ArticleImmunoHorizons2026
SHIP-1 adapter functions mediate recruitment of FCRL1 to the BCR and inhibition of ERK.
Article in ImmunoHorizons, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 authors.
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Abstract
FCRL1 is a plasma membrane coreceptor on B cells that has been shown to potentiate B cell receptor (BCR)-driven calcium flux and negatively regulate ERK phosphorylation in a GRB2 and tyrosine-dependent manner. Of the proteins that associate with FCRL1, the recruitment of the inositol phosphatase SHIP-1 is GRB2 dependent, implicating SHIP-1 in FCRL1-mediated ERK regulation. Using immunoprecipitation and Western blotting, it was found that a proline-rich region in the C-terminus of SHIP-1, rather than its N-terminal SH2 domain, mediates recruitment of SHIP-1 to Y281 in FCRL1 in a manner dependent on GRB2. Interestingly, Y281 and GRB2 were also required for FCRL1 colocalization to the BCR. Translational fusions between tyrosine-mutated FCRL1 and the SH2 domain of SHIP-1 were sufficient to drive both colocalization of FCRL1 with the BCR as well as the ERK-inhibitory activity of FCRL1. Our data are consistent with a function for SHIP-1 as an adapter between FCRL1 and the BCR signalosome, and that this adapter function is responsible for BCR/FCRL1 colocalization after BCR stimulation and modulation of ERK signaling.
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