J. J. G. Tesmer

This paper reports cryo-EM structures of ACKR3-arrestin2/3 complexes phosphorylated by GRK2 or GRK5, revealing how phosphorylation barcodes influence arrestin binding modes and receptor configuration.

This study identifies GRK2-mediated phosphorylation of SMO in the primary cilium as a critical step initiating SMO-PKA signaling in the Hedgehog pathway.

This study identifies two distinct Gβγ binding sites on PI3Kγ and shows how Gβγ activates the enzyme through conformational changes and allosteric control.

This study reports cryo-EM structures of AC5 with Gβγ and proposes a mechanism for its isoform-specific regulation, linking it to motor function and potential drug development.

This study shows that ACKR3 senses CXCR4 activation via GRK2-dependent phosphorylation, with GRK5 playing a dominant role in {beta}-arrestin recruitment and chemokine scavenging.

This study shows insulin impairs β2AR function via GRK2 and PP2A inhibition, with PI3Kγ regulating PP2A to sustain β2AR phosphorylation.

This paper introduces an automatic cryo-EM preprocessing pipeline using deep learning and image analysis tools, verified on multiple datasets and extended to include user-free sample screening.

The paper reports the crystal structure of LCAT bound to an activator and inhibitor, showing how the activator stabilizes the MBD and enhances LCAT activity in FLD variants.