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| Hauptseite > Publikationsdatenbank > Characterizing the membrane recruitment domain of BDCPs and its role in gray platelet syndrome |
| Hauptseite > Publikationsdatenbank > Characterizing the membrane recruitment domain of BDCPs and its role in gray platelet syndrome |
| Journal Article | FZJ-2026-04049 |
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2026
Rockefeller Univ. Press
New York, NY
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Please use a persistent id in citations: doi:10.1083/jcb.202510098
Abstract: BEACH domain–containing proteins (BDCPs) represent a family of large membrane–associated transmembrane cargoadaptors. In the current study, we determined the cryo-EM structure of the full-length typical BDCP NBEAL2, revealing anN-terminal arch-like structure with C-terminal globular domains attached to its convex surface. Using structure-guideddeletion mutants and protein chimeras as well as native alternatively spliced isoforms and disease-related point mutants, weshow that the N-terminal α-solenoid/concanavalin A–like domain assembly of the typical BDCPs NBEAL1, NBEAL2, LYST, ALFY,LRBA, and NBEA functions as a modular membrane recruitment domain. We report that gray platelet syndrome–associatedsingle aa mutations L388P or E643V within the membrane recruitment domain of NBEAL2 disrupt its membrane targeting instably transfected cells, highlighting a potential structure-function mechanism by which failed membrance recruitement cause gray platelet syndrome or other BDCPs-related diseases
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