Cargando…

An oligomeric state‐dependent switch in the ER enzyme FICD regulates AMPylation and deAMPylation of BiP

AMPylation is an inactivating modification that alters the activity of the major endoplasmic reticulum (ER) chaperone BiP to match the burden of unfolded proteins. A single ER‐localised Fic protein, FICD (HYPE), catalyses both AMPylation and deAMPylation of BiP. However, the basis for the switch in...

Descripción completa

Detalles Bibliográficos
Autores principales:	Perera, Luke A, Rato, Claudia, Yan, Yahui, Neidhardt, Lisa, McLaughlin, Stephen H, Read, Randy J, Preissler, Steffen, Ron, David
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	John Wiley and Sons Inc. 2019
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6826200/ https://www.ncbi.nlm.nih.gov/pubmed/31531998 http://dx.doi.org/10.15252/embj.2019102177

Ejemplares similares

FICD acts bi-functionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP
por: Preissler, Steffen, et al.
Publicado: (2016)

Catalytic deAMPylation in AMPylation-inhibitory/assistant forms of FICD protein
por: Liu, Meili, et al.
Publicado: (2023)

Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
por: Perera, Luke A., et al.
Publicado: (2021)

Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
por: Fauser, Joel, et al.
Publicado: (2021)

AMPylation targets the rate-limiting step of BiP’s ATPase cycle for its functional inactivation
por: Preissler, Steffen, et al.
Publicado: (2017)

AMPylation matches BiP activity to client protein load in the endoplasmic reticulum
por: Preissler, Steffen, et al.
Publicado: (2015)

FICD activity and AMPylation remodelling modulate human neurogenesis
por: Kielkowski, Pavel, et al.
Publicado: (2020)

A Ca(2+)-regulated deAMPylation switch in human and bacterial FIC proteins
por: Veyron, Simon, et al.
Publicado: (2019)

Infancy‐onset diabetes caused by de‐regulated AMPylation of the human endoplasmic reticulum chaperone BiP
por: Perera, Luke A, et al.
Publicado: (2023)

Adaptation to constant light requires Fic-mediated AMPylation of BiP to protect against reversible photoreceptor degeneration
por: Moehlman, Andrew T, et al.
Publicado: (2018)

AMPylation: Something Old is New Again
por: Woolery, Andrew R., et al.
Publicado: (2010)

Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes
por: Preissler, Steffen, et al.
Publicado: (2020)

MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP
por: Yan, Yahui, et al.
Publicado: (2019)

In silico identification of AMPylating enzymes and study of their divergent evolution
por: Khater, Shradha, et al.
Publicado: (2015)

Fic and non-Fic AMPylases: protein AMPylation in metazoans
por: Chatterjee, Bhaskar K., et al.
Publicado: (2021)

The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation
por: Frese, Matthias, et al.
Publicado: (2023)

A Pronucleotide Probe for Live‐Cell Imaging of Protein AMPylation
por: Kielkowski, Pavel, et al.
Publicado: (2020)

AMPylation Is Critical for Rab1 Localization to Vacuoles Containing Legionella pneumophila
por: Hardiman, Camille A., et al.
Publicado: (2014)

Chaperone AMPylation modulates aggregation and toxicity of neurodegenerative disease-associated polypeptides
por: Truttmann, Matthias C., et al.
Publicado: (2018)

Fic Proteins Inhibit the Activity of Topoisomerase IV by AMPylation in Diverse Bacteria
por: Lu, Can-Hua, et al.
Publicado: (2020)

Fido, a Novel AMPylation Domain Common to Fic, Doc, and AvrB
por: Kinch, Lisa N., et al.
Publicado: (2009)

Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
por: Du, Jiqing, et al.
Publicado: (2021)

Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation
por: Höpfner, Dorothea, et al.
Publicado: (2020)

Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation
por: Höpfner, Dorothea, et al.
Publicado: (2021)

AMPylation profiling during neuronal differentiation reveals extensive variation on lysosomal proteins
por: Becker, Tobias, et al.
Publicado: (2021)

Fic-mediated AMPylation tempers the unfolded protein response during physiological stress
por: Casey, Amanda K., et al.
Publicado: (2022)

Structural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidD
por: Chen, Yang, et al.
Publicado: (2013)

MS-Based in Situ Proteomics Reveals AMPylation of Host Proteins during Bacterial Infection
por: Rauh, Theresa, et al.
Publicado: (2020)

Correction: Structural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidD
por: Chen, Yang, et al.
Publicado: (2013)

Investigation of the Detailed AMPylated Reaction Mechanism for the Huntingtin Yeast-Interacting Protein E Enzyme HYPE
por: Liu, Meili, et al.
Publicado: (2021)

Structural basis for selective AMPylation of Rac-subfamily GTPases by Bartonella effector protein 1 (Bep1)
por: Dietz, Nikolaus, et al.
Publicado: (2021)

BiP chaperones ER entry
por: LeBrasseur, Nicole
Publicado: (2005)

A convolutional neural network based tool for predicting protein AMPylation sites from binary profile representation
por: Azim, Sayed Mehedi, et al.
Publicado: (2022)

Unstructured regions in IRE1α specify BiP-mediated destabilisation of the luminal domain dimer and repression of the UPR
por: Amin-Wetzel, Niko, et al.
Publicado: (2019)

A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response
por: Amin-Wetzel, Niko, et al.
Publicado: (2017)

The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3
por: Höpfner, Dorothea, et al.
Publicado: (2023)

Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker
por: Preissler, Steffen, et al.
Publicado: (2015)

Generation of human ER chaperone BiP in yeast Saccharomyces cerevisiae
por: Čiplys, Evaldas, et al.
Publicado: (2014)

The Lumenal Domain of Sec63p Stimulates the ATPase Activity of BiP and Mediates BiP Recruitment to the Translocon in Saccharomyces cerevisiae
por: Corsi, Ann K., et al.
Publicado: (1997)

UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor
por: Kopp, Megan C, et al.
Publicado: (2019)

Cannot write session to /tmp/vufind_sessions/sess_29m1jod4erq9df6moo7lgb377s