The Alexander Disease Protein GFAP Drives Mitochondrial Fission

• DOI: 10.1101/2024.02.20.581117
• Publication Date: 2024-02-27T18:13:23Z
• Authors: Ding Xiong; Linghai Kong; Ye Sing Tan; Fang Yuan; Zijun Sun; Xueyan Li; Emily Abella; Albee Messing; Su-Chun Zhang

Abstract Mitochondrial plasticity, coordinated by fission and fusion, is crucial to ensure cellular functions. mediated the GTPase Drp1 at constriction site, which proposed be driven actin-myosin contractile force. However, mechanism that propels remains unclear, potential involvement of additional mechanisms in this process an open question. Here, using structured illumination microscopy electron microscopy, we show type-III intermediate filament glial fibrillary acidic protein (GFAP) closely surrounds mitochondria sites associates with accumulated molecules. Remarkably, loss GFAP results hyperfused under physiological condition even Ca 2+ -induced mitochondrial fission. Additionally, mutations GFAP, cause Alexander disease, result elevated recruitment leading significantly increased fissions. Taking together, these findings suggest a novel division filaments.