cell division and this process is known to be controlled by ubiquitination. In this study, the ubiquitin ligase HACE1 is shown to be targeted to the Golgi membrane and is required for fusion after the completion of mitosis.

    • Danming Tang
    • , Yi Xiang
    •  & Yanzhuang Wang

  • Article |

    MITF is a transcription factor required for melanocyte development, which is activated in some melanomas. Zhao and colleagues show that USP13 removes ubiquitin from MITF, stabilizes MITF protein levels and enhances colony formation, suggesting that USP13 may be a therapeutic target in melanoma.

    • Xiansi Zhao
    • , Brian Fiske
    •  & David E Fisher

  • Article
    | Open Access

    Posttranslational modification of proteins by small ubiquitin-related modifier is a response to stress signalling in plants. Here, theArabdiposisprotein SIZ1 is shown to cause SUMOylation of nitrate reductases 1 and 2 and to increase their activity, suggesting that SIZ1 controls nitrate uptake via SUMOylation.

    • Bong Soo Park
    • , Jong Tae Song
    •  & Hak Soo Seo

  • Article
    | Open Access

    Complex diseases such as multiple sclerosis have both genetic and environmental components. This study demonstrates that variants of genes implicated in multiple sclerosis, and alterations in cellular metabolism and vitamin D3 levels, alterN-glycosylation, a post-translational modification causal of the disease in mice.

    • Haik Mkhikian
    • , Ani Grigorian
    •  & Michael Demetriou

  • Article |

    Phosphorylation of the microtubule-associated protein tau is associated with disease, but other post-translational modifications of tau are not well studied. Here, Cohenet al. study the acetylation of tau and suggest that this form of the protein may be associated with tauopathies.

    • Todd J. Cohen
    • , Jing L. Guo
    •  & Virginia M. Y. Lee

  • Article
    | Open Access

    Post-translational modifications are important in regulating protein function and turnover, and Ufm1 is part of a recently identified protein modification system. In this study, the authors show that Uba5, a component of the Ufm1 system, is important for regulating haematopoiesis and the differentiation of erythroid cells.

    • Kanako Tatsumi
    • , Harumi Yamamoto-Mukai
    •  & Masaaki Komatsu

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