AI Article Synopsis
- Lck is a Src family kinase essential for T cell development and activation, playing a key role in TCR signaling through phosphorylation of the TCR/CD3 complex.
- The study reveals that free Lck has greater mobility and higher levels of activating phosphorylation compared to coreceptor-bound Lck, indicating different molecular properties of the two forms.
- Free Lck demonstrates increased kinase activity and promotes stronger T cell activation, while the coreceptor-Lck interaction operates independently of TCR activation, suggesting a regulatory mechanism for modulating T cell sensitivity.
Article Abstract
Src family kinase Lck plays critical roles during T cell development and activation, as it phosphorylates the TCR/CD3 complex to initiate TCR signaling. Lck is present either in coreceptor-bound or coreceptor-unbound (free) forms, and we here present evidence that the two pools of Lck have different molecular properties. We discovered that the free Lck fraction exhibited higher mobility than CD8α-bound Lck in OT-I T hybridoma cells. The free Lck pool showed more activating Y394 phosphorylation than the coreceptor-bound Lck pool. Consistent with this, free Lck also had higher kinase activity, and free Lck mediated higher T cell activation as compared to coreceptor-bound Lck. Furthermore, the coreceptor-Lck coupling was independent of TCR activation. These findings give insights into the initiation of TCR signaling, suggesting that changes in coreceptor-Lck coupling constitute a mechanism for regulation of T cell sensitivity.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7355011 | PMC |
| http://dx.doi.org/10.1073/pnas.1913334117 | DOI Listing |
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