The unfolded protein response regulates ER exit sites via SNRPB-dependent RNA splicing and contributes to bone development.

ABSTRACT: Splicing and endoplasmic reticulum (ER)-proteostasis are two key processes that ultimately regulate the functional proteins that are produced by a cell. However, the extent to which these processes interact remains poorly understood. Here, we identify SNRPB and other components of the Sm-ring, as targets of the unfolded protein response and novel regulators of export from the ER. Mechanistically, The Sm-ring regulates the splicing of components of the ER export machinery, including Sec16A, a component of ER exit sites. Loss of function of SNRPB is causally linked to cerebro-costo-mandibular syndrome (CCMS), a genetic disease characterized by bone defects. We show that heterozygous deletion of SNRPB in mice resulted in bone defects reminiscent of CCMS and that knockdown of SNRPB delays traf

SUBMITTER: Dr. Muhammad Zahoor 

PROVIDER: S-SCDT-10_1038-S44318-024-00208-Z | biostudies-other |

REPOSITORIES: biostudies-other