{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(1)"],"submitter":["Watanabe K"],"pubmed_abstract":["Ildr2 was initially identified as a genetic modifier of diabetes susceptibility in B6.DBA Lep<sup>ob</sup> 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"],"journal":["Scientific reports"],"pagination":["8414"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8052334"],"repository":["biostudies-literature"],"pubmed_title":["ILDR2 stabilization is regulated by its interaction with GRP78."],"pmcid":["PMC8052334"],"pubmed_authors":["Matsumoto A","Tsuda H","Ohta S","Watanabe K","Nakayama K","Iwamoto S"],"additional_accession":[]},"is_claimable":false,"name":"ILDR2 stabilization is regulated by its interaction with GRP78.","description":"Ildr2 was initially identified as a genetic modifier of diabetes susceptibility in B6.DBA Lep<sup>ob</sup> 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","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2025-04-04T14:35:46.572Z","creation":"2022-02-09T15:51:49.914Z"},"accession":"S-EPMC8052334","cross_references":{"pubmed":["33863978"],"doi":["10.1038/s41598-021-87884-7"]}}