A powerful strategy to study protein function has been to deplete a protein of interest from the cell and then study the consequences. Leo James’ group has exploited new understanding of TRIM21’s mechanism of activation to develop new tools for targeted protein degradation.
Studying splicing fidelity has been difficult as some of the factors known to promote correct splice site use bind the spliceosome only transiently. Kiyoshi Nagai’s group have developed a method to study how proteins that ensure fidelity bind to RNA at different stages of splicing.
The intracellular immune receptor TRIM21 detects antibody-bound viruses inside our cells and targets them for destruction by creation of a polyubiquitin signal. David Neuhaus’ group, with Leo James’, has shown that TRIM21 is both the enzyme and recipient of the ubiquitination.
The airways in our lungs are kept clear of mucus by the rhythmic beating motion of slender cellular extensions called cilia, driven by dynein motors. Andrew Carter’s group, has discovered a novel protein that packages these molecular motors for delivery into the cilia.
Chris Russo’s, David Barford’s, Jan Löwe’s, and John Sutherland’s groups have together solved the structure of the inhibitor favipiravir-RTP in complex with the SARS-CoV-2 RNA-dependent RNA polymerase, providing new insight into its mechanism of action.
Scientists had thought that the protease furin was responsible for cleavage of the SARS-CoV-2 Spike protein to reveal the fusion machinery that enables infection, but new work from Leo James’ group shows that furin is not essential for SARS-CoV-2 infection.