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Published online July 9, 2007
doi:10.1083/jcb.200612071
The Journal of Cell Biology, Vol. 178, No. 2, 193-200
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Brandt et al.
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 Dia1 and IQGAP1 interact in cell migration and phagocytic cup formation

Dominique T. Brandt1, Sabrina Marion2, Gareth Griffiths2, Takashi Watanabe3, Kozo Kaibuchi3, and Robert Grosse1

1 Institute of Pharmacology, University of Heidelberg, 69120 Heidelberg, Germany
2 European Molecular Biology Laboratory Heidelberg, 69117 Heidelberg, Germany
3 Department of Cell Pharmacology, Nagoya University Graduate School of Medicine, Nagoya, Aichi 466-8550, Japan

Correspondence to Robert Grosse: Robert.Grosse{at}pharma.uni-heidelberg.de

The Diaphanous-related formin Dia1 nucleates actin polymerization, thereby regulating cell shape and motility. Mechanisms that control the cellular location of Dia1 to spatially define actin polymerization are largely unknown. In this study, we identify the cytoskeletal scaffold protein IQGAP1 as a Dia1-binding protein that is necessary for its subcellular location. IQGAP1 interacts with Dia1 through a region within the Diaphanous inhibitory domain after the RhoA-mediated release of Dia1 autoinhibition. Both proteins colocalize at the front of migrating cells but also at the actin-rich phagocytic cup in macrophages. We show that IQGAP1 interaction with Dia1 is required for phagocytosis and phagocytic cup formation. Thus, we identify IQGAP1 as a novel component involved in the regulation of phagocytosis by mediating the localization of the actin filament nucleator Dia1.

Abbreviations used in this paper: Arp2/3, actin-related protein 2/3; DAD, Diaphanous autoregulatory domain; DBR, Dia1-binding region; DID, Diaphanous inhibitory domain; DRF, Diaphanous-related formin; F-actin, filamentous actin; FH, formin homology; RBD, RhoA-binding domain; SRF, serum response factor.


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