{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Su C"],"funding":["National Natural Science Foundation of China"],"pagination":["107694"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11480233"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(10)"],"pubmed_abstract":["The canonical Wnt signaling pathway plays crucial roles in cell fate decisions as well as in pathogenesis of various diseases. Previously, we reported Caprin-2 as a new regulator of canonical Wnt signaling through a mechanism of facilitating LRP5/6 phosphorylation. Here, we resolved the crystal structure of the N-terminal homologous region 1 (HR1) domain of human Caprin-2. HR1 domain is so far only observed in Caprin-2 and its homologous protein Caprin-1, and the function of this domain remains largely mysterious. Here, the structure showed that HR1 domain of human Caprin-2 forms a homo-dimer and exhibits an overall structure roughly resembling the appearance of a pair of scissors. Moreover, we found that residues R200 and R201, which located at a basic cluster within the N-terminal \"blade"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Structural insights into the Caprin-2 HR1 domain in canonical Wnt signaling."],"pmcid":["PMC11480233"],"funding_grant_id":["31100532","31530094"],"pubmed_authors":["Su C","Miao H","Zhong Y","Luo H","Shi Z","Li L","Xie S","Zhou Z","Li Y","Li Z","Jia Y","Song X","Zhao J"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into the Caprin-2 HR1 domain in canonical Wnt signaling.","description":"The canonical Wnt signaling pathway plays crucial roles in cell fate decisions as well as in pathogenesis of various diseases. Previously, we reported Caprin-2 as a new regulator of canonical Wnt signaling through a mechanism of facilitating LRP5/6 phosphorylation. Here, we resolved the crystal structure of the N-terminal homologous region 1 (HR1) domain of human Caprin-2. HR1 domain is so far only observed in Caprin-2 and its homologous protein Caprin-1, and the function of this domain remains largely mysterious. Here, the structure showed that HR1 domain of human Caprin-2 forms a homo-dimer and exhibits an overall structure roughly resembling the appearance of a pair of scissors. Moreover, we found that residues R200 and R201, which located at a basic cluster within the N-terminal \"blade","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-06-01T09:54:06.418Z","creation":"2025-04-04T01:25:56.386Z"},"accession":"S-EPMC11480233","cross_references":{"pubmed":["39159816"],"doi":["10.1016/j.jbc.2024.107694"]}}