Structural basis of Sphingosine-1-phosphate transport via human SPNS2

No abstract available.

This study solves the structures of human spinster homolog 2 protein (SPNS2) in multiple states, including apo, sphingosine 1-phosphate (S1P)-bound, FTY720-P-bound, and 16d-bound states, providing a structural basis for understanding the S1P transport mechanism.

Through an S1P transport assay, the study reveals that SPNS2 directly transports S1P instead of sphingosine and SPNS2 is not a proton or sodium/potassium-dependent transporter.

These findings provide a framework for understanding the S1P transport mechanism and a rational basis for designing inhibitors targeting SPNS2.