Full Text Journal Articles by
Author Katrin Rittinger

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Advanced rules of relays.

Sonja Lorenz, Katrin Rittinger,

Nat Chem Biol (Nature chemical biology)
[2020, 16(11):1158-1159]

Cited: 0 times

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RNA binding regulates TRIM25-mediated RIG-I ubiquitylation

Kevin Haubrich, Sandra Augsten, Bernd Simon, Pawel Masiewicz, Kathryn Perez, Mathilde Lethier, Katrin Rittinger, Frank Gabel, Stephen Cusack, Janosch Hennig,

ABSTRACT TRIM25 is a ubiquitin E3 ligase active in innate immunity and cell fate decisions. Mounting evidence suggests that TRIM25’s E3 ligase activity is regulated by RNAs. However, while mutations affecting RNA-binding have been described, the precise RNA binding site has not been identified nor which domains are involved. Here, ... Read more >>

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The parkin-coregulated gene product PACRG promotes TNF signaling by stabilizing LUBAC.

Jens Meschede, Maria Šadić, Nikolas Furthmann, Tim Miedema, Dominik A Sehr, A Kathrin Müller-Rischart, Verian Bader, Lena A Berlemann, Anna Pilsl, Anita Schlierf, Katalin Barkovits, Barbara Kachholz, Katrin Rittinger, Fumiyo Ikeda, Katrin Marcus, Liliana Schaefer, Jörg Tatzelt, Konstanze F Winklhofer,

The Parkin-coregulated gene (PACRG), which encodes a protein of unknown function, shares a bidirectional promoter with Parkin (PRKN), which encodes an E3 ubiquitin ligase. Because PRKN is important in mitochondrial quality control and protection against stress, we tested whether PACRG also affected these pathways in various cultured human cell lines ... Read more >>

Sci Signal (Science signaling)
[2020, 13(617):]

Cited: 1 time

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Characterisation of class VI TRIM RING domains: linking RING activity to C-terminal domain identity.

Rebecca V Stevens, Diego Esposito, Katrin Rittinger,

TRIM E3 ubiquitin ligases regulate multiple cellular processes, and their dysfunction is linked to disease. They are characterised by a conserved N-terminal tripartite motif comprising a RING, B-box domains, and a coiled-coil region, with C-terminal domains often mediating substrate recruitment. TRIM proteins are grouped into 11 classes based on C-terminal ... Read more >>

Life Sci Alliance (Life science alliance)
[2019, 2(3):]

Cited: 2 times

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Fragment-Based Covalent Ligand Screening Enables Rapid Discovery of Inhibitors for the RBR E3 Ubiquitin Ligase HOIP.

Henrik Johansson, Yi-Chun Isabella Tsai, Ken Fantom, Chun-Wa Chung, Sandra Kümper, Luigi Martino, Daniel A Thomas, H Christian Eberl, Marcel Muelbaier, David House, Katrin Rittinger,

Modification of proteins with polyubiquitin chains is a key regulatory mechanism to control cellular behavior and alterations in the ubiquitin system are linked to many diseases. Linear (M1-linked) polyubiquitin chains play pivotal roles in several cellular signaling pathways mediating immune and inflammatory responses and apoptotic cell death. These chains are ... Read more >>

J Am Chem Soc (Journal of the American Chemical Society)
[2019, 141(6):2703-2712]

Cited: 8 times

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Structure-function analyses of the bacterial zinc metalloprotease effector protein GtgA uncover key residues required for deactivating NF-κB.

Elliott Jennings, Diego Esposito, Katrin Rittinger, Teresa L M Thurston,

The closely related type III secretion system zinc metalloprotease effector proteins GtgA, GogA, and PipA are translocated into host cells during Salmonella infection. They then cleave nuclear factor κ-light-chain-enhancer of activated B cells (NF-κB) transcription factor subunits, dampening activation of the NF-κB signaling pathway and thereby suppressing host immune responses. ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2018, 293(39):15316-15329]

Cited: 5 times

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RBR ligase-mediated ubiquitin transfer: a tale with many twists and turns.

Helen Walden, Katrin Rittinger,

RBR ligases are an enigmatic class of E3 ubiquitin ligases that combine properties of RING and HECT-type E3s and undergo multilevel regulation through autoinhibition, post-translational modifications, multimerization and interaction with binding partners. Here, we summarize recent progress in RBR structures and function, which has uncovered commonalities in the mechanisms by ... Read more >>

Nat. Struct. Mol. Biol. (Nature structural & molecular biology)
[2018, 25(6):440-445]

Cited: 15 times

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Structural basis for the glycosyltransferase activity of the Salmonella effector SseK3.

Diego Esposito, Regina A Günster, Luigi Martino, Kamel El Omari, Armin Wagner, Teresa L M Thurston, Katrin Rittinger,

The Salmonella-secreted effector SseK3 translocates into host cells, targeting innate immune responses, including NF-κB activation. SseK3 is a glycosyltransferase that transfers an N-acetylglucosamine (GlcNAc) moiety onto the guanidino group of a target arginine, modulating host cell function. However, a lack of structural information has precluded elucidation of the molecular mechanisms ... Read more >>

J. Biol. Chem. (The Journal of biological chemistry)
[2018, 293(14):5064-5078]

Cited: 11 times

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Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.

Katja K Dove, Jennifer L Olszewski, Luigi Martino, David M Duda, Xiaoli S Wu, Darcie J Miller, Katherine H Reiter, Katrin Rittinger, Brenda A Schulman, Rachel E Klevit,

RING-between-RING (RBR) E3s contain RING1 domains that are structurally similar yet mechanistically distinct from canonical RING domains. Both types of E3 bind E2∼ubiquitin (E2∼Ub) via their RINGs but canonical RING E3s promote closed E2∼Ub conformations required for direct Ub transfer from the E2 to substrate, while RBR RING1s promote open ... Read more >>

Structure (Structure (London, England : 1993))
[2017, 25(6):890-900.e5]

Cited: 16 times

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Linear ubiquitin chains: enzymes, mechanisms and biology.

Katrin Rittinger, Fumiyo Ikeda,

Ubiquitination is a versatile post-translational modification that regulates a multitude of cellular processes. Its versatility is based on the ability of ubiquitin to form multiple types of polyubiquitin chains, which are recognized by specific ubiquitin receptors to induce the required cellular response. Linear ubiquitin chains are linked through Met 1 ... Read more >>

Open Biol (Open biology)
[2017, 7(4):]

Cited: 22 times

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Transparency and openness in science.

Jeremy Sanders, Jon Blundy, Anne Donaldson, Steve Brown, Rob Ivison, Miles Padgett, Kevin Padian, Katrin Rittinger, Kerry Rowe, Anthony Stace, Essi Viding, Chris Chambers, Mark Chaplain,

(Royal Society open science)
[2017, 4(1):160979]

Cited: 0 times

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Determination of the pKa of the N-terminal amino group of ubiquitin by NMR.

Alain Oregioni, Benjamin Stieglitz, Geoffrey Kelly, Katrin Rittinger, Tom Frenkiel,

Ubiquitination regulates nearly every aspect of cellular life. It is catalysed by a cascade of three enzymes and results in the attachment of the C-terminal carboxylate of ubiquitin to a lysine side chain in the protein substrate. Chain extension occurs via addition of subsequent ubiquitin molecules to either one of ... Read more >>

Sci Rep (Scientific reports)
[2017, 7:43748]

Cited: 5 times

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SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes.

Sebastian Kupka, Diego De Miguel, Peter Draber, Luigi Martino, Silvia Surinova, Katrin Rittinger, Henning Walczak,

Recruitment of the deubiquitinase CYLD to signaling complexes is mediated by its interaction with HOIP, the catalytically active component of the linear ubiquitin chain assembly complex (LUBAC). Here, we identify SPATA2 as a constitutive direct binding partner of HOIP that bridges the interaction between CYLD and HOIP. SPATA2 recruitment to ... Read more >>

Cell Rep (Cell reports)
[2016, 16(9):2271-2280]

Cited: 44 times

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Structural determinants of TRIM protein function.

Diego Esposito, Marios G Koliopoulos, Katrin Rittinger,

Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of Really Interesting New Gene (RING) E3 ubiquitin ligases and contribute to the regulation of numerous cellular activities, including innate immune responses. The conserved TRIM harbours a RING domain that imparts E3 ligase activity to TRIM family proteins, whilst a ... Read more >>

Biochem. Soc. Trans. (Biochemical Society transactions)
[2017, 45(1):183-191]

Cited: 22 times

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In Vitro Analysis of Tem1 GTPase Activity and Regulation by the Bfa1/Bub2 GAP.

Marco Geymonat, Adonis Spanos, Katrin Rittinger,

Tem1 is a small GTPase that controls the mitotic progression of Saccharomyces cerevisiae through the Mitotic Exit Network. Tem1 activity is tightly controlled in mitosis by Bub2 and Bfa1 and is also regulated by the spindle orientation checkpoint that monitors the correct alignment of the mitotic spindle with the mother-daughter ... Read more >>

Methods Mol. Biol. (Methods in molecular biology (Clifton, N.J.))
[2017, 1505:71-80]

Cited: 0 times

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Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms.

Katja K Dove, Benjamin Stieglitz, Emily D Duncan, Katrin Rittinger, Rachel E Klevit,

RING-in-between-RING (RBR) ubiquitin (Ub) ligases are a distinct class of E3s, defined by a RING1 domain that binds E2 Ub-conjugating enzyme and a RING2 domain that contains an active site cysteine similar to HECT-type E3s. Proposed to function as RING/HECT hybrids, details regarding the Ub transfer mechanism used by RBRs ... Read more >>

EMBO Rep. (EMBO reports)
[2016, 17(8):1221-1235]

Cited: 27 times

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LUBAC-Recruited CYLD and A20 Regulate Gene Activation and Cell Death by Exerting Opposing Effects on Linear Ubiquitin in Signaling Complexes.

Peter Draber, Sebastian Kupka, Matthias Reichert, Helena Draberova, Elodie Lafont, Diego de Miguel, Lisanne Spilgies, Silvia Surinova, Lucia Taraborrelli, Torsten Hartwig, Eva Rieser, Luigi Martino, Katrin Rittinger, Henning Walczak,

Ubiquitination and deubiquitination are crucial for assembly and disassembly of signaling complexes. LUBAC-generated linear (M1) ubiquitin is important for signaling via various immune receptors. We show here that the deubiquitinases CYLD and A20, but not OTULIN, are recruited to the TNFR1- and NOD2-associated signaling complexes (TNF-RSC and NOD2-SC), at which ... Read more >>

Cell Rep (Cell reports)
[2015, 13(10):2258-2272]

Cited: 83 times

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pUBLically unzipping Parkin: how phosphorylation exposes a ligase bit by bit.

Katja K Dove, Rachel E Klevit, Katrin Rittinger,

EMBO J. (The EMBO journal)
[2015, 34(20):2486-2488]

Cited: 3 times

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Editorial overview: Multi-protein assemblies in signaling.

Deborah Fass, Katrin Rittinger,

Curr. Opin. Struct. Biol. (Current opinion in structural biology)
[2014, 29:vi-viii]

Cited: 0 times

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Sedimentation equilibrium studies.

Ian A Taylor, Katrin Rittinger, John F Eccleston,

The reversible formation of protein-protein interactions plays a crucial role in many biological processes. In order to carry out a thorough quantitative characterization of these interactions it is essential to establish the oligomerization state of the individual components first. The sedimentation equilibrium method is ideally suited to perform these studies ... Read more >>

Methods Mol. Biol. (Methods in molecular biology (Clifton, N.J.))
[2015, 1278:205-222]

Cited: 0 times

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Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the linker region between the NOD2 CARDs and NACHT domain.

Rhiannon Parkhouse, Joseph P Boyle, Sophie Mayle, Kovilen Sawmynaden, Katrin Rittinger, Tom P Monie,

NOD2 activation by muramyl dipeptide causes a proinflammatory immune response in which the adaptor protein CARD9 works synergistically with NOD2 to drive p38 and c-Jun N-terminal kinase (JNK) signalling. To date the nature of the interaction between NOD2 and CARD9 remains undetermined. Here we show that this interaction is not ... Read more >>

FEBS Lett. (FEBS letters)
[2014, 588(17):2830-2836]

Cited: 12 times

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Structural analysis of SHARPIN, a subunit of a large multi-protein E3 ubiquitin ligase, reveals a novel dimerization function for the pleckstrin homology superfold.

Benjamin Stieglitz, Lesley F Haire, Ivan Dikic, Katrin Rittinger,

SHARPIN (SHANK-associated RH domain interacting protein) is part of a large multi-protein E3 ubiquitin ligase complex called LUBAC (linear ubiquitin chain assembly complex), which catalyzes the formation of linear ubiquitin chains and regulates immune and apoptopic signaling pathways. The C-terminal half of SHARPIN contains ubiquitin-like domain and Npl4-zinc finger domains ... Read more >>

J. Biol. Chem. (The Journal of biological chemistry)
[2012, 287(25):20823-20829]

Cited: 12 times

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LUBAC synthesizes linear ubiquitin chains via a thioester intermediate.

Benjamin Stieglitz, Aylin C Morris-Davies, Marios G Koliopoulos, Evangelos Christodoulou, Katrin Rittinger,

The linear ubiquitin chain assembly complex (LUBAC) is a RING E3 ligase that regulates immune and inflammatory signalling pathways. Unlike classical RING E3 ligases, LUBAC determines the type of ubiquitin chain being formed, an activity normally associated with the E2 enzyme. We show that the RING-in-between-RING (RBR)-containing region of HOIP--the ... Read more >>

EMBO Rep (EMBO reports)
[2012, 13(9):840-846]

Cited: 113 times

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Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization.

Benjamin Stieglitz, Katrin Rittinger, Lesley F Haire,

An N-terminal fragment of human SHARPIN was recombinantly expressed in Escherichia coli, purified and crystallized. Crystals suitable for X-ray diffraction were obtained by a one-step optimization of seed dilution and protein concentration using a two-dimensional grid screen. The crystals belonged to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters ... Read more >>

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (Acta crystallographica. Section F, Structural biology and crystallization communications)
[2012, 68(Pt 7):816-819]

Cited: 0 times

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The tandem CARDs of NOD2: intramolecular interactions and recognition of RIP2.

Veronica Fridh, Katrin Rittinger,

Caspase recruitment domains (CARDs) are homotypic protein interaction modules that link the stimulus-dependent assembly of large signaling platforms such as inflammasomes to the activation of downstream effectors that often include caspases and kinases and thereby play an important role in the regulation of inflammatory and apoptotic signaling pathways. NOD2 belongs ... Read more >>

PLoS One (PloS one)
[2012, 7(3):e34375]

Cited: 19 times

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