Cargando…

Identification of PARP-7 substrates reveals a role for MARylation in microtubule control in ovarian cancer cells

PARP-7 (TiPARP) is a mono(ADP-ribosyl) transferase whose protein substrates and biological activities are poorly understood. We observed that PARP7 mRNA levels are lower in ovarian cancer patient samples compared to non-cancerous tissue, but PARP-7 protein nonetheless contributes to several cancer-r...

Descripción completa

Detalles Bibliográficos
Autores principales:	Palavalli Parsons, Lavanya H, Challa, Sridevi, Gibson, Bryan A, Nandu, Tulip, Stokes, MiKayla S, Huang, Dan, Lea, Jayanthi S, Kraus, W Lee
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	eLife Sciences Publications, Ltd 2021
Materias:	Biochemistry and Chemical Biology
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7884071/ https://www.ncbi.nlm.nih.gov/pubmed/33475085 http://dx.doi.org/10.7554/eLife.60481

Ejemplares similares

MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential
por: Challa, Sridevi, et al.
Publicado: (2021)

A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Ovarian Cancer Cells
por: Challa, Sridevi, et al.
Publicado: (2023)

Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets
por: Rodriguez, Kelsie M, et al.
Publicado: (2021)

FRI019 Mono(ADP-Ribosyl)ation Of Ribosomal Proteins During Adipogenesis
por: Tan, Xinrui, et al.
Publicado: (2023)

Development and characterization of new tools for detecting poly(ADP-ribose) in vitro and in vivo
por: Challa, Sridevi, et al.
Publicado: (2022)

OR23-5 Exploring the Role of PARP7 in Adipogenesis
por: Lee Kraus, W, et al.
Publicado: (2022)

PARP10 Multi-Site Auto- and Histone MARylation Visualized by Acid-Urea Gel Electrophoresis
por: García-Saura, Antonio Ginés, et al.
Publicado: (2021)

SAT-030 Role of PARP-1 in Regulating Cytokine-Mediated Pro-Inflammatory Transcriptional Responses in Macrophages
por: Gupte, Rebecca, et al.
Publicado: (2019)

Biochemical reconstitution of branching microtubule nucleation
por: Alfaro-Aco, Raymundo, et al.
Publicado: (2020)

Structural insight into TPX2-stimulated microtubule assembly
por: Zhang, Rui, et al.
Publicado: (2017)

Autoregulatory control of microtubule binding in doublecortin-like kinase 1
por: Agulto, Regina L, et al.
Publicado: (2021)

HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase
por: Rudolph, Johannes, et al.
Publicado: (2021)

The speed of GTP hydrolysis determines GTP cap size and controls microtubule stability
por: Roostalu, Johanna, et al.
Publicado: (2020)

The mitotic spindle protein CKAP2 potently increases formation and stability of microtubules
por: McAlear, Thomas S, et al.
Publicado: (2022)

Multivalency of NDC80 in the outer kinetochore is essential to track shortening microtubules and generate forces
por: Volkov, Vladimir A, et al.
Publicado: (2018)

Tight bending of the Ndc80 complex provides intrinsic regulation of its binding to microtubules
por: Scarborough, Emily Anne, et al.
Publicado: (2019)

Molecular determinants of the Ska-Ndc80 interaction and their influence on microtubule tracking and force-coupling
por: Huis in 't Veld, Pim J, et al.
Publicado: (2019)

Astrin-SKAP complex reconstitution reveals its kinetochore interaction with microtubule-bound Ndc80
por: Kern, David M, et al.
Publicado: (2017)

Antibacterial potency of type VI amidase effector toxins is dependent on substrate topology and cellular context
por: Radkov, Atanas, et al.
Publicado: (2022)

Doublecortin engages the microtubule lattice through a cooperative binding mode involving its C-terminal domain
por: Rafiei, Atefeh, et al.
Publicado: (2022)

FRI011 Exploring The Contribution Of PARP1-mediated Site-specific ADP-Ribosylation Of C/EBPb In Macrophages To Diet-induced Obesity
por: Whitaker, Amy L, et al.
Publicado: (2023)

Origin and evolution of transporter substrate specificity within the NPF family
por: Jørgensen, Morten Egevang, et al.
Publicado: (2017)

UBE2G1 governs the destruction of cereblon neomorphic substrates
por: Lu, Gang, et al.
Publicado: (2018)

Correction: Origin and evolution of transporter substrate specificity within the NPF family
por: Jørgensen, Morten Egevang, et al.
Publicado: (2019)

Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
por: Shin, Donghyuk, et al.
Publicado: (2020)

Protomer alignment modulates specificity of RNA substrate recognition by Ire1
por: Li, Weihan, et al.
Publicado: (2021)

Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme
por: Fedoryshchak, Roman O, et al.
Publicado: (2020)

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamase
por: Chen, John Z, et al.
Publicado: (2020)

Comprehensive substrate specificity profiling of the human Nek kinome reveals unexpected signaling outputs
por: van de Kooij, Bert, et al.
Publicado: (2019)

Conformational and dynamic plasticity in substrate-binding proteins underlies selective transport in ABC importers
por: de Boer, Marijn, et al.
Publicado: (2019)

Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates
por: Cockman, Matthew E, et al.
Publicado: (2019)

Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease
por: Tzeng, Shiou-Ru, et al.
Publicado: (2021)

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

The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)
por: Rale, Michael J, et al.
Publicado: (2022)

Nicotinamide mononucleotide adenylyltransferase uses its NAD(+) substrate-binding site to chaperone phosphorylated Tau
por: Ma, Xiaojuan, et al.
Publicado: (2020)

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation
por: Greene, Eric R, et al.
Publicado: (2019)

The molecular coupling between substrate recognition and ATP turnover in a AAA+ hexameric helicase loader
por: Puri, Neha, et al.
Publicado: (2021)

Molecular mechanism of Afadin substrate recruitment to the receptor phosphatase PTPRK via its pseudophosphatase domain
por: Hay, Iain M, et al.
Publicado: (2022)

A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment
por: Wang, Xinru, et al.
Publicado: (2020)

A single power stroke by ATP binding drives substrate translocation in a heterodimeric ABC transporter
por: Stefan, Erich, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_clum96odgm9nts2tpcbdk5idpn