International Society for Protein Termini (ISPT)

International Society for Protein Termini (ISPT)

@ispt-proteinterm.bsky.social

Non-profit society of scientists devoted to understanding the molecular mechanisms and biological role of protein termini in plants, animals, fungi and bacteria. Conference every second year. Website: https://proteintermini.org/

196 followers229 following26 posts

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

Very happy to see this out!! Thank you all! Check out or latest publication www.pnas.org/doi/10.1073/...

pnas.orgA synthetic ERFVII-dependent circuit in yeast sheds light on the regulation of early hypoxic responses of plants | PNASPlants face hypoxic conditions either chronically, as particular tissues are characterized by fluctuating or stable low oxygen levels, or acutely, ...
Oxford Biology@biology.ox.ac.uk

Without oxygen, the first minutes matter 🌱 In low oxygen, eg when flooded, plants need to act quickly to survive. New research led by @mikellavi.bsky.social has revealed a molecular circuit that kicks into gear in minutes - and it can work completely independently 👇

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

A conference about #proteostasis in a palazzo in Palermo; inclusive, affordable, and organised by the marvellous @giglionelab.bsky.social - what’s not to like? Oh, and there is a fantastic lineup of talks plus slots to spare #ProteinTermini2026

See you at Palazzo dei Normanni in Palermo for the 2026 Protein Termini Conference | Co- and post-translational modifications | Proteolytic processing and degradation pathways | Microbes, plants, animals #ProteinTermini2026 #Proteostasis #ProteinModifications #PalazzoDeiNormanni #Palermo2026

International Society for Protein Termini (ISPT) reposted

The countdown to Palermo is on! 🇮🇹 The FEBS Workshop "Protein Termini 2026" is set. • 151 participants from all over the world. • >50% ECRs! • 30+ travel grants. Thx to sponsors: FEBS, IUBMB, CDBC, ARS, and others.. See you at Palazzo dei Normanni! #ProteinTermini #FEBS #Proteostasis

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

How are histones acetylated as they emerge from the ribosome? We show that NAA40 cooperates with the NAC complex to enable co-translational acetylation of H2A/H4, revealing NAC as a coordinator of nascent protein modification. Read more about our collaboration with @kirmizislab.bsky.social #cryoEM

rdcu.beNAA40 and NAC cooperate in co-translational histone acetylation in humansNature Communications - N-terminal histone acetylation by human NAA40 alters epigenetic signaling and affects gene regulation. Here, the authors combine biochemistry and cryo-EM to unravel the...

International Society for Protein Termini (ISPT) reposted

International Society for Protein Termini (ISPT) reposted

My review “Co-translational control of protein stability and quality in plants” is now online at @jxbotany.bsky.social, in which I describe how co-translational processing and ribosome-associated quality control together establish protein stability and fate early in synthesis. tinyurl.com/5dhhz9h6

tinyurl.comCo-translational control of protein stability and quality in plantsAbstract. Proteostasis relies on the coordinated control of protein synthesis, folding, modification and degradation, and an increasingly clear picture is

International Society for Protein Termini (ISPT) reposted

Join us at the @crick.ac.uk for the 2026 meeting of the UK proteostasis community! We especially encourage students and postdocs to attend and share their work. All talks (except the keynotes) will be selected from abstracts.

Proteostasis UK@proteostasisuk.bsky.social

📣 UK Proteostasis Meeting 2026 – Registration Now Open! I’m delighted to share that registration is now open for the UK Proteostasis Meeting 2026, hosted by The Francis Crick Institute on 20–21 July 2026
. Please register here(lnkd.in/ervXMzWN) and through Eventbrite for payment (lnkd.in/eTxqjnQy)

Protein degradation in Turnip - an adapted Arg/N-degron pathway. Preprint from Brian Mooney et al. Emmanuelle Graciet lab. www.biorxiv.org/content/10.6...

biorxiv.orgFunctional divergence of the Arg/N-degron pathway between the crop Brassica rapa and the model plant Arabidopsis thalianaThe ubiquitin-dependent Arg/N-degron pathway relates the stability of a substrate protein to the nature of its N-terminal amino acid residue or its biochemical modifications, with some N-terminal residues being recognized by specific E3 ubiquitin ligases, resulting in the ubiquitylation and degradation of the substrate protein. Work in the model plant Arabidopsis thaliana has shown that the Arg/N-degron pathway is a key regulator of plant responses to hypoxia, which can be either physiological or a stress in the context of waterlogging or submergence. The role of the Arg/N-degron pathway in hypoxia response is mediated via the oxygen-dependent degradation of group VII ETHYLENE RESPONSE FACTOR (ERFVII) transcription factors, which act as the master regulators of the hypoxia response program in plants. Analysis of Arabidopsis mutants for different enzymatic components of the Arg/N-degron pathway has also revealed its roles in the regulation of responses to other abiotic stresses (e.g. salt stress), as well as to pathogens. Although much has been learned from studies in Arabidopsis about the functions of the Arg/N-degron pathway, very little is known about this pathway in crops, including in Brassica crops such as oilseed rape, cabbage or turnip. To determine functional similarities and divergence of the Arg/N-degron pathway between Arabidopsis and Brassica crops, we isolated and characterized the first Arg/N-degron pathway mutants in Brassica rapa (turnip, pak choi), a diploid Brassica crop closely related to oilseed rape. We focused on two enzymatic components, namely the arginine-transferases ( ATE s) and the E3 ubiquitin ligase PROTEOLYSIS6 ( PRT6 ). Our results show both similarities and divergence of function for these Arg/N-degron pathway components in B. rapa compared to Arabidopsis. Specifically, ATE mutants in B. rapa arrest their development at the seedling stage, which contrasts with the mild phenotypic defects of the equivalent Arabidopsis mutants. Double mutant lines for two of the three PRT6 genes in B. rapa indicated a constitutive activation of hypoxia response genes at the transcriptional level, as shown in the single prt6 mutant in Arabidopsis. However, contrary to Arabidopsis, the B. rapa double mutants were more sensitive to waterlogging and hypoxia, and did not show differential response to salt stress or to biotic stress compared to the wild type. The functional divergence identified likely reflects variability in each species in the substrate repertoire and/or in the regulation of pathways or targets downstream of Arg/N-degron pathway substrates. Such differences could be driven by direct selective pressures at N-termini (e.g. gain or loss of a destabilizing N-terminal residue), or by species-specific proteases that may generate destabilizing neo-N-termini after cleavage. These similarities and differences highlight the difficulties in translating research findings from Arabidopsis to crops, even within the same plant family (Brassicaceae) and highlight the need to study pathways in crops. ### Competing Interest Statement The authors have declared no competing interest. Science Foundation Ireland, https://ror.org/0271asj38, 13/IA/1870, 20/FFP-P/8433 Irish Research Council, https://ror.org/051xex213, GOIPG/2017/2

International Society for Protein Termini (ISPT) reposted

Complexity at the ribosomal polypeptide tunnel exit. The major N-terminal acetyltransferase NatA may form different complexes on the ribosome to facilitate protein maturation. By Marius Klein & Klemens Wild in Irmgard Sinning's lab BZH & Nina McTiernan in my lab. www.nature.com/articles/s41...