{"database":"bioimages","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Karim El Azzouzi"],"journal":["The Journal of Cell Biology"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-JCBD-201510043"],"attach_to":["JCB"],"legend":["MT1-MMP-pHluorin mCherry-Talin-1C.ome.acff"],"repository":["bioimages"],"figure_sub":["Figure 1 - None","Figure 1","Image 635357 (Figure 1 - None)"],"pubmed_authors":["Karim El Azzouzi","Stefan Linder","Christiane Wiesner"],"additional_accession":[]},"is_claimable":false,"name":"Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence","description":"Podosomes are dynamic cell adhesions that are also sites of extracellular matrix degradation, through recruitment of matrix-lytic enzymes, particularly of matrix metalloproteinases. Using total internal reflection fluorescence microscopy, we show that the membrane-bound metalloproteinase MT1-MMP is enriched not only at podosomes but also at distinct “islets” embedded in the plasma membrane of primary human macrophages. MT1-MMP islets become apparent upon podosome dissolution and persist beyond podosome lifetime. Importantly, the majority of MT1-MMP islets are reused as sites of podosome reemergence. siRNA-mediated knockdown and recomplementation analyses show that islet formation is based on the cytoplasmic tail of MT1-MMP and its ability to bind the subcortical actin cytoskeleton. Collect","dates":{"release":"2016-04-11T11:28:13Z","modification":"2018-11-29T11:28:13Z","creation":"2018-11-29T11:28:13Z"},"accession":"S-JCBD-201510043","cross_references":{"doi":["10.1083/jcb.201510043"]}}