Researchers Identified EPHA2 as LAT3 Regulator
The kinase EPHA2 has been identified as a regulator that destabilizes the amino acid transporter LAT3.
Updated on Sept. 26, 2026 in Life Sciences
Researchers have identified the receptor kinase EPHA2 as a negative regulator that controls the stability of the LAT3 protein. This research-stage finding describes a mechanism where EPHA2 phosphorylates the transporter, providing new insight into protein regulation.
Why it matters
Understanding how LAT3 is regulated is critical to mapping how cells transport essential amino acids. This discovery identifies the specific interaction that limits LAT3 abundance, revealing a key control point in protein stability.
The study identified 167 high-confidence membrane-associated interactors for LAT3, 43 of which localized to the plasma membrane. EPHA2 was confirmed as the only receptor kinase to phosphorylate LAT3 at tyrosine 251.
The players
EPHA2
A receptor tyrosine kinase identified as a negative regulator of LAT3 protein stability.
LAT3
A protein that mediates the sodium-independent transport of neutral and branched-chain amino acids.
The details
Researchers utilized a photo-lysine-based optoproteomics strategy—a method using light-activated amino acids to map protein-protein interactions—combined with affinity purification-mass spectrometry to isolate LAT3 candidates. They found that EPHA2 directly interacts with LAT3 and triggers phosphorylation at tyrosine 251, a chemical modification that influences protein stability. When EPHA2 is inhibited, the abundance of LAT3 protein increases, confirming its role as a negative regulator of the transporter.
Timeline
September 26, 2026: The research findings were published.
The Tech Race
This research contributes to the broader effort within the human membrane proteome mapping initiative to define the regulatory networks governing nutrient transport. It refines our understanding of protein stability in a field currently focused on identifying actionable targets for metabolic control.
This discovery provides researchers with a new molecular target, EPHA2, for studying amino acid transport dynamics in laboratory settings. While this is currently research-stage and does not affect clinical workflows today, it establishes a framework for future studies on LAT3-mediated processes.
The takeaway
The identification of the EPHA2 kinase as a negative regulator of LAT3 offers a concrete site—tyrosine 251—for further functional exploration. Researchers should monitor subsequent studies that characterize the impact of EPHA2 inhibition on cellular amino acid uptake rates.
Further reading
For more on the molecular mechanisms of protein transport, visit Life Sciences.
More information
Read the complete peer-reviewed research article published in Nature.
Source note: This article includes information reported by Nature.
