期刊
BIOMOLECULES
卷 11, 期 3, 页码 -出版社
MDPI
DOI: 10.3390/biom11030377
关键词
RAS; dimers; multimers; nanoclusters; membrane dynamics; nonproductive interfaces
资金
- National Cancer Institute, National Institutes of Health [HHSN261200800001E]
RAS proteins are mutated in about 20% of cancers, and are associated with poor clinical outcomes. They function as molecular switches on the plasma membrane and form dynamic nanoclusters, which respond to cellular input signals. Disruption of these nanoclusters can lead to downregulation of signaling.
RAS proteins are mutated in approximately 20% of all cancers and are generally associated with poor clinical outcomes. RAS proteins are localized to the plasma membrane and function as molecular switches, turned on by partners that receive extracellular mitogenic signals. In the on-state, they activate intracellular signal transduction cascades. Membrane-bound RAS molecules segregate into multimers, known as nanoclusters. These nanoclusters, held together through weak protein-protein and protein-lipid associations, are highly dynamic and respond to cellular input signals and fluctuations in the local lipid environment. Disruption of RAS nanoclusters results in downregulation of RAS-mediated mitogenic signaling. In this review, we discuss the propensity of RAS proteins to display clustering behavior and the interfaces that are associated with these assemblies. Strategies to therapeutically disrupt nanocluster formation or the stabilization of signaling incompetent RAS complexes are discussed.
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