Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions.
Architecture of the human interactome defines protein communities and disease networks.
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BioPlex 2.0 is an affinity-purification mass-spectrometry interaction resource, so its LRCH2-DOCK8 record is screen-level co-association evidence.
"Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes), which uses robust affinity purification-mass spectrometry methodology to elucidate protein interaction networks and co-complexes nucleated by more than 25% of protein-coding genes from the human genome, and constitutes, to our knowledge, the largest such network so far."
Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals spatially organized RAC1 signalling from integrin adhesions.
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The study systematically mapped substrate specificity, interactomes, and localization across human RhoGEF and RhoGAP regulators.
"Through a family-wide characterization of substrate specificities, interactomes and localization, we reveal at the systems level how RhoGEFs and RhoGAPs contextualize and spatiotemporally control Rho signalling."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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BioPlex 3.0 provides cell-line-specific AP-MS interaction networks; its LRCH2- DOCK8 record is context-dependent screen evidence rather than a mechanism.
"Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks."
Novel genes bearing mutations in rare cases of early-onset ataxia with cerebellar hypoplasia.
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A hemizygous LRCH2 p.Lys258Glu variant in one family was proposed as a candidate cause of congenital ataxia, cerebellar hypoplasia, and demyelinating polyneuropathy.
"In Family I, the unique missense mutation (p.Lys258Glu) was found in the LRCH2 gene inherited in an X-linked manner. p.Lys258Glu occurs in the evolutionarily invariant site of the leucine-rich repeat domain of LRCH2."
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Expression analysis placed LRCH2 in Schwann-lineage cells and above its paralogs in the developing cerebellar cortex.
"The LRCH2 gene for Family I patients (in which congenital cerebellar hypoplasia was associated with demyelinating polyneuropathy) is expressed in Schwann and precursor Schwann cells and predominantly over its paralogous genes in the developing cerebellar cortex."
LRCH proteins: a novel family of cytoskeletal regulators.
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The sole Drosophila LRCH protein stabilizes the mitotic cortex, a family-level result that cannot be assigned specifically to human LRCH2.
"Taking advantage of the existence of a single LRCH gene in flies, dLRCH, we explored its function in cultured cells, and show that dLRCH act to stabilize the cell cortex during cell division."
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The study establishes the shared LRR and CH architecture of four human LRCH paralogs, including LRCH2.
"In human, only four highly-related proteins (hLRCH1-4) simultaneously harbor these two motifs."
LRCH1 interferes with DOCK8-Cdc42-induced T cell migration and ameliorates experimental autoimmune encephalomyelitis.
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LRCH1 binds the catalytic DHR-2 domain of DOCK8 and restricts its guanyl-nucleotide exchange activity, providing a paralog-specific boundary for LRCH2 interpretation.
"Next, we identified that LRCH1 competes with Cdc42 for binding to the catalytic DHR-2 domain of DOCK8 and restricts the GEF activity of DOCK8."