ILDR2 stabilization is regulated by its interaction with GRP78.

ABSTRACT: Ildr2 was initially identified as a genetic modifier of diabetes susceptibility in B6.DBA Lep^ob congenic mice, and was associated with decreased β-cell replication rates, reduced β-cell mass, and persistent mild hypoinsulinemic hyperglycemia. However, the molecular mechanisms of how the ILDR2 protein is involved in these effects are largely unknown. We sought to identify ILDR2-interacting proteins to further elucidate the molecular mechanisms underpinning ILDR2 function in pancreatic β-cells. Using TAP tag technology, we purified proteins interacting with ILDR2 in the pancreatic β-cell line MIN6, and identified the endoplasmic reticulum resident chaperones, GRP78 and PDIA1, as novel proteins interacting with ILDR2. We demonstrated that GRP78 interacted with ILDR2 and was possibl

SUBMITTER: Watanabe K 

PROVIDER: S-EPMC8052334 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature