<HashMap><database>bioimages</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Karim El Azzouzi</submitter><journal>The Journal of Cell Biology</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-JCBD-201510043</full_dataset_link><attach_to>JCB</attach_to><legend>MT1-MMP-pHluorin mCherry-Talin-1C.ome.acff</legend><repository>bioimages</repository><figure_sub>Figure 1 - None</figure_sub><figure_sub>Figure 1</figure_sub><figure_sub>Image 635357 (Figure 1 - None)</figure_sub><pubmed_authors>Karim El Azzouzi</pubmed_authors><pubmed_authors>Stefan Linder</pubmed_authors><pubmed_authors>Christiane Wiesner</pubmed_authors></additional><is_claimable>false</is_claimable><name>Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence</name><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</description><dates><release>2016-04-11T11:28:13Z</release><modification>2018-11-29T11:28:13Z</modification><creation>2018-11-29T11:28:13Z</creation></dates><accession>S-JCBD-201510043</accession><cross_references><doi>10.1083/jcb.201510043</doi></cross_references></HashMap>