bims-hypusi Biomed News
on Hypusine and eIF5A
Issue of 2026–08–16
two papers selected by
Sebastian J. Hofer, Max Delbrück Center



  1. STAR Protoc. 2026 Aug 10. pii: S2666-1667(26)00427-2. [Epub ahead of print]7(3): 104774
      Hypusination is a unique posttranslational modification in which deoxyhypusine synthase (DHPS) transfers an aminobutyl moiety from spermidine to specific lysine residues, followed by deoxyhypusine hydroxylase (DOHH)-mediated hydroxylation. Here, we present a protocol that enables proteome-wide identification of candidate hypusinated proteins. We describe steps for the synthesis of a clickable alkynyl-spermidine probe, DHPS-dependent metabolic labeling in cells, click chemistry-mediated biotinylation, streptavidin-based enrichment, and subsequent mass spectrometry analysis of probe-labeled proteins. We also describe the procedures for data processing and statistical analysis. For complete details on the use and execution of this protocol, please refer to Zhang et al.1.
    Keywords:  Cell Biology; Mass Spectrometry; Molecular/Chemical Probes
    DOI:  https://doi.org/10.1016/j.xpro.2026.104774
  2. Trends Neurosci. 2026 Aug 11. pii: S0166-2236(26)00142-6. [Epub ahead of print]
      Protein synthesis is a highly energy-dependent process that consists of initiation, elongation, termination, and ribosome recycling. Historically, initiation has been viewed as the major site of translation regulation. However, growing recognition of elongation as a regulatory node has highlighted the importance of eukaryotic elongation factor (eEF)1A-dependent decoding, eEF2-catalyzed ribosome translocation, conditional elongation factors, ribosome speed, and tRNA dynamics. In neurons, these mechanisms are especially important because protein synthesis must be regulated across highly polarized cellular compartments. In this review, we summarize evidence from diverse model systems showing that tightly regulated translation elongation supports cellular function and viability, whereas disrupted elongation contributes to dysfunction and disease throughout the nervous system.
    Keywords:  FMRP; GCN2; eEF1; eEF2; eIF5A; tRNA
    DOI:  https://doi.org/10.1016/j.tins.2026.07.004