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Autoimmunity-associated DIORA1 binds the MRCK family of serine/threonine kinases and controls cell motility

ABSTRACT: Autoimmunity-associated DIORA1 binds the MRCK family of serine/threonine kinases and controls cell motility

PROVIDER: PRJNA1274935 | ENA |

REPOSITORIES: ENA

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Autoimmunity-associated DIORA1 binds the MRCK family of serine/threonine kinases and controls cell motility

Project description:Genetic association links DIORA1 to numerous autoimmune rheumatic diseases, including systemic lupus erythematosus, Sjögren's disease, rheumatoid arthritis, polymyositis and systemic sclerosis. However, its cellular function has remained unknown. Here, we identify the MRCK family of serine/threonine kinases - key regulators of actomyosin contractility and cell motility - as direct interactors of DIORA1. Through interaction mapping, we show that DIORA1 binds three distinct modules of MRCK kinases, including the conserved kinase inhibitory motif (KIM), C1-PH and CNH domains. DIORA1 knockdown in human cells altered cellular phosphorylation patterns and reduced phosphorylation of known MRCK targets. RNA-sequencing and proteomic analyses revealed upregulation of epithelial-mesenchymal transition genes and proteins, and functional analyses confirmed increased cell invasion, following knockdown of DIORA1. Together, these findings identify the autoimmunity-associated DIORA1 protein as a previously uncharacterized interactor of MRCK kinases and a regulator of cell motility.

2025-09-08 | GSE299540 | GEO

Autoimmunity-associated DIORA1 binds the MRCK family of serine/threonine kinases and controls cell motility

Project description:Genetic association links DIORA1 to numerous autoimmune rheumatic diseases including systemic lupus erythematous, Sjögren's disease, myositis, scleroderma and rheumatoid arthritis, but its cellular function remains unknown. Here, we identify the MRCK kinase family as DIORA1 interactors. MRCK kinases regulate the activity of actin-myosin networks, including cell adhesion, motility and invasion. Mapping the interaction between DIORA1 and MRCKs, we found that DIORA1 binds three distinct modules of MRCK kinases, including the conserved autoinhibitory kinase inhibitory motif (KIM) and C1-PH-CNH domains. Knockdown of DIORA1 altered cellular phosphorylation patterns, including reduced phosphorylation of known MRCK targets. Functional analyses revealed enhanced cellular migration and invasion following knockdown of DIORA1, and RNA-sequencing and proteomic analyses confirmed upregulation of epithelial mesenchymal transition genes and proteins. In summary, our findings identify autoimmunity-associated DIORA1 as a previously uncharacterized interactor of MRCK kinases and a modulator of cell motility.

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