DRAK2 regulates myosin light chain phosphorylation in T cells.

Autor:	Wilander BA; Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.; Graduate School of Biomedical Sciences, St. Jude Children's Research Hospital, Memphis, TN 38105, USA., Harris TL; Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA., Mandarano AH; Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA., Guy CS; Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA., Prater MS; The Center for Advanced Genome Engineering, St. Jude Children's Research Hospital; Memphis TN 38105, USA.; Department of Cell and Molecular Biology; St. Jude Children's Research Hospital; Memphis TN 38105, USA., Pruett-Miller SM; The Center for Advanced Genome Engineering, St. Jude Children's Research Hospital; Memphis TN 38105, USA.; Department of Cell and Molecular Biology; St. Jude Children's Research Hospital; Memphis TN 38105, USA., Ogden SK; Department of Cell and Molecular Biology; St. Jude Children's Research Hospital; Memphis TN 38105, USA., McGargill MA; Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Jazyk:	angličtina
Zdroj:	Journal of cell science [J Cell Sci] 2024 Oct 18. Date of Electronic Publication: 2024 Oct 18.
DOI:	10.1242/jcs.261813
Abstrakt:	Death-associated protein kinase-related apoptosis-inducing kinase-2 (DRAK2 or STK17B) is a serine/threonine kinase expressed in T cells. Drak2-deficient (Drak2-/-) mice respond effectively to tumors and pathogens while displaying resistance to T cell-mediated autoimmune disease. However, the molecular mechanisms by which DRAK2 impacts T cell function remain unclear. Gaining further insight into the function of DRAK2 in T cells will shed light on differentially regulated pathways in autoreactive and pathogen-specific T cells, which is critical for improving autoimmune therapies. Here, we demonstrate that DRAK2 contributes to activation of myosin light chain (MLC) in both murine and human T cells. In the absence of Drak2, the amount of polymerized actin was decreased, suggesting that DRAK2 modulates actomyosin dynamics. We further show that myosin-dependent T cell functions, such as migration, T cell receptor microcluster accumulation, and conjugation to antigen presenting cells are decreased in the absence of Drak2. These findings reveal that DRAK2 plays an important role in regulating MLC activation within T cells. (© 2024. Published by The Company of Biologists Ltd.)
Databáze:	MEDLINE
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