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The type III TGF? receptor regulates filopodia formation via a Cdc42-mediated IRSp53-N-WASP interaction in epithelial cells.

ABSTRACT: Cell adhesion and migration are tightly controlled by regulated changes in the actin cytoskeleton. Previously we reported that the TGF? (transforming growth factor ?) superfamily co-receptor, T?RIII (type III TGF? receptor; also known as ?glycan), regulates cell adhesion, migration and invasion, and suppresses cancer progression, in part, through activation of the small GTPase Cdc42 (cell division cycle 42), and Cdc42-dependent alterations to the actin cytoskeleton. In the present study we demonstrate that T?RIII specifically promotes filopodial formation and extension in MCF10A and HMEC (human mammary epithelial cell) mammary epithelial cells. Mechanistically, cell-surface T?RIII and Cdc42 co-localize to filopodial structures and co-complex in a ?-arrestin2-dependent, and a T?RI/T?RII-independent manner. The ?-arrestin2-mediated interaction between T?RIII and Cdc42 increases complex formation between the Cdc42 effectors IRSp53 with N-WASP (neuronal Wiskott-Aldrich syndrome protein) to increase filopodial formation. We demonstrate a function link between filopodial structures and epithelial cell adhesion as regulated by the T?RIII-Cdc42 interaction. The present studies identify T?RIII as a novel regulator of IRSp53/N-WASP via Cdc42 to regulate filopodial formation and cell adhesion.


PROVIDER: S-EPMC4082962 | BioStudies | 2013-01-01

REPOSITORIES: biostudies

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