A single base change makes a difference

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A recent study published in Science examines how a specific single nucleotide polymorphism (SNP) influences memory performance, revealing that individuals with a Thymine base at a particular locus outperform those with a Cystine base in short-term memory tasks. This genetic variation affects the KIBRA protein, which plays a crucial role in memory and learning processes. Further research by Ji et al. in 2019 explores the molecular mechanisms of KIBRA, identifying its interaction with Dendrin, a protein involved in synaptic function. The study demonstrates that KIBRA's binding to Dendrin is essential for effective synaptic transmission and long-term potentiation, which are critical for spatial learning and memory. Mutations in the KIBRA gene have been linked to neurological disorders, highlighting its significance in cognitive functions.
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There's a new paper in Science that investigates the effect of a single SNP (single nucleotide polymorphism) on memory usage effectiveness. People with the Thymine base in a certain locus do markedly better in task involving short-term memory than those with the Cystine base at that location. The location affects the protein KIBRA.

See this discussion by John Hawks, which has links to the original paper and some other references.

http://johnhawks.net/weblog/reviews/genetics/brain/kibra_memory_association_2006.html
 
Biology news on Phys.org
Here's a more recent paper proposing some molecular mechanisms for how the Kibra protein might contribute to learning and memory:

Ji et al. Kibra Modulates Learning and Memory via Binding to Dendrin. Cell Rep 26: 2064 (2019) https://www.sciencedirect.com/science/article/pii/S2211124719301342?via=ihub
Abstract:
Kibra is a synaptic scaffold protein regulating learning and memory. Alterations of Kibra-encoding gene WWC1 cause various neuronal disorders, including Alzheimer’s disease and Tourette syndrome. However, the molecular mechanism underlying Kibra’s function in neurons is poorly understood. Here we discover that Kibra, via its N-terminal WW12 tandem domains, binds to a postsynaptic density enriched protein, Dendrin, with a nanomolar dissociation constant. On the basis of the structure of Kibra WW12 in complex with Dendrin PY motifs, we developed a potent peptide inhibitor capable of specifically blocking the binding between Kibra and Dendrin in neurons. Systematic administration of the inhibitory peptide attenuated excitatory synaptic transmission, completely blocked long-term potentiation induction, and impaired spatial learning and memory. A Kibra mutation found in Tourette syndrome patients causes defects in binding to Dendrin. Thus, Kibra can modulate spatial learning and memory via binding to Dendrin.
 
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