The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes
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The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes. / Panzer, Linda; Trübe, Leona; Klose, Matthias; Joosten, Ben; Slotman, Johan; Cambi, Alessandra; Linder, Stefan.
in: J CELL SCI, Jahrgang 129, Nr. 2, 15.01.2016, S. 298-313.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes
AU - Panzer, Linda
AU - Trübe, Leona
AU - Klose, Matthias
AU - Joosten, Ben
AU - Slotman, Johan
AU - Cambi, Alessandra
AU - Linder, Stefan
N1 - © 2016. Published by The Company of Biologists Ltd.
PY - 2016/1/15
Y1 - 2016/1/15
N2 - Podosomes are actin-rich adhesion structures that depend on Arp2/3-complex-based actin nucleation. We now report the identification of the formins FHOD1 and INF2 as novel components and additional actin-based regulators of podosomes in primary human macrophages. FHOD1 surrounds the podosome core and is also present at podosome-connecting cables, whereas INF2 localizes at the podosome cap structure. Using a variety of microscopy-based methods; including a semiautomated podosome reformation assay, measurement of podosome oscillations, FRAP analysis of single podosomes, and structured illumination microscopy, both formins were found to regulate different aspects of podosome-associated contractility, with FHOD1 mediating actomyosin contractility between podosomes, and INF2 regulating contractile events at individual podosomes. Moreover, INF2 was found to be a crucial regulator of podosome de novo formation and size. Collectively, we identify FHOD1 and INF2 as novel regulators of inter- and intra-structural contractility of podosomes. Podosomes thus present as one of the few currently identified structures which depend on the concerted activity of both Arp2/3 complex and specific formins and might serve as a model system for the analysis of complex actin architectures in cells.
AB - Podosomes are actin-rich adhesion structures that depend on Arp2/3-complex-based actin nucleation. We now report the identification of the formins FHOD1 and INF2 as novel components and additional actin-based regulators of podosomes in primary human macrophages. FHOD1 surrounds the podosome core and is also present at podosome-connecting cables, whereas INF2 localizes at the podosome cap structure. Using a variety of microscopy-based methods; including a semiautomated podosome reformation assay, measurement of podosome oscillations, FRAP analysis of single podosomes, and structured illumination microscopy, both formins were found to regulate different aspects of podosome-associated contractility, with FHOD1 mediating actomyosin contractility between podosomes, and INF2 regulating contractile events at individual podosomes. Moreover, INF2 was found to be a crucial regulator of podosome de novo formation and size. Collectively, we identify FHOD1 and INF2 as novel regulators of inter- and intra-structural contractility of podosomes. Podosomes thus present as one of the few currently identified structures which depend on the concerted activity of both Arp2/3 complex and specific formins and might serve as a model system for the analysis of complex actin architectures in cells.
U2 - 10.1242/jcs.177691
DO - 10.1242/jcs.177691
M3 - SCORING: Journal article
C2 - 26621033
VL - 129
SP - 298
EP - 313
JO - J CELL SCI
JF - J CELL SCI
SN - 0021-9533
IS - 2
ER -
