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Article

Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells.

Human molecular genetics - 15 Sept 2017

Dettmer Ulf, Ramalingam Nagendran, von Saucken Victoria E, Kim Tae-Eun, Newman Andrew J, Terry-Kantor Elizabeth, Nuber Silke, Ericsson Maria, Fanning Saranna, Bartels Tim, Lindquist Susan, Levy Oren A, Selkoe Dennis

Abstract excerpt

α-Synuclein (αS) forms round cytoplasmic inclusions in Parkinson's disease (PD) and dementia with Lewy bodies (DLB). Evidence suggests a physiological function of αS in vesicle trafficking and release. In contrast to earlier tenets, recent work indicates that αS normally exists in cells in a dynamic equilibrium between monomers and tetramers/multimers. We engineered αS mutants incapable of multimerization,...

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Identifiers

PMID: 28911198
DOI: 10.1093/hmg/ddx227
PMCID: PMC5884392

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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