ArticleBMC cell biology2000
Imaging of dynamic changes of the actin cytoskeleton in microextensions of live NIH3T3 cells with a GFP fusion of the F-actin binding domain of moesin.
Article in BMC cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
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- Punctuated actin contractions during convergent extension and their permissive regulation by the non-canonical Wnt-signaling pathway.Journal of cell science · 2011Article
- Actin interaction and regulation of cyclin-dependent kinase 5/p35 complex activity.Journal of neurochemistry · 2011Article
- Dephosphorylation-dependent inhibitory activity of juxtanodin on filamentous actin disassembly.The Journal of biological chemistry · 2010Article
- Macroscopic stiffening of embryonic tissues via microtubules, RhoGEF and the assembly of contractile bundles of actomyosin.Development (Cambridge, England) · 2010Article
- Experimental control of excitable embryonic tissues: three stimuli induce rapid epithelial contraction.Experimental cell research · 2010Article
- Article
- Morphogenetic movements driving neural tube closure in Xenopus require myosin IIB.Developmental biology · 2009Article
- Convergence and extension at gastrulation require a myosin IIB-dependent cortical actin network.Development (Cambridge, England) · 2008Article
- Ermin, a myelinating oligodendrocyte-specific protein that regulates cell morphology.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- GLUT1CBP(TIP2/GIPC1) interactions with GLUT1 and myosin VI: evidence supporting an adapter function for GLUT1CBP.Molecular biology of the cell · 2005Article
- A mesenchyme-free culture system to elucidate the mechanism of otic vesicle morphogenesis.Journal of anatomy · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe cell surface undergoes continuous change during cell movement. This is characterized by transient protrusion and partial or complete retraction of microspikes, filopodia, and lamellipodia. This requires a dynamic actin cytoskeleton, moesin, components of Rho-mediated signal pathways, rearrangement of membrane constituents and the formation of focal adhesion sites. While the immunofluorescence distribution of endogenous moesin is that of a membrane-bound molecule with marked enhancement in some but not all microextensions, the C-terminal fragment of moesin co-distributes with filamentous actin consistent with its actin-binding activity. By taking advantage of this property we studied the spontaneous protrusive activity of live NIH3T3 cells, expressing a fusion of GFP and the C-terminal domain of moesin.
resultsC-moesin-GFP localized to stress fibers and was enriched in actively protruding cellular regions such as filopodia or lamellipodia. This localization was reversibly affected by cytochalasin D. Multiple types of cytoskeletal rearrangements were observed that occurred independent of each other in adjacent regions of the cell surface. Assembly and disassembly of actin filaments occurred repeatedly within the same space and was correlated with either membrane protrusion and retraction, or no change in shape when microextensions were adherent.
conclusionsShape alone provided an inadequate criterion for distinguishing between retraction fibers and advancing, retracting or stable filopodia. Fluorescence imaging of C-moesin-GFP, however, paralleled the rapid and dynamic changes of the actin cytoskeleton in microextensions. Regional regulatory control is implicated because opposite changes occurred in close proximity and presumably independent of each other. This new and sensitive tool should be useful for investigating mechanisms of localized actin dynamics in the cell cortex.
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