{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang K"],"funding":["American Heart Association","NCATS NIH HHS","American Heart Association-American Stroke Association","NCI NIH HHS","U.S. Department of Health & Human Services | National Institutes of Health (NIH)","U.S. Department of Health & Human Services | National Institutes of Health","NIGMS NIH HHS","American Heart Association (American Heart Association, Inc.)"],"pagination":["1998"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11865535"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Protein degradation orchestrated by SKP1·CUL1·F-box protein (SCF) ubiquitin ligases is a fundamental process essential for cellular and organismal function. The dynamic assembly of SCFs, facilitated by CAND1, ensures timely ubiquitination of diverse SCF target proteins. As a homolog of CAND1, CAND2 alone has been implicated in various human diseases, yet its functional mechanisms remain elusive. Here, we investigate the role of CAND2 in human cells and its distinct mode of action compared to CAND1. Using an array of quantitative assays, we demonstrate that CAND2 promotes SCF-mediated protein degradation as an F-box protein exchange factor. While CAND2 binds CUL1 with structure and affinity comparable to CAND1, it exhibits lower efficiency in exchanging F-box proteins. Kinetic measurements "],"journal":["Nature communications"],"pubmed_title":["Molecular mechanisms of CAND2 in regulating SCF ubiquitin ligases."],"pmcid":["PMC11865535"],"funding_grant_id":["20CDA35270030 - XING LIU","U24 GM129541","T32 GM132024","R35 GM138016","905924/SK/2021","UL1 TR002529","R01GM143268","P30 CA023168","P30 CA082709","T32GM132024","R01 GM143268","P30CA023168","R35GM138016","20CDA35270030"],"pubmed_authors":["Liu X","Reitsma JM","Das C","Kenny S","Zhou Y","Li L","Wang K","Gan D"],"additional_accession":[]},"is_claimable":false,"name":"Molecular mechanisms of CAND2 in regulating SCF ubiquitin ligases.","description":"Protein degradation orchestrated by SKP1·CUL1·F-box protein (SCF) ubiquitin ligases is a fundamental process essential for cellular and organismal function. The dynamic assembly of SCFs, facilitated by CAND1, ensures timely ubiquitination of diverse SCF target proteins. As a homolog of CAND1, CAND2 alone has been implicated in various human diseases, yet its functional mechanisms remain elusive. Here, we investigate the role of CAND2 in human cells and its distinct mode of action compared to CAND1. Using an array of quantitative assays, we demonstrate that CAND2 promotes SCF-mediated protein degradation as an F-box protein exchange factor. While CAND2 binds CUL1 with structure and affinity comparable to CAND1, it exhibits lower efficiency in exchanging F-box proteins. Kinetic measurements ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-06-01T18:00:11.853Z","creation":"2025-04-04T02:54:01.475Z"},"accession":"S-EPMC11865535","cross_references":{"pubmed":["40011427"],"doi":["10.1038/s41467-025-57065-5"]}}