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TitleResidues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 34, Page e2315006121, Year 2024
Publish dateAug 20, 2024
AuthorsKatherine M Dewison / Benjamin Rowlinson / Jonathan M Machin / Joel A Crossley / Dev Thacker / Martin Wilkinson / Sabine M Ulamec / G Nasir Khan / Neil A Ranson / Patricija van Oosten-Hawle / David J Brockwell / Sheena E Radford /
PubMed AbstractAmyloid formation by α-synuclein (αSyn) occurs in Parkinson's disease, multiple system atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn amyloid fibril formation ...Amyloid formation by α-synuclein (αSyn) occurs in Parkinson's disease, multiple system atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn amyloid fibril formation will not only provide mechanistic insight but may also reveal targets to prevent and treat disease. Previous investigations have identified several regions of αSyn to be important in the regulation of amyloid formation, including the non-amyloid-β component (NAC), P1 region (residues 36 to 42), and residues in the C-terminal domain. Recent studies have also indicated the importance of the N-terminal region of αSyn for both its physiological and pathological roles. Here, the role of residues 2 to 7 in the N-terminal region of αSyn is investigated in terms of their ability to regulate amyloid fibril formation in vitro and in vivo. Deletion of these residues (αSynΔN7) slows the rate of fibril formation in vitro and reduces the capacity of the protein to be recruited by wild-type (αSynWT) fibril seeds, despite cryo-EM showing a fibril structure consistent with those of full-length αSyn. Strikingly, fibril formation of αSynΔN7 is not induced by liposomes, despite the protein binding to liposomes with similar affinity to αSynWT. A model also showed that αSynΔN7::YFP forms few puncta and lacks motility and lifespan defects typified by expression of αSynWT::YFP. Together, the results demonstrate the involvement of residues 2 to 7 of αSyn in amyloid formation, revealing a target for the design of amyloid inhibitors that may leave the functional role of the protein in membrane binding unperturbed.
External linksProc Natl Acad Sci U S A / PubMed:39133842 / PubMed Central
MethodsEM (helical sym.)
Resolution2.5 Å
Structure data

18570

8qpz

EMDB-18570, PDB-8qpz:
CryoEM structure of recombinant DeltaN7 alpha-synuclein in PBS
Method: EM (helical sym.) / Resolution: 2.5 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / synuclein / Parkinson's disease / neurodegeneration / amyloid / helical / fibril

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