Home > Publications Database > Physiological shedding and C-terminal proteolytic processing of TMEM106B > print

001     274095
005     20250119000330.0
024 7 _ |a 10.1016/j.celrep.2024.115107
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037 _ _ |a DZNE-2025-00051
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100 1 _ |a Held, Sebastian
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245 _ _ |a Physiological shedding and C-terminal proteolytic processing of TMEM106B
260 _ _ |a [New York, NY]
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520 _ _ |a Genetic variants in TMEM106B, coding for a transmembrane protein of unknown function, have been identified as critical genetic modulators in various neurodegenerative diseases with a strong effect in patients with frontotemporal degeneration. The luminal domain of TMEM106B can form amyloid-like fibrils upon proteolysis. Whether this luminal domain is generated under physiological conditions and which protease(s) are involved in shedding remain unclear. We developed a commercially available antibody against the luminal domain of TMEM106B, allowing a detailed survey of the proteolytic processing under physiological conditions in cellular models and TMEM106B-related mouse models. Moreover, fibrillary TMEM106B was detected in human autopsy material. We find that the luminal domain is generated by multiple lysosomal cysteine-type proteases. Cysteine-type proteases perform additional C-terminal trimming, for which experimental evidence has been lacking. The presented results allow an in-depth perception of the processing of TMEM106B, a prerequisite to understanding factors leading to fibril formation.
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700 1 _ |a Erck, Christian
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700 1 _ |a Kemppainen, Susanna
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700 1 _ |a Bleibaum, Florian
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700 1 _ |a Giridhar, Neha Jadhav
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700 1 _ |a Feederle, Regina
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700 1 _ |a Krenner, Claudia
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700 1 _ |a Juopperi, Sini-Pauliina
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700 1 _ |a Calliari, Anna
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700 1 _ |a Mentrup, Torben
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700 1 _ |a Schröder, Bernd
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700 1 _ |a Dickson, Dennis W.
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700 1 _ |a Rauramaa, Tuomas
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700 1 _ |a Petrucelli, Leonard
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700 1 _ |a Prudencio, Mercedes
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700 1 _ |a Hiltunen, Mikko
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700 1 _ |a Lüningschrör, Patrick
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700 1 _ |a Capell, Anja
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700 1 _ |a Damme, Markus
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773 _ _ |a 10.1016/j.celrep.2024.115107
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