{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ito K"],"funding":["American Cancer Society","Breast Cancer Research Foundation","Susan G. Komen","New York State Department of Health","NCI NIH HHS"],"pagination":["946-957"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10977041"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(3)"],"pubmed_abstract":["Epithelial-mesenchymal transition (EMT) in cancer promotes metastasis and chemotherapy resistance. A subset of triple-negative breast cancer (TNBC) exhibits a mesenchymal gene signature that is associated with poor patient outcomes. We previously identified PTK6 tyrosine kinase as an oncogenic driver of EMT in a subset of TNBC. PTK6 induces EMT by stabilizing SNAIL, a key EMT-initiating transcriptional factor. Inhibition of PTK6 activity reverses mesenchymal features of TNBC cells and suppresses their metastases by promoting SNAIL degradation via a novel mechanism. In the current study, we identify membrane-associated RING-CH2 (MARCH2) as a novel PTK6-regulated E3 ligase that promotes the ubiquitination and degradation of SNAIL protein. The MARCH2 RING domain is critical for SNAIL ubiquiti"],"journal":["Cancer research communications"],"pubmed_title":["MARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase, Suppresses Triple-negative Breast Cancer Metastases."],"pmcid":["PMC10977041"],"funding_grant_id":["C36612GG","P30 CA196521","PDF17488499","RSG-18-044-01-LIB","CCRCR17499360"],"pubmed_authors":["Harada I","Port E","Nayak A","Ito K","Zhu J","Byerly JH","Irie HY","Martinez C","Sato K","Lee E","Tripathi E"],"additional_accession":[]},"is_claimable":false,"name":"MARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase, Suppresses Triple-negative Breast Cancer Metastases.","description":"Epithelial-mesenchymal transition (EMT) in cancer promotes metastasis and chemotherapy resistance. A subset of triple-negative breast cancer (TNBC) exhibits a mesenchymal gene signature that is associated with poor patient outcomes. We previously identified PTK6 tyrosine kinase as an oncogenic driver of EMT in a subset of TNBC. PTK6 induces EMT by stabilizing SNAIL, a key EMT-initiating transcriptional factor. Inhibition of PTK6 activity reverses mesenchymal features of TNBC cells and suppresses their metastases by promoting SNAIL degradation via a novel mechanism. In the current study, we identify membrane-associated RING-CH2 (MARCH2) as a novel PTK6-regulated E3 ligase that promotes the ubiquitination and degradation of SNAIL protein. The MARCH2 RING domain is critical for SNAIL ubiquiti","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-07-16T04:13:01.433Z","creation":"2025-04-05T23:18:16.834Z"},"accession":"S-EPMC10977041","cross_references":{"pubmed":["38457262"],"doi":["10.1158/2767-9764.CRC-23-0090"]}}