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© The Rockefeller University Press, 0021-9525/1999//453 $5.00
The Journal of Cell Biology, Volume 146, Number 2, , 1999 453-464

Original Article

Daip1, a Dictyostelium Homologue of the Yeast Actin-Interacting Protein 1, Is Involved in Endocytosis, Cytokinesis, and Motility



Angelika Konzoka, Igor Webera, Evelyn Simmetha, Ulrike Hackera, Markus Maniakb, and Annette Müller-Taubenbergera

a Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany
b MRC Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom
Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany.49-89-8578-388549-89-8578-2322/2339

amueller{at}biochem.mpg.de

The 64-kD protein DAip1 from Dictyostelium contains nine WD40-repeats and is homologous to the actin-interacting protein 1, Aip1p, from Saccharomyces cerevisiae, and to related proteins from Caenorhabditis, Physarum, and higher eukaryotes.

We show that DAip1 is localized to dynamic regions of the cell cortex that are enriched in filamentous actin: phagocytic cups, macropinosomes, lamellipodia, and other pseudopodia. In cells expressing green fluorescent protein (GFP)-tagged DAip1, the protein rapidly redistributes into newly formed cortical protrusions.

Functions of DAip1 in vivo were assessed using null mutants generated by gene replacement, and by overexpressing DAip1. DAip1-null cells are impaired in growth and their rates of fluid-phase uptake, phagocytosis, and movement are reduced in comparison to wild-type rates. Cytokinesis is prolonged in DAip1-null cells and they tend to become multinucleate. On the basis of similar results obtained by DAip1 overexpression and effects of latrunculin-A treatment, we propose a function for DAip1 in the control of actin depolymerization in vivo, probably through interaction with cofilin. Our data suggest that DAip1 plays an important regulatory role in the rapid remodeling of the cortical actin meshwork.

Key Words: actin • Dictyostelium discoideum • endocytosis • motility • WD-repeat

© 1999 The Rockefeller University Press

1.used in this paper: GFP, green fluorescent protein; Lat-A, latrunculin-A


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