Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 1, Pages -Publisher
MDPI
DOI: 10.3390/ijms22010126
Keywords
Cdc37; co-chaperone; Lck; tyrosine kinase; TCR signaling; heat shock protein 90 (Hsp90)
Funding
- German Research Foundation (DFG) [CRC 854, B19]
- medical health campus of the Otto-von-Guericke University (GC-I3)
- State of Saxony-Anhalt (project INITIATE, research network autonomy in old age, EFRE/ESF funding programs)
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Experimental data does not support the idea that Cdc37 regulates the activity/stability of Lck, as evidenced by unaffected Lck stability and TCR signaling in T cells with augmented or suppressed Cdc37 expression.
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.
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