| |  Online-Ressource |
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| Verfasst von: | Wabnitz, Guido H. [VerfasserIn]  |
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| | Honus, Sibylle [VerfasserIn] |
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| | Habicht, Jüri [VerfasserIn] |
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| | Orlik, Christian [VerfasserIn] |
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| | Kirchgessner, Henning [VerfasserIn] |
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| | Samstag, Yvonne [VerfasserIn] |
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| Titel: | LFA-1 cluster formation in T-cells depends on L-plastin phosphorylation regulated by P90RSK and PP2A |
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| Verf.angabe: | Guido H. Wabnitz, Sibylle Honus, Jüri Habicht, Christian Orlik, Henning Kirchgessner, Yvonne Samstag |
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| E-Jahr: | 2021 |
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| Jahr: | 15 January 2021 |
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| Umfang: | 22 S. |
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| Fussnoten: | Im Titel ist 'RSK' hochgestellt ; Gesehen am 27.07.2021 |
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| Titel Quelle: | Enthalten in: Cellular and molecular life sciences |
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| Ort Quelle: | Cham (ZG) : Springer International Publishing AG, 1997 |
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| Jahr Quelle: | 2021 |
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| Band/Heft Quelle: | 78(2021), 7, Seite 3543-3564 |
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| ISSN Quelle: | 1420-9071 |
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| Abstract: | The integrin LFA-1 is crucial for T-cell/ APC interactions and sensitive recognition of antigens. Precise nanoscale organization and valency regulation of LFA-1 are mandatory for an appropriate function of the immune system. While the inside-out signals regulating the LFA-1 affinity are well described, the molecular mechanisms controlling LFA-1 avidity are still not fully understood. Here, we show that activation of the actin-bundling protein L-plastin (LPL) through phosphorylation at serine-5 enables the formation of clusters containing LFA-1 in high-affinity conformation. Phosphorylation of LPL is induced by an nPKC-MEK-p90RSK pathway and counter-regulated by the serine-threonine phosphatase PP2A. Interestingly, recruitment of LFA-1 into the T-cell/APC contact zone is not affected by LPL phosphorylation. Instead, for this process, activation of the actin-remodeling protein cofilin through dephosphorylation is essential. Together, this study reveals a dichotomic spatial regulation of LFA-1 clustering and microscale movement in T-cells by two different actin-binding proteins, LPL and cofilin. |
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| DOI: | doi:10.1007/s00018-020-03744-z |
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| URL: | Volltext: https://doi.org/10.1007/s00018-020-03744-z |
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| | DOI: https://doi.org/10.1007/s00018-020-03744-z |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | Actins |
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| | Cells, Cultured |
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| | Humans |
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| | Immune synapse |
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| | LFA-1 cluster |
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| | LPL |
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| | Lymphocyte Function-Associated Antigen-1 |
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| | Microfilament Proteins |
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| | p90RSK |
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| | Phosphorylation |
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| | PP2A |
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| | Protein Phosphatase 2 |
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| | Ribosomal Protein S6 Kinases, 90-kDa |
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| | T-cells |
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| | T-Lymphocytes |
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| K10plus-PPN: | 1764620534 |
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| Verknüpfungen: | → Zeitschrift |
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| Lokale URL UB: |  Zum Volltext |
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LFA-1 cluster formation in T-cells depends on L-plastin phosphorylation regulated by P90RSK and PP2A / Wabnitz, Guido H. [VerfasserIn]; 15 January 2021 (Online-Ressource)
