The non-canonical CDK2 activator SPY1 uses separable mechanisms to activate phosphorylated and unphosphorylated CDK2
Liam P Fawcett, Nicholas M Levinson · 2026
Read The non-canonical CDK2 activator SPY1 uses separable mechanisms to activate phosphorylated and unphosphorylated CDK2 by Liam P Fawcett, Nicholas M Levinson (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13570426.txt.
Description
Liam P. Fawcett and Nicholas M. Levinson dissect, in a 2026 study, how an unusual activator protein called SPY1 switches on CDK2, a key engine of cell division, without the phosphate tag that the normal activator requires. Fluorescence experiments tracked shape changes in the engine as each activator bound, in both tagged and untagged states.
SPY1 activated both forms as strongly as the standard activator and shifted the engine's shape just as far. A mutant version long thought to mimic the phosphate tag failed on untagged CDK2 yet worked fully on tagged CDK2, proving the activator uses two separate tricks. The distinction matters for designing drugs that block this division engine in cancer.
Catalog record
| CREATOR | Liam P Fawcett, Nicholas M Levinson |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 34 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |