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The peptide sequence LLAMNLGLPDLVAKYNTSNGA, part of Kelch-like protein 20 (KLHL20) in the BTB-Kelch family, is linked with important cellular functions, especially through its association with death-associated protein kinase (DAPK). KLHL20 interacts with DAPK1 by acting as an adaptor within the Cullin3 E3 ubiquitin ligase complex, facilitating ubiquitination and subsequent degradation of DAPK1. This process is crucial for regulating DAPK1 levels, which affects cellular responses to stress and contributes to pathways associated with apoptosis and autophagy.
KLHL20's role in targeting DAPK1 for degradation highlights its potential relevance in drug development, particularly for conditions involving dysregulated apoptosis, such as cancer. By modulating KLHL20’s interaction with DAPK1, there could be a therapeutic approach to control cell death pathways, offering a strategy to either promote or inhibit apoptosis based on disease context. This interaction is also involved in immune signaling and neurodegenerative conditions, making it a promising candidate for further investigation in targeted therapy research.
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