LFA-1 cluster formation in T-cells depends on L-plastin phosphorylation regulated by P90RSK and PP2A
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 describ...
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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
15 January 2021
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| In: |
Cellular and molecular life sciences
Year: 2021, Jahrgang: 78, Heft: 7, Pages: 3543-3564 |
| ISSN: | 1420-9071 |
| DOI: | 10.1007/s00018-020-03744-z |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/s00018-020-03744-z
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| Verfasserangaben: | Guido H. Wabnitz, Sibylle Honus, Jüri Habicht, Christian Orlik, Henning Kirchgessner, Yvonne Samstag |
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| 245 | 1 | 0 | |a LFA-1 cluster formation in T-cells depends on L-plastin phosphorylation regulated by P90RSK and PP2A |c Guido H. Wabnitz, Sibylle Honus, Jüri Habicht, Christian Orlik, Henning Kirchgessner, Yvonne Samstag |
| 246 | 3 | 3 | |a LFA-1 cluster formation in T-cells depends on L-plastin phosphorylation regulated by P90 RSK and PP2A |
| 264 | 1 | |c 15 January 2021 | |
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| 520 | |a 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. | ||
| 650 | 4 | |a Actins | |
| 650 | 4 | |a Cells, Cultured | |
| 650 | 4 | |a Humans | |
| 650 | 4 | |a Immune synapse | |
| 650 | 4 | |a LFA-1 cluster | |
| 650 | 4 | |a LPL | |
| 650 | 4 | |a Lymphocyte Function-Associated Antigen-1 | |
| 650 | 4 | |a Microfilament Proteins | |
| 650 | 4 | |a p90RSK | |
| 650 | 4 | |a Phosphorylation | |
| 650 | 4 | |a PP2A | |
| 650 | 4 | |a Protein Phosphatase 2 | |
| 650 | 4 | |a Ribosomal Protein S6 Kinases, 90-kDa | |
| 650 | 4 | |a T-cells | |
| 650 | 4 | |a T-Lymphocytes | |
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| 700 | 1 | |a Samstag, Yvonne |e VerfasserIn |0 (DE-588)1056828285 |0 (DE-627)794131794 |0 (DE-576)170331059 |4 aut | |
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