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Originally published as MBC in Press, 10.1091/mbc.E08-05-0469 on September 24, 2008

Vol. 19, Issue 12, 5168-5180, December 2008

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INF1 Is a Novel Microtubule-associated Formin

Kevin G. Young, Susan F. Thurston, Sarah Copeland, Chelsea Smallwood, and John W. Copeland

Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, Canada, K1H 8M5

Submitted May 8, 2008; Revised August 15, 2008; Accepted September 17, 2008
Monitoring Editor: Fred Chang

Formin proteins, characterized by the presence of conserved formin homology (FH) domains, play important roles in cytoskeletal regulation via their abilities to nucleate actin filament formation and to interact with multiple other proteins involved in cytoskeletal regulation. The C-terminal FH2 domain of formins is key for actin filament interactions and has been implicated in playing a role in interactions with microtubules. Inverted formin 1 (INF1) is unusual among the formin family in having the conserved FH1 and FH2 domains in its N-terminal half, with its C-terminal half being composed of a unique polypeptide sequence. In this study, we have examined a potential role for INF1 in regulating microtubule structure. INF1 associates discretely with microtubules, and this association is dependent on a novel C-terminal microtubule-binding domain. INF1 expressed in fibroblast cells induced actin stress fiber formation, coalignment of microtubules with actin filaments, and the formation of bundled, acetylated microtubules. Endogenous INF1 showed an association with acetylated microtubules, and knockdown of INF1 resulted in decreased levels of acetylated microtubules. Our data suggests a role for INF1 in microtubule modification and potentially in coordinating microtubule and F-actin structure.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-05-0469) on September 24, 2008.

Address correspondence to: John W. Copeland (jcopelan{at}uottawa.ca)

Abbreviations used: DAD, diaphanous autoregulatory domain; DID, diaphanous inhibitory domain; FH1 and FH2, formin homology 1 and 2 domains; MTBD, microtubule-binding domain.




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E. S. Chhabra, V. Ramabhadran, S. A. Gerber, and H. N. Higgs
INF2 is an endoplasmic reticulum-associated formin protein
J. Cell Sci., May 1, 2009; 122(9): 1430 - 1440.
[Abstract] [Full Text] [PDF]


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