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Related Experiment Video

Updated: Feb 22, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Cryptic sequence features within the disordered protein p27Kip1 regulate cell cycle signaling.

Rahul K Das¹, Yongqi Huang², Aaron H Phillips²

¹Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130;

Proceedings of the National Academy of Sciences of the United States of America

|May 4, 2016

Summary

This summary is machine-generated.

Intrinsically disordered regions (IDRs) control cell signaling through modifications. Altering charge patterns in p27 IDR sequences reveals how these regions modulate motif function and phosphorylation efficiency.

Keywords:

disordered regions motif p27

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Last Updated: Feb 22, 2026

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Analysis of Cell Cycle Position in Mammalian Cells

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Published on: January 21, 2012

Area of Science:

Protein intrinsically disordered regions (IDRs)
Posttranslational modifications
Cell signaling pathways

Background:

Peptide motifs in protein IDRs are key sites for posttranslational modifications controlling cell signaling.
The p27(Kip1) protein's C-terminal IDR, a polyampholytic sequence, regulates cell cycle entry via Thr-187 phosphorylation.
Charge patterning in polyampholytic sequences influences IDR conformational properties.

Purpose of the Study:

Investigate how intrinsically disordered region (IDR) sequences modulate the functionality of embedded motifs.
Determine the impact of altered charge patterning on the p27 IDR's structure and function.
Uncover cryptic sequence features within the p27 IDR that influence Thr-187 phosphorylation efficiency.

Main Methods:

Designed sequence variants of the p27 IDR to modify charge patterning.
Employed computer simulations and biophysical measurements to assess IDR dimensions.
Conducted functional studies to evaluate the impact on Thr-187 phosphorylation.

Main Results:

Confirmed that charge patterning significantly affects the global dimensions of IDRs.
Identified a positive correlation between T187 phosphorylation efficiency and the weighted net charge per residue of an auxiliary motif.
Demonstrated that excessive positive charges in the auxiliary motif can inhibit T187 phosphorylation by promoting long-range intra-IDR interactions.

Conclusions:

Cryptic sequence features within the wild-type p27 IDR negatively regulate T187 phosphorylation signaling.
The linear arrangement of charged residues in IDRs critically influences motif function.
Developed a generalizable strategy for studying sequence context effects on motif functionality in other IDRs.