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TitleLilrB3 is a putative cell surface receptor of APOE4.
Journal, issue, pagesCell Res, Vol. 33, Issue 2, Page 116-130, Year 2023
Publish dateJan 2, 2023
AuthorsJiayao Zhou / Yumeng Wang / Gaoxingyu Huang / Min Yang / Yumin Zhu / Chen Jin / Dan Jing / Kai Ji / Yigong Shi /
PubMed AbstractThe three isoforms of apolipoprotein E (APOE2, APOE3, and APOE4) only differ in two amino acid positions but exert quite different immunomodulatory effects. The underlying mechanism of such APOE ...The three isoforms of apolipoprotein E (APOE2, APOE3, and APOE4) only differ in two amino acid positions but exert quite different immunomodulatory effects. The underlying mechanism of such APOE isoform dependence remains enigmatic. Here we demonstrate that APOE4, but not APOE2, specifically interacts with the leukocyte immunoglobulin-like receptor B3 (LilrB3). Two discrete immunoglobin-like domains of the LilrB3 extracellular domain (ECD) recognize a positively charged surface patch on the N-terminal domain (NTD) of APOE4. The atomic structure reveals how two APOE4 molecules specifically engage two LilrB3 molecules, bringing their intracellular signaling motifs into close proximity through formation of a hetero-tetrameric complex. Consistent with our biochemical and structural analyses, APOE4, but not APOE2, activates human microglia cells (HMC3) into a pro-inflammatory state in a LilrB3-dependent manner. Together, our study identifies LilrB3 as a putative immune cell surface receptor for APOE4, but not APOE2, and may have implications for understanding the biological functions as well as disease relevance of the APOE isoforms.
External linksCell Res / PubMed:36588123 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

34216

8grx

EMDB-34216, PDB-8grx:
APOE4 receptor in complex with APOE4 NTD
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Receptor complex

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