Zona occludens proteins modulate podosome formation and function.
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Zona occludens proteins modulate podosome formation and function. / Kremerskothen, Joachim; Stölting, Miriam; Wiesner, Christiane; Korb-Pap, Adelheid; van Vliet, Vanessa; Linder, Stefan; Huber, Tobias B; Rottiers, Patricia; Reuzeau, Edith; Genot, Elisabeth; Pavenstädt, Hermann.
in: FASEB J, Jahrgang 25, Nr. 2, 2, 2011, S. 505-514.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Zona occludens proteins modulate podosome formation and function.
AU - Kremerskothen, Joachim
AU - Stölting, Miriam
AU - Wiesner, Christiane
AU - Korb-Pap, Adelheid
AU - van Vliet, Vanessa
AU - Linder, Stefan
AU - Huber, Tobias B
AU - Rottiers, Patricia
AU - Reuzeau, Edith
AU - Genot, Elisabeth
AU - Pavenstädt, Hermann
PY - 2011
Y1 - 2011
N2 - Podosomes are highly dynamic structures that are involved in cell adhesion and extracellular matrix remodeling. They present as intracellular columns composed of an actin-rich core region and a surrounding ring-like structure containing focal adhesion proteins, actin binders as well as cell signaling molecules. A key player in podosome biogenesis is the scaffolding protein cortactin, which is thought to control actin assembly at the core region. We show that the zona occludens protein 1 (ZO-1), a pivotal tight junction protein and known binding partner of cortactin, is a component of podosomes. In the smooth muscle cell line A7r5, phorbol ester treatment induced a rapid relocation of ZO-1 from the cell cortex and cytosolic pools toward newly formed podosomes. Podosomal localization was also observed for the known ZO-1-binding proteins l-afadin, -catenin, and phospho-connexin 43. Truncation studies revealed that the actin-binding domain but not the association with cortactin is necessary for ZO-1 recruitment to podosomes. Moreover, impaired ZO-1 expression leads to significantly reduced podosome formation and concomitant decreased matrix degradation at podosomes. Our findings demonstrate that besides their known function in tight junction assembly and intercellular communication, zona occludens proteins and their binding partners may play a novel role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling.
AB - Podosomes are highly dynamic structures that are involved in cell adhesion and extracellular matrix remodeling. They present as intracellular columns composed of an actin-rich core region and a surrounding ring-like structure containing focal adhesion proteins, actin binders as well as cell signaling molecules. A key player in podosome biogenesis is the scaffolding protein cortactin, which is thought to control actin assembly at the core region. We show that the zona occludens protein 1 (ZO-1), a pivotal tight junction protein and known binding partner of cortactin, is a component of podosomes. In the smooth muscle cell line A7r5, phorbol ester treatment induced a rapid relocation of ZO-1 from the cell cortex and cytosolic pools toward newly formed podosomes. Podosomal localization was also observed for the known ZO-1-binding proteins l-afadin, -catenin, and phospho-connexin 43. Truncation studies revealed that the actin-binding domain but not the association with cortactin is necessary for ZO-1 recruitment to podosomes. Moreover, impaired ZO-1 expression leads to significantly reduced podosome formation and concomitant decreased matrix degradation at podosomes. Our findings demonstrate that besides their known function in tight junction assembly and intercellular communication, zona occludens proteins and their binding partners may play a novel role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling.
M3 - SCORING: Zeitschriftenaufsatz
VL - 25
SP - 505
EP - 514
JO - FASEB J
JF - FASEB J
SN - 0892-6638
IS - 2
M1 - 2
ER -
