Phosphorylation articles within Nature

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  • Article
    | Open Access

    Analysis of the kinase activity of 300 protein Ser/Thr kinases reveals that the substrate specificity of the kinome is substantially more diverse than expected and is driven extensively by negative selectivity

    • Jared L. Johnson
    • , Tomer M. Yaron
    •  & Lewis C. Cantley

  • Article
    | Open Access

    The core cell cycle is largely driven by increasing total CDK activity together with minor differences in the substrate specificity of the CDKs initiating DNA replication and mitosis.

    • Souradeep Basu
    • , Jessica Greenwood
    •  & Paul Nurse

  • Article |

    MARK4 regulates cardiomyocyte contractility by promoting MAP4 phosphorylation, which facilitates the access of VASH2 to microtubules for the detyrosination of α-tubulin; MARK4 deficiency after acute myocardial infarction limits the reduction in the left ventricular ejection fraction.

    • Xian Yu
    • , Xiao Chen
    •  & Xuan Li

  • Article |

    Inhibition of YBX1, a downstream target of the Janus kinase JAK2, sensitizes myeloproliferative neoplasm cells to JAK and could provide a means to eradicate such cells in human haematopoietic cancers.

    • Ashok Kumar Jayavelu
    • , Tina M. Schnöder
    •  & Florian H. Heidel

  • Article |

    Chaperones interact with a canonical motif in α-synuclein, which can be prevented by phosphorylation of α-synuclein at Tyr39, whereas inhibition of this interaction leads to the localization of α-synuclein to the mitochondria and aggregate formation.

    • Björn M. Burmann
    • , Juan A. Gerez
    •  & Sebastian Hiller

  • Article |

    ERK reversibly regulates embryonic stem cell transcription via selective redistribution of co-factors and RNA polymerase from pluripotency to early differentiation enhancers, while leaving transcription factors bound to their enhancers, thus preserving plasticity.

    • William B. Hamilton
    • , Yaron Mosesson
    •  & Joshua M. Brickman

  • Letter |

    The stress-activated kinase p38γ has a role in regulating entry into the cell cycle; in the liver, it can induce cellular proliferation during regeneration and promote the development of hepatocellular carcinoma.

    • Antonia Tomás-Loba
    • , Elisa Manieri
    •  & Guadalupe Sabio

  • Letter |

    Phosphorylation of one of two adjacent serine residues in TSC2 is both required and sufficient for PKG1-mediated cardiac protection against pressure overload in mice; these serine residues provide a genetic tool for the bidirectional regulation of stress-stimulated mTORC1 activity.

    • Mark J. Ranek
    • , Kristen M. Kokkonen-Simon
    •  & David A. Kass

  • Article |

    Stabilization of a transient protein kinase–substrate complex using a nanobody provides molecular details about how the Parkinson’s disease-linked protein kinase PINK1 phosphorylates ubiquitin, and suggests new pharmacological strategies.

    • Alexander F. Schubert
    • , Christina Gladkova
    •  & David Komander

  • Article |

    The PINK1 ubiquitin kinase is shown to recruit the two autophagy receptors NDP52 and OPTN to mitochondria to activate mitophagy directly, independently of the ubiquitin ligase parkin; once recruited to mitochondria, NDP52 and OPTN recruit autophagy initiation components, and parkin may amplify the phospho-ubiquitin signal generated by PINK1, resulting in robust autophagy induction.

    • Michael Lazarou
    • , Danielle A. Sliter
    •  & Richard J. Youle

  • News & Views |

    The orchestration of cell division requires a programme of events choreographed by protein modification. A study shows that the relative activity of a phosphatase enzyme towards its substrates imposes order during the final act of division.

    • Curt Wittenberg

  • Letter |

    Two classes of enzyme — cyclin-dependent kinases (CDK) and Dbf4-dependent kinase (DDK) — facilitate the initiation of DNA replication in eukaryotes. It is now shown that, when DNA damage is sensed, another kinase, Rad53, halts the firing of late replication origins by inhibiting both the CDK and the DDK pathways. Rad53 acts on DDK directly by inhibiting Dbf4, whereas the CDK pathway is blocked by Rad53-mediated phosphorylation of the downstream CDK substrate Sld3.

    • Jaime Lopez-Mosqueda
    • , Nancy L. Maas
    •  & David P. Toczyski

  • Letter |

    Two classes of enzyme — cyclin-dependent kinases (CDK) and Dbf4-dependent kinase (DDK) — facilitate the initiation of DNA replication in eukaryotes. It is now shown that, when DNA damage is sensed, another kinase, Rad53, halts the firing of late replication origins by inhibiting both the CDK and the DDK pathways. Rad53 acts on DDK directly by inhibiting Dbf4, whereas the CDK pathway is blocked by Rad53-mediated phosphorylation of the downstream CDK substrate Sld3.

    • Philip Zegerman
    •  & John F. X. Diffley

  • Letter |

    The chromosomal passenger complex (CPC) coordinates several processes during cell division, including chromosome bi-orientation and cytokinesis, and its proper localization is crucial. These authors provide a mechanism for its localization to the inner centromere. Cdk1–cyclin-B-dependent phosphorylation of the CPC promotes binding to shugoshin, which the authors define as a conserved centromeric adaptor of the CPC. This mechanism is conserved between fission yeast and human cells and highlights a crucial role of Cdk1–cyclin B in chromosome bi-orientation.

    • Tatsuya Tsukahara
    • , Yuji Tanno
    •  & Yoshinori Watanabe

  • Letter |

    The initiation of protein synthesis requires the eukaryotic translation initiation factor (eIF) 2, which uses energy from the hydrolysis of GTP. Another factor, eIF5, accelerates the GTP-hydrolysing activity of eIF2. Here, two other roles for eIF5 have been defined. One involves stabilizing GDP, the product of GTP hydrolysis, on eIF2. In its other role, eIF5 works with phosphorylated eIF2 to inhibit the guanine-nucleotide exchange factor eIF2B. These results clarify our understanding of how the initiation of translation is regulated.

    • Martin D. Jennings
    •  & Graham D. Pavitt

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