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TitleApolipoprotein E secreted by astrocytes forms antiparallel dimers in discoidal lipoproteins.
Journal, issue, pagesNeuron, Vol. 112, Issue 7, Page 1100-11109.e5, Year 2024
Publish dateApr 3, 2024
AuthorsMichael R Strickland / Michael J Rau / Brock Summers / Katherine Basore / John Wulf / Hong Jiang / Yun Chen / Jason D Ulrich / Gwendalyn J Randolph / Rui Zhang / James A J Fitzpatrick / Anil G Cashikar / David M Holtzman /
PubMed AbstractThe Apolipoprotein E gene (APOE) is of great interest due to its role as a risk factor for late-onset Alzheimer's disease. ApoE is secreted by astrocytes in the central nervous system in high-density ...The Apolipoprotein E gene (APOE) is of great interest due to its role as a risk factor for late-onset Alzheimer's disease. ApoE is secreted by astrocytes in the central nervous system in high-density lipoprotein (HDL)-like lipoproteins. Structural models of lipidated ApoE of high resolution could aid in a mechanistic understanding of how ApoE functions in health and disease. Using monoclonal Fab and F(ab') fragments, we characterize the structure of lipidated ApoE on astrocyte-secreted lipoproteins. Our results provide support for the "double-belt" model of ApoE in nascent discoidal HDL-like lipoproteins, where two ApoE proteins wrap around the nanodisc in an antiparallel conformation. We further show that lipidated, recombinant ApoE accurately models astrocyte-secreted ApoE lipoproteins. Cryogenic electron microscopy of recombinant lipidated ApoE further supports ApoE adopting antiparallel dimers in nascent discoidal lipoproteins.
External linksNeuron / PubMed:38266643 / PubMed Central
MethodsEM (single particle)
Resolution7.71 - 8.73 Å
Structure data

EMDB-41830: Lipidated recombinant apolipoprotein E4
Method: EM (single particle) / Resolution: 8.73 Å

EMDB-41831: Gradient-fixed lipidated recombinant apolipoprotein E4
Method: EM (single particle) / Resolution: 7.71 Å

Source
  • Escherichia coli (E. coli)

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