Post-translational modifications articles within Nature Communications

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  • Article |

    Acetylation of tubulin is proposed to be an important mechanism for the regulation of microtubule stability and diversity. Kalebic et al. generate mice lacking α-tubulin acetyltransferase activity, and reveal that an apparent absence of detectable tubulin acetylation is associated with impaired sperm motility.

    • Nereo Kalebic
    • , Simona Sorrentino
    •  & Paul A. Heppenstall

  • Article |

    Erm methyltransferases confer antimicrobial drug resistance and their expression is induced by macrolides. Gupta et al.show that Erm-catalysed modification of rRNA affects synthesis of some proteins and reduces cell fitness, explaining why expression of Erm is deleterious in the absence of antibiotics.

    • Pulkit Gupta
    • , Shanmugapriya Sothiselvam
    •  & Alexander S. Mankin

  • Article
    | Open Access

    The organized initiation of DNA replication at sites throughout the genome must be carefully choreographed to maintain genome stability. Bonne-Andrea and colleagues show that protein SUMOylation controls the density of origin firing, and identify cyclin E as an important substrate in this context.

    • Catherine Bonne-Andrea
    • , Malik Kahli
    •  & Olivier Coux

  • Article |

    Mono-ADP-ribosylation is a recently discovered post-translational modification whose function remains unclear. Verheugd et al. show that the mono-ADP-ribosyltransferase ARTD10 inhibits NF-κB activation by preventing the poly-ubiquitination of NEMO, suggesting a functional link between these two modifications.

    • Patricia Verheugd
    • , Alexandra H. Forst
    •  & Bernhard Lüscher

  • Article
    | Open Access

    Vascular endothelial-cadherin is a junctional protein implicated in the control of vascular permeability. Orsenigo et al.find that vascular endothelial-cadherin is phosphorylated in veins but not in arteries of mice, and that this sensitizes vessels to rapid changes in permeability in response to inflammatory mediators.

    • Fabrizio Orsenigo
    • , Costanza Giampietro
    •  & Elisabetta Dejana

  • Article |

    The sulfation of protein tyrosine residues is a common post-translational modification in eukaryotes. Here, Han et al.show that the protein RaxST, produced by a plant bacterium, has tyrosine sulfotransferase activity, demonstrating for the first time tyrosine sulfation in prokaryotes.

    • Sang-Wook Han
    • , Sang-Won Lee
    •  & Pamela C. Ronald

  • 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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