Blar i forfatter "McEwan, David G."

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    • Atg8 family proteins, LIR/AIM motifs and other interaction modes 

      Rogov, Vladimir V.; Nezis, Ioannis P.; Tsapras, P; Zhang, Hong; Dagdas, Yasin; Noda, Nobuo N; Nakatogawa, Hitoshi; Wirth, Martina; Mouilleron, Stephane; McEwan, David G.; Behrends, Christian; Deretic, Vojo P.; Elazar, Zvulun; Tooze, Sharon A.; Dikic, Ivan; Lamark, Trond; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-03-19)
      The Atg8 family of ubiquitin-like proteins play pivotal roles in autophagy and other processes involving vesicle fusion and transport where the lysosome/vacuole is the end station. Nuclear roles of Atg8 proteins are also emerging. Here, we review the structural and functional features of Atg8 family proteins and their protein-protein interaction modes in model organisms such as yeast, Arabidopsis, ...

    • Structural and functional analysis of a novel interaction motif within UFM1-activating enzyme 5 (UBA5) required for binding to ubiquitin-like proteins and ufmylation 

      Habisov, Sabrina; Huber, Jessica; Ichimura, Yoshinobu; Akutsu, Masato; Rogova, Natalia; Loehr, Frank; McEwan, David G.; Johansen, Terje; Dikic, Ivan; Doetsch, Volker; Komatsu, Masaaki; Rogov, Vladimir V; Kirkin, Vladimir (Journal article; Tidsskriftartikkel; Peer reviewed, 2016-02-29)
      The covalent conjugation of ubiquitin-fold modifier 1 (UFM1) to proteins generates a signal that regulates transcription, response to cell stress, and differentiation. Ufmylation is initiated by ubiquitin-like modifier activating enzyme 5 (UBA5), which activates and transfers UFM1 to ubiquitin-fold modifier-conjugating enzyme 1 (UFC1). The details of the interaction between UFM1 and UBA5 required ...