Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus
Year: 2026
Type: article
Abstract: Arginine, lysine, and ornithine are critical to several fundamental aspects of organismal physiology, including protein structure and function, the urea cycle, and intracellular signaling. These cationic amino acids are imported by several membrane transporters, most notably the Cationic Amino acid Transporters (CATs) in the SLC7 family. Of these, CAT1 is also the receptor for two orthoretroviruses, and determines the host tropism for these viruses. Here, using a combination of CryoEM and in vitro biochemical techniques, we characterize the substrate recognition and transport of CAT1 from Mus musculus. Further, by determining the structures of MmCAT1 in complex with the receptor binding domain from the Friend Murine Leukemia Virus, we identify the key structural interactions that determine the virus' rodent-specific tropism.
Source: Nature Communications
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,990
Awards: G1139804978, G2003881057, G251996476, G646469678, EUbOPEN: Enabling and Unlocking biology in the OPEN, G8080493566, G8453787180, Purchase of electron microscopic infrastructure to establish a multi-user facility for cryo electron microscopy, in particular cryo electron tomography., Investigating Mechanisms and Models Predictive of Accessibility of Therapeutics (IM2PACT) Into The Brain
OpenAlex ID: W7129003891