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Published online May 5, 2008
doi:10.1083/jcb.200709029
The Journal of Cell Biology, Vol. 181, No. 3, 523-536
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Bartolini et al.
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Article

 The formin mDia2 stabilizes microtubules independently of its actin nucleation activity

Francesca Bartolini1, James B. Moseley2, Jan Schmoranzer1, Lynne Cassimeris3, Bruce L. Goode2, and Gregg G. Gundersen1

1 Department of Pathology, Anatomy and Cell Biology, Columbia University, New York, NY 10032
2 Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454
3 Department of Biological Sciences, Lehigh University, Bethlehem, PA 18015

Correspondence to Gregg G. Gundersen: ggg1{at}columbia.edu

A critical microtubule (MT) polarization event in cell migration is the Rho/mDia-dependent stabilization of a subset of MTs oriented toward the direction of migration. Although mDia nucleates actin filaments, it is unclear whether this or a separate activity of mDia underlies MT stabilization. We generated two actin mutants (K853A and I704A) in a constitutively active version of mDia2 containing formin homology domains 1 and 2 (FH1FH2) and found that they still induced stable MTs and bound to the MT TIP proteins EB1 and APC, which have also been implicated in MT stabilization. A dimerization-impaired mutant of mDia2 (W630A) also generated stable MTs in cells. We examined whether FH1FH2mDia2 had direct activity on MTs in vitro and found that it bound directly to MTs, stabilized MTs against cold- and dilution-induced disassembly, and reduced the rates of growth and shortening during MT assembly and disassembly, respectively. These results indicate that mDia2 has a novel MT stabilization activity that is separate from its actin nucleation activity.

J.B. Moseley's present address is Laboratory of Yeast Genetics and Cell Biology, The Rockefeller University, New York, NY 10021.

Abbreviations used in this paper: DAD, diaphanous autoregulatory domain; DIC, differential interference contrast; DRF, Diaphanous-related formin; FH, formin homology; GBD, GTPase binding domain; LPA, lysophosphatidic acid; MT, microtubule; TIRF, total internal reflection fluorescence.


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