The Dsc ubiquitin ligase complex identifies transmembrane degrons to degrade orphaned proteins at the Golgi.

The Golgi apparatus is essential for protein sorting, yet its quality control mechanisms are poorly understood. Here we show that the Dsc ubiquitin ligase complex uses its rhomboid pseudo-protease subunit, Dsc2, to assess the hydrophobic length of α-helical transmembrane domains (TMDs) at the Golgi. Thereby the Dsc complex likely interacts with orphaned ER and Golgi proteins that have shorter TMDs and ubiquitinates them for targeted degradation.

A case of epithelioid glioblastoma with lung metastases in a young Cane Corso dog.

Astrocytomas are relatively common primary brain tumours of humans and companion animals. In dogs, they represent approximately 17-28% of primary central nervous system tumours. However, extracranial metastasis is extremely rare.

The Dsc complex and its role in Golgi quality control.

Membrane proteins play crucial roles in cellular functions. However, processes such as the insertion of membrane proteins into the endoplasmic reticulum (ER), their folding into native structures, the assembly of multi-subunit membrane protein complexes, and their targeting from the ER to specific organelles are prone to errors and have a relatively high failure rate. To prevent the accumulation of defective or orphaned membrane proteins, quality control mechanisms assess folding, quantity, and localization of these proteins.

Gastric adenocarcinoma with carcinomatosis and degenerative joint disease of the xiphisternum in a Bactrian camel (Camelus bactrianus).

Gastric adenocarcinomas have been sporadically reported in camelids. This report describes a primary gastric adenocarcinoma and subsequent peritoneal carcinomatosis in a 20-year-old female Bactrian camel (Camelus bactrianus). Numerous metastases were present throughout the omentum, liver, abdominal lymph nodes, intestinal serosa, kidneys and lungs.