Researchers decipher the cryo-EM structure of a spinach PSII-LHCII megacomplex, revealing architectural principles for higher-order assembly and potential regulatory mechanisms. The study identifies PsbR and PsbY as small membrane proteins regulating PSII function.
The Max Delbrück Center researchers identified a new layer of PKA regulation through the binding of ARHGAP36 to its catalytic subunit. This interaction can inhibit PKA's kinase action, and its expression is limited to embryonic muscle cells and certain types of cancer.
Researchers at LMU Munich developed a new theoretical model explaining how regulatory proteins are transported to their sites of action in microtubules. The model suggests that energy is required to capture freely diffusing particles and proposes a mechanism for efficient transport by diffusion.
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Researchers at UCSD School of Medicine have solved the structure of protein kinase A, a key enzyme involved in memory formation, nerve cell communication, and cardiac function. The study reveals how PKA is inhibited and activated by cyclic AMP, shedding light on its role in cardiac disease and breast cancer.
Researchers at UCLA have made an important advancement in protein engineering by developing a new method to control proteins using nanotechnology. They successfully replaced the natural chemical mechanism controlling protein function with mechanical control, opening up possibilities for reduced side effects and improved treatment options.
Deleting the b1 subunit of the BK channel in mice causes high blood pressure and enlarged hearts, suggesting it as a promising target for anti-hypertension drugs. The study provides a new model for investigating the molecular basis of hypertension.
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The proteasome is a crucial macromolecular machine responsible for eliminating abnormal proteins. It plays a vital role in various biological processes, including the regulation of cell cycle, apoptosis, and immune response. The molecular architecture of the 20S proteasome is conserved from archaea to eukaryotes.