The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages.
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The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages. / Kopp, Petra; Lammers, Reiner; Aepfelbacher, Martin; Woehlke, Günther; Rudel, Thomas; Machuy, Nikolaus; Steffen, Walter; Linder, Stefan.
in: MOL BIOL CELL, Jahrgang 17, Nr. 6, 6, 2006, S. 2811-2823.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages.
AU - Kopp, Petra
AU - Lammers, Reiner
AU - Aepfelbacher, Martin
AU - Woehlke, Günther
AU - Rudel, Thomas
AU - Machuy, Nikolaus
AU - Steffen, Walter
AU - Linder, Stefan
PY - 2006
Y1 - 2006
N2 - Microtubules are important for the turnover of podosomes, dynamic, actin-rich adhesions implicated in migration and invasion of monocytic cells. The molecular basis for this functional dependency, however, remained unclear. Here, we show that contact by microtubule plus ends critically influences the cellular fate of podosomes in primary human macrophages. In particular, we identify the kinesin KIF1C, a member of the Kinesin-3 family, as a plus-end-enriched motor that targets regions of podosome turnover. Expression of mutation constructs or small interfering RNA-/short hairpin RNA-based depletion of KIF1C resulted in decreased podosome dynamics and ultimately in podosome deficiency. Importantly, protein interaction studies showed that KIF1C binds to nonmuscle myosin IIA via its PTPD-binding domain, thus providing an interface between the actin and tubulin cytoskeletons, which may facilitate the subcellular targeting of podosomes by microtubules. This is the first report to implicate a kinesin in podosome regulation and also the first to describe a function for KIF1C in human cells.
AB - Microtubules are important for the turnover of podosomes, dynamic, actin-rich adhesions implicated in migration and invasion of monocytic cells. The molecular basis for this functional dependency, however, remained unclear. Here, we show that contact by microtubule plus ends critically influences the cellular fate of podosomes in primary human macrophages. In particular, we identify the kinesin KIF1C, a member of the Kinesin-3 family, as a plus-end-enriched motor that targets regions of podosome turnover. Expression of mutation constructs or small interfering RNA-/short hairpin RNA-based depletion of KIF1C resulted in decreased podosome dynamics and ultimately in podosome deficiency. Importantly, protein interaction studies showed that KIF1C binds to nonmuscle myosin IIA via its PTPD-binding domain, thus providing an interface between the actin and tubulin cytoskeletons, which may facilitate the subcellular targeting of podosomes by microtubules. This is the first report to implicate a kinesin in podosome regulation and also the first to describe a function for KIF1C in human cells.
M3 - SCORING: Zeitschriftenaufsatz
VL - 17
SP - 2811
EP - 2823
JO - MOL BIOL CELL
JF - MOL BIOL CELL
SN - 1059-1524
IS - 6
M1 - 6
ER -