Sarah Henretta, Karisa Bockley, Jacob Odell, Jan Lammerding
{"title":"Filamin A interacting protein 1-like (FILIP1L) has mitochondrial localization.","authors":"Sarah Henretta, Karisa Bockley, Jacob Odell, Jan Lammerding","doi":"10.17912/micropub.biology.001572","DOIUrl":null,"url":null,"abstract":"<p><p>Filamin A interacting protein 1-like (FILIP1L) is a multifunctional protein that plays a role in cancer progression, apoptosis, and angiogenesis. However, FILIP1L remains a relatively underexplored protein, and many of FILIP1L's key mechanisms and interacting partners are still unknown. Using immunofluorescence staining for endogenous FILIP1L and high-resolution confocal microscopy, we show that FILIP1L colocalizes with the mitochondrial marker, TOM20, suggesting a novel connection between FILIP1L and mitochondria. Further exploring the relationship between FILIP1L and mitochondria might provide a deeper understanding of the emerging function of FILIP1L in health and disease.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2025 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11979717/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"microPublication biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17912/micropub.biology.001572","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Filamin A interacting protein 1-like (FILIP1L) is a multifunctional protein that plays a role in cancer progression, apoptosis, and angiogenesis. However, FILIP1L remains a relatively underexplored protein, and many of FILIP1L's key mechanisms and interacting partners are still unknown. Using immunofluorescence staining for endogenous FILIP1L and high-resolution confocal microscopy, we show that FILIP1L colocalizes with the mitochondrial marker, TOM20, suggesting a novel connection between FILIP1L and mitochondria. Further exploring the relationship between FILIP1L and mitochondria might provide a deeper understanding of the emerging function of FILIP1L in health and disease.