Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b

Autor: Marietta S. Kaspers, Vivian Pogenberg, Christian Pett, Stefan Ernst, Felix Ecker, Philipp Ochtrop, Michael Groll, Christian Hedberg, Aymelt Itzen

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)

Abstract Bacterial pathogens often make use of post-translational modifications to manipulate host cells. Legionella pneumophila, the causative agent of Legionnaires disease, secretes the enzyme AnkX that uses cytidine diphosphate-choline to post-tra

Externí odkaz: https://doaj.org/article/24651e6d5226410298bde574e8f3a727

Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1

Autor: Jiqing Du, Marie-Kristin von Wrisberg, Burak Gulen, Matthias Stahl, Christian Pett, Christian Hedberg, Kathrin Lang, Sabine Schneider, Aymelt Itzen

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)

The Legionella effector DrrA AMPylates the host protein Rab1 during infection, but the mechanism is still under debate. Here, the authors provide structural insights into the low-affinity DrrA:Rab1 interaction, showing that Rab1 allosterically activa

Externí odkaz: https://doaj.org/article/db46eaf2179e4b49abbf39b105a93816

Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation

Autor: Dorothea Höpfner, Joel Fauser, Marietta S. Kaspers, Christian Pett, Christian Hedberg, Aymelt Itzen

Publikováno v: iScience, Vol 23, Iss 12, Pp 101800- (2020)

Summary: AMPylation is a post-translational modification that modifies amino acid side chains with adenosine monophosphate (AMP). Recently, a role of AMPylation as a universal regulatory mechanism in infection and cellular homeostasis has emerged, dr

Externí odkaz: https://doaj.org/article/555092eab7f54de6a6233f1f99eb48b5

Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD

Autor: Martin Zacharias, Christian Hedberg, Christoph Krisp, Joel Fauser, Matthias J. Feige, Christian Pett, Aymelt Itzen, Dorothea Höpfner, Danial Pourjafar-Dehkordi, Burak Gulen, Gesa König, Hartmut Schlüter, Vivian Pogenberg

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications 12(1), 2426 (2021). doi:10.1038/s41467-021-22596-0
Nature Communications

Nature Communications 12(1), 2426 (2021). doi:10.1038/s41467-021-22596-0
To adapt to fluctuating protein folding loads in the endoplasmic reticulum (ER), the Hsp70 chaperone BiP is reversibly modified with adenosine monophosphate (AMP) by the ER

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d40798e1b2f32b1564e04d9e1ffc15f
https://doaj.org/article/5b881075f8d343709870eb7b338a3da3

Identification of targets of AMPylating Fic enzymes by co-substrate-mediated covalent capture

Autor: Christian Pett, Christian Hedberg, Burak Gulen, Hartmut Schlüter, Joel Fauser, Michael F. Albers, Vivian Pogenberg, Aymelt Itzen, Christoph Krisp, Marie Rosselin

Publikováno v: Nature Chemistry. 12:732-739

Various pathogenic bacteria use post-translational modifications to manipulate the central components of host cell functions. Many of the enzymes released by these bacteria belong to the large Fic family, which modify targets with nucleotide monophos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1baf586e4a4f86a1ece1f3455e018b1
https://doi.org/10.1038/s41557-020-0484-6