{"database":"bioimages","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":[null],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-BIAD952"],"repository":["bioimages"],"figure_sub":["Specimen","Funding","Study Component","organisation","Biosample","Associations","Image acquisition"],"pubmed_authors":["Lisa Gold","Silke Hoffmann","Oliver H. Weiergräber","Alina Üffing","Thomas Gensch","Dieter Willbold"],"additional_accession":[]},"is_claimable":false,"name":"Highlighting the hidden: Monitoring the avidity-driven association of a fluorescent GABARAP tandem with microtubules in living cells","description":"GABARAP, like other ATG8 proteins, is a ubiquitin-like modifier and its C-terminal lipid conjugation enables association with cellular membranes. To prevent interference with the lipidation process, N-terminal fluorescent protein (FP) tagging strategies have become the standard for studying ATG8 localization and function in living cells, significantly contributing to our understanding of this protein family's multifaceted roles. \nWe employed live cell imaging with particular emphasis on a GABARAP split-tandem construct, GABARAP(G116A)-mTagBFP2-GABARAP (G-B-G), which retains both a free N-terminus and a lipidation-competent C-terminus, while bivalence creates a gain in affinity conferred by avidity. Notably, reminiscent of early in vitro studies demonstrating an interaction of GABARAP and t","dates":{"release":"2023-11-30T00:00:00Z","modification":"2024-05-07T14:39:47.068Z","creation":"2023-11-22T14:37:27.335Z"},"accession":"S-BIAD952","cross_references":{}}