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Updated: Jun 21, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Generating models for isoform-specific PKM-KIBRA interactions with BIFC, stabilization and AlphaFold 3.
Edna Amoah1, Tyler W Dunn1, Larissa Ferguson1
1Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, H3A 2B4, Canada.
Aplysia Kidney/Brain protein (KIBRA) interactions with protein kinase M (PKM) variants were studied. Some KIBRA variants bind PKM but do not stabilize it, suggesting inhibition is key for memory maintenance.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Protein kinase M (PKM) is crucial for long-term memory.
- Aplysia Kidney/Brain protein (KIBRA) stabilizes atypical PKM Apl III.
- KIBRA variants affect PKM stabilization and neuronal plasticity.
Purpose of the Study:
- Investigate biomolecular fluorescence complementation (BIFC) between KIBRA variants and PKM Apl III.
- Examine KIBRA variants with altered binding sites and mutations.
- Understand the discrepancy between KIBRA-PKM binding and PKM stabilization.
Main Methods:
- Biomolecular fluorescence complementation (BIFC) in Aplysia neurons.
- Analysis of KIBRA variants with modified binding sites.
- Utilizing AlphaFold 3 for protein-protein interaction modeling.
Main Results:
- Some KIBRA variants exhibit BIFC with PKM Apl III without stabilizing it.
- Altered KIBRA binding sites disrupt PKM Apl III stabilization and plasticity.
- Protein interaction modeling provided insights into BIFC-stabilization discrepancies.
Conclusions:
- KIBRA-PKM interaction does not always equate to stabilization.
- Stable inhibition of PKM by KIBRA may be essential for memory maintenance.
- Further research into KIBRA's inhibitory role in PKM regulation is warranted.
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