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Ly49Q, an atypical Ly49 receptor expressed in non-NK cells, binds MHC-I in <jats:italic>cis<\/jats:italic> and mediates chemotaxis of neutrophils and type I interferon production by plasmacytoid dendritic cells. We identified a lipid-binding motif in the juxtamembrane region of Ly49Q and found that Ly49Q organized functional membrane domains comprising sphingolipids via sulfatide binding. Ly49Q recruited actin-remodeling molecules to an immunoreceptor tyrosine-based inhibitory motif, which enabled the sphingolipid-enriched membrane domain to mediate complicated actin remodeling at the lamellipodia and phagosome membranes during phagocytosis. Thus, Ly49Q facilitates integrative regulation of proteins and lipid species to construct a cell type-specific membrane platform. Other Ly49 members possess lipid binding motifs; therefore, membrane platform organization may be a primary role of some NK cell receptors.<\/jats:p>","DOI":"10.3389\/fimmu.2024.1401294","type":"journal-article","created":{"date-parts":[[2024,4,24]],"date-time":"2024-04-24T04:51:51Z","timestamp":1713934311000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":4,"title":["Collaboration between a cis-interacting natural killer cell receptor and membrane sphingolipid is critical for the phagocyte 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