Abstract
The Rho family of small guanosine triphosphatases (GTPases) is critical for controlling cell shape, motility, polarity, and behavior in development and tumor progression. However, little is known about how the activity of different Rho GTPases is spatially coordinated to control these processes. Wang et al. (see the Perspective by Jaffe and Hall) examined the role of Smurf1, a HECT domain E3 ubiquitin ligase that modulates Smad signaling. The localization of Smurf1 to lamellipodia and filopodia required the activity of atypical protein kinase zeta, an effector involved in establishing cell polarity. Smurf1 controls the local level of RhoA whose accumulation in cellular protrusions is linked to the suppression of the transformed phenotype induced by knocking down Smurf1 expression. H.-R. Wang, Y. Zhang, B. Ozdamar, A. A. Ogunjimi, E. Alexandrova, G. H. Thomsen, J. L. Wrana, Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302 , 1775-1779 (2003). [Abstract] [Full Text] A. B. Jaffe, A. Hall, Smurfing at the leading edge. Science 302 , 1690-1691 (2003). [SUmmary] [Full Text]
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