{
  "id": 10719118,
  "title": "Dynamic protein phosphorylation shapes mitochondrial catalysis, import, and architecture",
  "url": "https://urgent.news/2026/09/29/dynamic-protein-phosphorylation-shapes-mitochondrial-catalysis-import",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-29T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.28.755151v1?rss=1"
  },
  "original_language": "en",
  "account": "Phosphorylation, a common modification of proteins within mitochondria, holds significant sway over the functionality of these organelles. To uncover the breadth of its impact, scientists analyzed the phosphoproteome of AML12 cells after altering the activity of 10 key mitochondrial phosphatases. This analysis led to a deeper understanding of how phosphorylation influences mitochondrial processes tied to catalysis, import, and morphology.\n\nUpon investigation, researchers discovered that phosphorylation of adenylate kinase 2 lessens its ability to bind nucleotides and catalyze reactions. Furthermore, higher phosphorylation levels near the mitochondrial targeting sequence of branched chain ketoacid dehydrogenase kinase disrupts its import into the mitochondria and its processing, leading to an upsurge in the breakdown of branched chain amino acids.\n\nPerhaps the most striking finding was the extensive phosphorylation observed on proteins associated with mitochondrial cristae architecture, including several members of the MICOS complex and ATP synthase, following the silencing of the phosphatase PGAM5. These results suggest a strong connection between reversible phosphorylation and resident phosphatases, highlighting their role in controlling a wide array of mitochondrial functions.",
  "summary": "Phosphorylation is a pervasive mitochondrial protein post-translational modification, yet the extent of its influence over mitochondrial functions remains unclear. To identify dynamic mitochondrial phosphoisoforms, we profiled the phosphoproteome of AML12 cells following individual genetic perturbations of 10 resident mitochondrial phosphatases. Guided by these results, we investigated the…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}