Flying under the radar: TMEM106B(120-254) fibrils break out in diverse neurodegenerative disorders

Katie E Copley; James Shorter

doi:10.1016/j.cell.2022.03.032

Flying under the radar: TMEM106B(120-254) fibrils break out in diverse neurodegenerative disorders

Cell. 2022 Apr 14;185(8):1290-1292. doi: 10.1016/j.cell.2022.03.032.

Authors

Katie E Copley¹, James Shorter²

Affiliations

¹ Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA; Neuroscience Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
² Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA; Neuroscience Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: [email protected].

Abstract

Neurodegenerative diseases commonly exhibit aggregation of specific proteins that define each disease. Chang et al. (2022) establish that a C-terminal fragment of TMEM106B, a frontotemporal-lobar-degeneration risk factor, unexpectedly forms amyloid fibrils with similar structures in diverse neurodegenerative disorders. These unanticipated TMEM106B(120-254) fibrils may herald etiological shifts for several neurodegenerative diseases.

Publication types

Comment

MeSH terms

Frontotemporal Dementia*
Frontotemporal Lobar Degeneration* / metabolism
Humans
Membrane Proteins / genetics
Membrane Proteins / metabolism
Nerve Tissue Proteins / metabolism

Substances

Membrane Proteins
Nerve Tissue Proteins
TMEM106B protein, human

Abstract

Publication types

MeSH terms

Substances

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