Milky Way's warp caused by galactic collision, Gaia suggests

Astronomers have pondered for years why our galaxy, the Milky Way, is warped. Data from ESA's star-mapping satellite Gaia suggest the distortion might be caused by an ongoing collision with another, smaller, galaxy, which ...

ESA's next sun mission will be shadow-casting pair

After Solar Orbiter, ESA's next mission observing the sun will not be one spacecraft but two: the double satellites making up Proba-3 will fly in formation to cast an artificial solar eclipse, opening up the clearest view ...

The rare molecule weighing in on the birth of planets

Astronomers using one of the most advanced radio telescopes have discovered a rare molecule in the dust and gas disc around a young star—and it may provide an answer to one of the conundrums facing astronomers.

New coating process provides effective protection for brake discs

More than many other auto parts, brake discs are subject to repeated mechanical loads. As a result of this continual abrasion, they produce fine particulate matter, which pose a substantial environmental burden. Now, however, ...

Second baby planet found using pioneering technique

Monash astrophysicists using the ALMA telescope in Chile have a made a world-first discovery with the sighting of a second new 'baby' planet (two to three times heavier than Jupiter) inside a gas and dust gap.

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DLG4

PSD-95 (postsynaptic density protein 95) also known as SAP-90 (synapse-associated protein 90) is a protein that in humans is encoded by the DLG4 (disks large homolog 4) gene.

PSD-95 is a member of the membrane-associated guanylate kinase (MAGUK) family. With PSD-93 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.

PSD-95 is the best studied member of the MAGUK-family of PDZ domain-containing proteins. Like all MAGUK-family proteins, its basic structure includes three PDZ domains, an SH3 domain, and a guanylate kinase-like domain (GK) connected by disordered linker regions. It is almost exclusively located in the post synaptic density of neurons, and is involved in anchoring synaptic proteins. Its direct and indirect binding partners include neuroligin, NMDA receptors, AMPA receptors, and potassium channels.

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