Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence
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Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence. / El Azzouzi, Karim; Wiesner, Christiane; Linder, Stefan.
In: J CELL BIOL, Vol. 213, No. 1, 11.04.2016, p. 109-25.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence
AU - El Azzouzi, Karim
AU - Wiesner, Christiane
AU - Linder, Stefan
N1 - © 2016 El Azzouzi et al.
PY - 2016/4/11
Y1 - 2016/4/11
N2 - 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. Collectively, our data reveal a previously unrecognized phase in the podosome life cycle and identify a structural function of MT1-MMP that is independent of its proteolytic activity. MT1-MMP islets thus act as cellular memory devices that enable efficient and localized reformation of podosomes, ensuring coordinated matrix degradation and invasion.POM-Newsletter
AB - 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. Collectively, our data reveal a previously unrecognized phase in the podosome life cycle and identify a structural function of MT1-MMP that is independent of its proteolytic activity. MT1-MMP islets thus act as cellular memory devices that enable efficient and localized reformation of podosomes, ensuring coordinated matrix degradation and invasion.POM-Newsletter
U2 - 10.1083/jcb.201510043
DO - 10.1083/jcb.201510043
M3 - SCORING: Journal article
C2 - 27069022
VL - 213
SP - 109
EP - 125
JO - J CELL BIOL
JF - J CELL BIOL
SN - 0021-9525
IS - 1
ER -