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MBC in Press, published online ahead of print October 18, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0767

A more recent version of this article appeared on December 1, 2006
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Submitted on August 30, 2006
Revised on September 28, 2006
Accepted on October 5, 2006

Enlazin, a Natural Fusion of Two Classes of Canonical Cytoskeletal Proteins, Contributes to Cytokinesis Dynamics

Edelyn Octtaviani, Janet C. Effler, and Douglas N. Robinson

Department of Cell Biology, Johns Hopkins School of Medicine, Baltimore, MD 21205

Monitoring Editor: Yu-li Wang

Cytokinesis requires a complex network of equatorial and global proteins to regulate cell shape changes. Here, using interaction genetics, we report the first characterization of a novel protein, enlazin. Enlazin is a natural fusion of two canonical classes of actin-associated proteins, the ERMs and fimbrin, and is localized to actin-rich structures. A fragment of enlazin (enl-tr) was isolated as a genetic suppressor of the cytokinesis defect of cortexillin-I mutants. Expression of enl-tr disrupts expression of endogenous enlazin, indicating that enl-tr functions as a dominant-negative lesion. Enlazin is distributed globally during cytokinesis and is required for cortical tension and cell adhesion. Consistent with a role in cell mechanics, inhibition of enlazin in a cortexillin-I background restores cytokinesis furrowing dynamics and suppresses the growth-in-suspension defect. However, as expected for a role in cell adhesion, inhibiting enlazin in a myosin-II background induces a synthetic cytokinesis phenotype, frequently arresting furrow ingression at the dumbbell shape and/or causing recession of the furrow. Thus, enlazin has roles in cell mechanics and adhesion, and these roles appear to be differentially significant for cytokinesis, depending on the genetic background.

Address correspondence to: Douglas N. Robinson (dnr{at}jhmi.edu)




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