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Published online 7 August 2000. doi:10.1083/jcb.150.3.539
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© The Rockefeller University Press, 0021-9525/2000//539 $5.00
The Journal of Cell Biology, Volume 150, Number 3, , 2000 539-552

Original Article

Functional Analysis of a Human Homologue of the Drosophila Actin Binding Protein Anillin Suggests a Role in Cytokinesis



Karen Oegemaa, Matthew S. Savoianc, Timothy J. Mitchisonb, and Christine M. Fieldb

a Cell Biology Program, European Molecular Biology Laboratory, Heidelberg, Germany D-69117
b Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115
c Division of Molecular Medicine, New York State Department of Health, Wadsworth Center, Albany, New York 12201-0509
Cell Biology Program, European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany D-69117.49-6221-387-51249-6221-387-337

karen.oegema{at}embl-heidelberg.de

We have characterized a human homologue of anillin, a Drosophila actin binding protein. Like Drosophila anillin, the human protein localizes to the nucleus during interphase, the cortex following nuclear envelope breakdown, and the cleavage furrow during cytokinesis. Anillin also localizes to ectopic cleavage furrows generated between two spindles in fused PtK1 cells. Microinjection of antianillin antibodies slows cleavage, leading to furrow regression and the generation of multinucleate cells. GFP fusions that contain the COOH-terminal 197 amino acids of anillin, which includes a pleckstrin homology (PH) domain, form ectopic cortical foci during interphase. The septin Hcdc10 localizes to these ectopic foci, whereas myosin II and actin do not, suggesting that anillin interacts with the septins at the cortex. Robust cleavage furrow localization requires both this COOH-terminal domain and additional NH2-terminal sequences corresponding to an actin binding domain defined by in vitro cosedimentation assays. Endogenous anillin and Hcdc10 colocalize to punctate foci associated with actin cables throughout mitosis and the accumulation of both proteins at the cell equator requires filamentous actin. These results indicate that anillin is a conserved cleavage furrow component important for cytokinesis. Interactions with at least two other furrow proteins, actin and the septins, likely contribute to anillin function.

Key Words: Hedc10 • pleckstrin homology domain • septin • cleavage furrow • cortex

© 2000 The Rockefeller University Press

Abbreviations used in this paper: GFP, green fluorescent protein; hsanillin, human anillin; PH, pleckstrin homology.


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