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DTX2 and DTX3L modify ADP-ribosylated H2B and PARP1 peptides with ubiquitin. Left: PARP1 Glu-ADPr, and H2B Ser-ADPr peptides reacted with wild-type DTX2(RING-DTC) and DTX3L(RING-DTC) and (right) their DTC domain mutants. All reactions contain E1, UbcH5b, Ub, MgCl2, ATP. ADP-ribosylated peptides were detected with antibodies for ubiquitin or poly/mono-ADPr, or Neutravidin800. Auto-modified DTX is indicated as His-DTX-Ubn on the merged image. ADPr-Ub on peptide substrates are indicated as pep-ADPr-Ub on the merged images.

DTX2 and DTX3L modify ADP-ribosylated H2B and PARP1 peptides with ubiquitin. Left: PARP1 Glu-ADPr, and H2B Ser-ADPr peptides reacted with wild-type DTX2(RING-DTC) and DTX3L(RING-DTC) and (right) their DTC domain mutants. All reactions contain E1, UbcH5b, Ub, MgCl2, ATP. ADP-ribosylated peptides were detected with antibodies for ubiquitin or poly/mono-ADPr, or Neutravidin800. Auto-modified DTX is indicated as His-DTX-Ubn on the merged image. ADPr-Ub on peptide substrates are indicated as pep-ADPr-Ub on the merged images.

Recent studies have shown that ADP-ribosyl modifications can be further modified by #ubiquitin (ADPr-Ub). @chatrin-c.bsky.social &co biochemically characterize the amino acid specificity for ADPr-Ub production and its recognition by E3 ubiquitin ligases @plosbiology.org 🧪 plos.io/4t43UJK

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DTX2 and DTX3L modify ADP-ribosylated H2B and PARP1 peptides with ubiquitin. Left: PARP1 Glu-ADPr, and H2B Ser-ADPr peptides reacted with wild-type DTX2(RING-DTC) and DTX3L(RING-DTC) and (right) their DTC domain mutants. All reactions contain E1, UbcH5b, Ub, MgCl2, ATP. ADP-ribosylated peptides were detected with antibodies for ubiquitin or poly/mono-ADPr, or Neutravidin800. Auto-modified DTX is indicated as His-DTX-Ubn on the merged image. ADPr-Ub on peptide substrates are indicated as pep-ADPr-Ub on the merged images.

DTX2 and DTX3L modify ADP-ribosylated H2B and PARP1 peptides with ubiquitin. Left: PARP1 Glu-ADPr, and H2B Ser-ADPr peptides reacted with wild-type DTX2(RING-DTC) and DTX3L(RING-DTC) and (right) their DTC domain mutants. All reactions contain E1, UbcH5b, Ub, MgCl2, ATP. ADP-ribosylated peptides were detected with antibodies for ubiquitin or poly/mono-ADPr, or Neutravidin800. Auto-modified DTX is indicated as His-DTX-Ubn on the merged image. ADPr-Ub on peptide substrates are indicated as pep-ADPr-Ub on the merged images.

Recent studies have shown that ADP-ribosyl modifications can be further modified by #ubiquitin (ADPr-Ub). @chatrin-c.bsky.social &co biochemically characterize the amino acid specificity for ADPr-Ub production and its recognition by E3 ubiquitin ligases @plosbiology.org 🧪 plos.io/4t43UJK

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DTX2 and DTX3L modify ADP-ribosylated H2B and PARP1 peptides with ubiquitin. Left: PARP1 Glu-ADPr, and H2B Ser-ADPr peptides reacted with wild-type DTX2(RING-DTC) and DTX3L(RING-DTC) and (right) their DTC domain mutants. All reactions contain E1, UbcH5b, Ub, MgCl2, ATP. ADP-ribosylated peptides were detected with antibodies for ubiquitin or poly/mono-ADPr, or Neutravidin800. Auto-modified DTX is indicated as His-DTX-Ubn on the merged image. ADPr-Ub on peptide substrates are indicated as pep-ADPr-Ub on the merged images.

DTX2 and DTX3L modify ADP-ribosylated H2B and PARP1 peptides with ubiquitin. Left: PARP1 Glu-ADPr, and H2B Ser-ADPr peptides reacted with wild-type DTX2(RING-DTC) and DTX3L(RING-DTC) and (right) their DTC domain mutants. All reactions contain E1, UbcH5b, Ub, MgCl2, ATP. ADP-ribosylated peptides were detected with antibodies for ubiquitin or poly/mono-ADPr, or Neutravidin800. Auto-modified DTX is indicated as His-DTX-Ubn on the merged image. ADPr-Ub on peptide substrates are indicated as pep-ADPr-Ub on the merged images.

Recent studies have shown that ADP-ribosyl modifications can be further modified by #ubiquitin (ADPr-Ub). @chatrin-c.bsky.social &co biochemically characterize the amino acid specificity for ADPr-Ub production and its recognition by E3 ubiquitin ligases @plosbiology.org 🧪 plos.io/4t43UJK

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Registration now open! 2026 #EMBO #Ubiquitin Workshop set in stunning Monopoli, Puglia 🇮🇹
Cutting edge science, great speakers, short talk opportunities, travel awards
Limited spaces. Dont miss out - register early!
Registration & more info: meetings.embo.org/event/26-ubi...

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Such an exciting opportunity!
Be among the first to join the brand-new @leokiss.bsky.social lab @unidue.bsky.social 🧬✨
#CellularBiochemistry #Ubiquitin #Proteostasis #ProteinDegradation

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Excited to decode the intricate language of ubiquitin chains and unravel their role in protein degradation? 🧬🔬
👉 APPLY NOW to join the lab of Dr. Leo Kiss @leokiss.bsky.social @imprs-lm.bsky.social.
#CellularBiochemistry #Ubiquitin #Proteostasis #ProteinDegradation

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🔍 Want to uncover how proteolytic enzymes in the ubiquitin system work—and exploit those insights for novel therapeutic approaches? Apply to the Gersch Lab @maltegersch.bsky.social at @imprs-lm.bsky.social.
#proteolysis #ubiquitin #biochemistry #proteinchemistry

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#Pseudogenes aren’t always silent 🧬 RPS27AP5, once considered non-functional, produces a #ubiquitin variant (UbP5) and #ribosomal #protein variant (S27aP5) that alters #mRNA association, adding evidence for ribosome diversity 👏
https://ow.ly/hsNn50Yh11e

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Our very own Cansu Dilege on: How are E2 enzymes regulated?
-> Yes, kinases are involved (several)!
#MBP2026 #ecr #ubiquitin #UniHamburg

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The second day of #Biochemistry2026 gets on the way with an exciting talk by Satpal Virdee (@e3chembio.bsky.social). "Next-generation Activity-Based Probes for Ubiquitin and Ubiquitin-like E3 Ligases".

www.nature.com/articles/nch...
#ChemBio #Biochemistry #ChemSky #ubiquitin #TPD #degradation

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🔬 In our latest issue, we invite you to discover the Editor's Choice article exploring deubiquitination mechanism involved in resistance to tyrosine kinase inhibitors in chronic myeloid leukemia, accompanied by an insightful Commentary.
Discover, here ➡️ buff.ly/jdODi5z
#CML #ubiquitin #TKI

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Light-shedding article review by Liu & Yan:

‘Protein engineering fixes a major crop trade-off’

tinyurl.com/uu2fu45v

#WIS

#PlantandEnvironmentalScience

#ColdStress

#ProteinDesign

#CropYield

#Phosphorous

#Maize

#InorganicPhosphate

#HighYieldVariety

#JasmonicAcid

#Ubiquitin

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The accessory adapters FAF1, FAF2, and UBXN7 accelerate proteasomal degradation by increasing prior p97-mediated substrate unfolding A group of accessory adapters positions the p97 adapter Ufd1 to boost substrate unfolding and subsequent proteasomal degradation.

VCP/p97’s accessory adapters (FAF1, FAF2, UBXN7) boost unfolding and subsequent proteasomal degradation. #ubiquitin. Our paper is out now:
Science Advances www.science.org/doi/10.1126/...

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Registration is now open for the EMBO Workshop "#Ubiquitin and ubiquitin-like proteins in health and disease" in #Monopoli, Italy, 28 Sep–2 Oct 2026.

Registration deadline: 31 May
Abstract submission deadline: 15 Jun

https://meetings.embo.org/event/26-ubiquitin
#EMBOubiquitin #EMBOevents 🧪

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🚀 We're excited to announce that our new issue is now online!
5️⃣ Featuring: 2 articles honouring #WomenInScience, a state-of-the-art Review, a Viewpoint, an Editor's Choice with a Commentary, several original articles.
Discover ➡️https://buff.ly/XIqf1Na
#lipidation #Cas9 #ubiquitin #structuralbiology

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Registration now open for #EMBOUbiquitin.
meetings.embo.org/event/26-ubi...

Childcare, accessibility, and travel grants available.

#ubiquitin #TargetedProteinDegradation #Proteostasis #UBL

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A #ubiquitin variant hiding in a #pseudogene? UbKEKS (from UBBP4) looks like canonical ubiquitin — but NMR reveals structural & dynamic shifts that prevent K48-linked proteasomal degradation and reshape its substrate profile 🧫
https://ow.ly/ugo950Yh0MI

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Check our YouTube Channel to watch the First IMPReSsion of the Đikić Group and learn about Ivan Đikić’s motivation and inspiration to do science!( @idikic.bsky.social , @goetheuni.bsky.social ) youtu.be/medBsmcfv1w?si=03zTBPCtRvPuc6Ub
#structuralbiology #biochemistry #ubiquitin #autophagy

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🥁 New insights alert! Today, we take you into the fascinating world of RING-type E3 ubiquitin ligases through this article from our #Highlights2025 collection.
📕 RING dimerisation drives higher-order organisation of SINA/SIAH E3 ubiquitin ligases
➡️ buff.ly/rIErxm1
#ubiquitin #E3ligase #RING #SIAH1

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Protein Termini 2026 – International Society for Protein Termini (ISPT)

8 days left to register | 28 invited speakers | Keynotes from F. Ulrich Hartl, Roland Beckmann and Michael Rapé | #chaperones #degradation #ubiquitin #cryoEM #acetylation #lipidation #ribosomes #proteins
proteintermini.org/meeting/

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Check out our new work on #ubiquitin and #neurological disorders @natrevmcb.nature.com

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Model describing the effect of CUL5 on the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing. CUL5-KO could reduce the ubiquitination of PTBP1, thereby increasing the alternative splicing of RUBCN pre-mRNA, leading to an increase in Rubicon-S which inhibits autophagy, and thus enhances the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing (cartoon created in BioRender).

Model describing the effect of CUL5 on the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing. CUL5-KO could reduce the ubiquitination of PTBP1, thereby increasing the alternative splicing of RUBCN pre-mRNA, leading to an increase in Rubicon-S which inhibits autophagy, and thus enhances the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing (cartoon created in BioRender).

CD8+ T cells can target & eliminate malignant #tumor cells, but tumors can develop resistance mechanisms to escape them. This study shows that loss of the E3 #ubiquitin ligase CUL5 enhances CD8+ #Tcell #cytotoxicity & anti PD-1 efficacy by inhibiting #autophagy @plosbiology.org 🧪 plos.io/3Mv1EuR

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Model describing the effect of CUL5 on the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing. CUL5-KO could reduce the ubiquitination of PTBP1, thereby increasing the alternative splicing of RUBCN pre-mRNA, leading to an increase in Rubicon-S which inhibits autophagy, and thus enhances the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing (cartoon created in BioRender).

Model describing the effect of CUL5 on the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing. CUL5-KO could reduce the ubiquitination of PTBP1, thereby increasing the alternative splicing of RUBCN pre-mRNA, leading to an increase in Rubicon-S which inhibits autophagy, and thus enhances the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing (cartoon created in BioRender).

CD8+ T cells can target & eliminate malignant #tumor cells, but tumors can develop resistance mechanisms to escape them. This study shows that loss of the E3 #ubiquitin ligase CUL5 enhances CD8+ #Tcell #cytotoxicity & anti PD-1 efficacy by inhibiting #autophagy @plosbiology.org 🧪 plos.io/3Mv1EuR

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Model describing the effect of CUL5 on the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing. CUL5-KO could reduce the ubiquitination of PTBP1, thereby increasing the alternative splicing of RUBCN pre-mRNA, leading to an increase in Rubicon-S which inhibits autophagy, and thus enhances the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing (cartoon created in BioRender).

Model describing the effect of CUL5 on the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing. CUL5-KO could reduce the ubiquitination of PTBP1, thereby increasing the alternative splicing of RUBCN pre-mRNA, leading to an increase in Rubicon-S which inhibits autophagy, and thus enhances the sensitivity of bladder cancer cells to CD8+ T cell-mediated killing (cartoon created in BioRender).

CD8+ T cells can target & eliminate malignant #tumor cells, but tumors can develop resistance mechanisms to escape them. This study shows that loss of the E3 #ubiquitin ligase CUL5 enhances CD8+ #Tcell #cytotoxicity & anti PD-1 efficacy by inhibiting #autophagy @plosbiology.org 🧪 plos.io/3Mv1EuR

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Plants use cell-surface and intracellular receptors that collaborate to detect pathogens🦠. We discovered that a key #ubiquitin recognition event recruits both receptor types into an unexpected dual receptor complex that boost the translation of defence proteins and establishes robust #PlantImmunity👇🏾

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Targeting UCHL3 attenuates pathological markers in neuronal models of Huntington’s disease Ishtayeh et al. identify the cancer-associated deubiquitinating enzyme UCHL3 as a potential therapeutic target in Huntington’s disease. Genetic and pharmac

Our new paper in @brain1878.bsky.social. 🎉 We identify a new function of #ubiquitin enzyme in #Huntington’s disease models. Great collaboration with the Ellerby Lab.
academic.oup.com/brain/articl...

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Very happy to share our recent preprint describing #Golgi protein quality control #PQC in mammalian cells. #proteasome #ubiquitin #ChemBio Fantastic work by @joaodiamantino.bsky.social and team! #proudPI @unidue-zmb.bsky.social @imprs-lm.bsky.social

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We’re excited to share our latest work on bioRxiv:

"Salmonella exploits USP32 to coordinate Rab14 and Rab11 recycling pathways for intracellular survival" by Sapmaz et al

www.biorxiv.org/content/10.6...

#Salmonella #CellBiology #HostPathogen #Ubiquitin #bioRxiv

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A CK2-FBXW11 kinase-E3 ubiquitin ligase cascade is a metabolic sensor regulating Tryptophan 2,3-dioxygenase stability Small molecules toggling the ubiquitin-proteasome system (UPS) are powerful regulators of protein degradation. Yet, mechanistic knowledge of how endogenous ligands gate UPS decisions remains rudimentary. Here, we define control of UPS access to Tryptophan-2,3-dioxygenase (TDO2), which converts the essential amino acid tryptophan (Trp) to N-formylkynurenine. When Trp concentrations are limiting, TDO2 is degraded to avert tryptophanemia. Using CRISPRi screening and biochemistry, we identify a CK2-FBXW11 kinase-E3 ligase cascade that generates and recognizes tandem TDO2 phosphodegrons when not protected by Trp. Trp binding to an exosite safeguards TDO2 from phosphorylation-dependent ubiquitylation. Effects of Trp analogs on CK2-FBXW11-dependent ubiquitylation indicated that the indole, amino, and carboxylate groups are necessary for substrate shielding. Cryo-EM reveals how these moieties order a region proximal to the phosphodegrons; without Trp, this segment is flexible, enabling phosphorylation-coupled ubiquitylation. Overall, our data uncovered an endogenous small molecule allosterically stabilizing its own metabolizing enzyme through protection from a phosphorylation-ubiquitylation cascade. ### Competing Interest Statement B.A.S. is a member of the scientific advisory boards of Proxygen and Lyterian. The other authors declare no competing interests. Max Planck Society, https://ror.org/01hhn8329 European Union, ERC AdvG, UPSmeetMet, 101098161 to BAS Boehringer Ingelheim Fonds, https://ror.org/00dkye506

New year, new preprint! 🎊

We are excited to share our recent work on #E3 ligase regulation in #metabolism!

www.biorxiv.org/content/10.6...

#ubiquitin #targetedproteindegradation #chemicalbiology

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If you are interested in #ubiquitin related topics (Who isn’t???) & looking for a friendly and collegial meeting where you can talk to anyone & everyone, this is your meeting!

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