The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37

Kowallik, Sarah; Kritikos, Andreas; Kästle, Matthias; Thurm, Christoph; Schraven, Burkhart; Simeoni, Luca

doi:10.3390/ijms22010126

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The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37

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Institute of Molecular and Clinical Immunology, Otto-von-Guericke University, 39120 Magdeburg, Germany

Health Campus Immunology, Infectiology and Inflammation (GC-I³), Medical Faculty, Otto-von Guericke University, 39120 Magdeburg, Germany

Author to whom correspondence should be addressed.

Int. J. Mol. Sci. 2021, 22(1), 126; https://doi.org/10.3390/ijms22010126

Received: 30 November 2020 / Revised: 21 December 2020 / Accepted: 22 December 2020 / Published: 24 December 2020

(This article belongs to the Special Issue The Many Facets of the Regulation of TCR Signaling)

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Abstract

Lymphocyte-specific protein tyrosine kinase (Lck) is a pivotal tyrosine kinase involved in T cell receptor (TCR) signaling. Because of its importance, the activity of Lck is regulated at different levels including phosphorylation of tyrosine residues, protein–protein interactions, and localization. It has been proposed that the co-chaperone Cdc37, which assists the chaperone heat shock protein 90 (Hsp90) in the folding of client proteins, is also involved in the regulation of the activity/stability of Lck. Nevertheless, the available experimental data do not clearly support this conclusion. Thus, we assessed whether or not Cdc37 regulates Lck. We performed experiments in which the expression of Cdc37 was either augmented or suppressed in Jurkat T cells. The results of our experiments indicated that neither the overexpression nor the suppression of Cdc37 affected Lck stability and activity. Moreover, TCR signaling proceeded normally in T cells in which Cdc37 expression was either augmented or suppressed. Finally, we demonstrated that also under stress conditions Cdc37 was dispensable for the regulation of Lck activity/stability. In conclusion, our data do not support the idea that Lck is a Cdc37 client. View Full-Text

Keywords: Cdc37; co-chaperone; Lck; tyrosine kinase; TCR signaling; heat shock protein 90 (Hsp90)

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MDPI and ACS Style

Kowallik, S.; Kritikos, A.; Kästle, M.; Thurm, C.; Schraven, B.; Simeoni, L. The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37. Int. J. Mol. Sci. 2021, 22, 126. https://doi.org/10.3390/ijms22010126

AMA Style

Kowallik S, Kritikos A, Kästle M, Thurm C, Schraven B, Simeoni L. The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37. International Journal of Molecular Sciences. 2021; 22(1):126. https://doi.org/10.3390/ijms22010126

Chicago/Turabian Style

Kowallik, Sarah, Andreas Kritikos, Matthias Kästle, Christoph Thurm, Burkhart Schraven, and Luca Simeoni. 2021. "The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37" International Journal of Molecular Sciences 22, no. 1: 126. https://doi.org/10.3390/ijms22010126

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The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37

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