ArticleThe Journal of biological chemistry2026
The amyloidogenic C-terminal region of TMEM106B modulates lipid membrane biophysical properties: Functional and pathological insights.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The lysosomal transmembrane protein 106B (TMEM106B) forms amyloid filaments in the human brain in an age-dependent manner, observed both in neurologically healthy individuals and in patients with neurodegenerative diseases also containing tau, α-synuclein, or TDP-43 inclusions. Despite its pathological and physiological relevance, the biochemical mechanisms governing TMEM106B structural stability and its functional interactions with membranes remain largely unknown. Here, we examined the luminal C-terminal fragment of TMEM106B (called TST, residues 120-254), corresponding to the amyloid fibril core identified by cryo-electron microscopy, to elucidate its functional membrane-binding properties. Using static solid-state
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