Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions.
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This study is a large mammalian Hippo-pathway interaction screen; the GOA LRCH3-DOCK7 record is therefore screen-level association evidence.
"We identified 749 protein interactions, including 599 previously unrecognized interactions, and demonstrated that several interactions with serine and threonine phosphatases were phosphorylation-dependent."
A proteome-scale map of the human interactome network.
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This systematic human binary-interactome map provides screen-level context for the GOA LRCH3-DOCK8 isoform association.
"Here, we describe a systematic map of ?14,000 high-quality human binary protein-protein interactions."
The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics.
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LRCH3 links MYO6 and DOCK7 through distinct regions: its LRR region associates with DOCK7, whereas residues 383-648 bind MYO6.
"These experiments showed both MYO6 and DOCK7 can bind to LRCH3; DOCK7 binds to its leucine‐rich repeats and MYO6 to a region between amino acids 383–648 (Fig 5C)."
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Mammalian two-hybrid experiments support a direct LRCH3-MYO6 interaction and map the LRCH3-binding requirement to both MYO6 cargo-binding motifs.
"Indeed, our M2H assay confirmed that LRCH3 interacts directly with MYO6; the binding site again mapped to amino acids 363–648 and required both the WWY and RRL motif in the MYO6 CBD, corroborating our earlier SILAC experiments (Figs 1E and 5D)."
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The LRCH3 calponin-homology region is sufficient in the knock-sideways assay to recruit and oligomerize SEPT7 away from its actin-associated distribution.
"Co‐expression of MitoGBD with GFP alone, full‐length GFP‐LRCH3 or GFP‐tagged domain fragments of LRCH3 in RPE cells caused all to relocalise to the mitochondria; however, only relocalisation of full‐length LRCH3 or a fragment containing its calponin homology domain triggered the concomitant recruitment, and oligomerisation, of SEPT7, from its steady state localisation along actin filaments to mitochondria (Figs 6A and EV5C)."
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Coexpression of LRCH3 with the DOCK7 DHR2 region strongly increased septin ring formation, supporting a cellular role in septin cytoskeleton remodeling.
"Strikingly however, the co‐expression of LRCH3 and the DOCK7 DHR2 domain, which contains the LRCH3 and MYO6 binding sites as well as the RAC1/CDC42 GEF activity of DOCK7, caused a very dramatic increase in the number of cells (~80%) containing septin ring structures (Fig 6D)."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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BioPlex 3.0 comprises cell-line-specific AP-MS interaction networks, making its LRCH3-DOCK7 record context-dependent screen evidence.
"Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks."
OpenCell: Endogenous tagging for the cartography of human cellular organization.
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OpenCell combines endogenous tagging, live-cell imaging, and mass spectrometry; its LRCH3 associations provide localization-aware screen evidence.
"We combined genome engineering, confocal live-cell imaging, mass spectrometry, and data science to systematically map the localization and interactions of human proteins."
Multimodal cell maps as a foundation for structural and functional genomics.
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The 2025 U2OS multimodal cell map jointly measures biophysical interactions and imaging for thousands of proteins; LRCH3 edges remain screen-level evidence.
"Here we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins in U2OS osteosarcoma cells."
LRCH proteins: a novel family of cytoskeletal regulators.
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Expressed human LRCH3 accumulates at the cleavage furrow from anaphase in HeLa cells, providing direct human localization evidence in a mitotic context.
"Similarly, we found that hLRCH3 accumulates at the cleavage furrow from anaphase onset (Figure S6C), albeit without significant cortical accumulation being observed at previous stages of mitosis."
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Four human LRCH paralogs share the LRR-plus-CH architecture, but the paper's loss-of-function mechanism was established for the single Drosophila LRCH gene.
"In human, only four highly-related proteins (hLRCH1-4) simultaneously harbor these two motifs."