Publications by authors named "Polina Isaikina"

Article Synopsis
  • - Arrestins are key proteins that help regulate G protein-coupled receptors (GPCRs) by promoting their desensitization after they are activated and phosphorylated, while also enabling distinct signaling pathways independent of G proteins.
  • - Non-visual GPCRs feature diverse receptors controlled by just two human non-visual arrestin isoforms, and recent research has examined GPCR-arrestin complexes using various structural and biochemical techniques.
  • - Current studies reveal that the stability and activity of GPCR-arrestin complexes are influenced by the specific patterns and density of phosphorylation sites, but more high-resolution structural data is needed to fully understand these interactions for developing targeted therapeutics.
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The two non-visual arrestins, arrestin2 and arrestin3, bind hundreds of GPCRs with different phosphorylation patterns, leading to distinct functional outcomes. Structural information on these interactions is available only for very few GPCRs. Here, we have characterized the interactions between the phosphorylated human CC chemokine receptor 5 (CCR5) and arrestin2.

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The numerous chemokines and their cognate G protein-coupled chemokine receptors on the surface of leukocytes form a complex signaling network, which regulates the immune response and also other key physiological processes. Currently only a very limited number of structures of chemokine•chemokine receptor complexes have been solved. More structures are needed for the understanding of their mechanism of action and the rational design of drugs against these highly relevant therapeutic targets.

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The human CC chemokine receptor 5 (CCR5) is a G protein-coupled receptor (GPCR) that plays a major role in inflammation and is involved in cancer, HIV, and COVID-19. Despite its importance as a drug target, the molecular activation mechanism of CCR5, i.e.

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