ArticleMolecular biology of the cell2004
DWWA, a novel protein containing two WW domains and an IQ motif, is required for scission of the residual cytoplasmic bridge during cytokinesis in Dictyostelium.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 16 citations in OpenAlex.
- A Proteomics Analysis of Calmodulin-Binding Proteins inInternational journal of molecular sciences · 2021Article
- Calmodulin and Calmodulin Binding Proteins inInternational journal of molecular sciences · 2020Review
- Separation anxiety: stress, tension and cytokinesis.Experimental cell research · 2012Review
- Deconvolution of the cellular force-generating subsystems that govern cytokinesis furrow ingression.PLoS computational biology · 2012Article
- Dominant negative mutant actins identified in flightless Drosophila can be classified into three classes.The Journal of biological chemistry · 2010Article
- The association of CaM and Hsp70 regulates S-phase arrest and apoptosis in a spatially and temporally dependent manner in human cells.Cell stress & chaperones · 2009Article
- Balance of actively generated contractile and resistive forces controls cytokinesis dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The stress and strain of cytokinesis.Trends in cell biology · 2005Review
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
We have identified a novel gene, dwwA, which is required for cytokinesis of Dictyostelium cells on solid surfaces. Its product, Dd WW domain containing protein A (DWWA), contains several motifs, including two WW domains, an IQ motif, a C2 domain, and a proline-rich region. On substrates, cells lacking dwwA were multinucleated and larger and flatter than wild-type cells due to their frequent inability to sever the cytoplasmic bridge connecting daughter cells after mitosis. When cultured in suspension, however, dwwA-null cells seemed to carry out cytokinesis normally via a process not driven by the shearing force arising from agitation of the culture. GFP-DWWA localized to the cell cortex and nucleus; analysis of the distributions of various truncation mutants revealed that the N-terminal half of the protein, which contains the C2 domain, is required for the cortical localization of DWWA. The IQ motif of DWWA binds calmodulin in vitro. Given that the scission process is also defective in calmodulin knockdown cells cultured on substrates (Liu et al., 1992), we propose that DWWA's multiple binding domains enable it to function as an adaptor protein, facilitating the scission process through the regulation of Ca(2+)/calmodulin-mediated remodeling of the actin cytoskeleton and/or modulation of membrane dynamics.
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