Identification of TRAMs as sphingolipid-binding proteins using a photoactivatable and clickable short-chain ceramide analog.

ABSTRACT: Ceramide is a lipid molecule that regulates diverse physiological and pathological reactions in part through inverting the topology of certain transmembrane proteins. This topological inversion is achieved through regulated alternative translocation (RAT), which reverses the direction by which membrane proteins are translocated across the endoplasmic reticulum during translation. However, owing to technical challenges in studying protein-ceramide interaction, it remains unclear how ceramide levels are sensed in cells to trigger RAT. Here, we report the synthesis of pac-C₇-Cer, a photoactivatable and clickable short-chain ceramide analog that can be used as a probe to study protein-ceramide interactions. We demonstrate that translocating chain-associated membrane protein 2 (TRAM2

SUBMITTER: Deng Y 

PROVIDER: S-EPMC8665359 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature