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Bacterial cell division is mediated by the divisome which is organized by the Z ring, a cytoskeletal element formed by the polymerization of the tubulin homologue FtsZ. Despite billions of years of bacterial evolution, the Z ring is nearly universal among bacteria that have a cell wall and divide by binary fission. Recent studies have revealed the mechanism of cooperative assembly of FtsZ and that the Z ring consists of patches of FtsZ filaments tethered to the membrane that treadmill to distribute the septal biosynthetic machinery. Here, we summarize these advances and discuss questions raised by these new findings.

Spatiotemporal regulation of septal PG synthesis is achieved by coupling assembly and activation of the synthetic enzymes (FtsWI) to the Z ring, a cytoskeletal element required for division in most bacteria. In E. coli the recruitment of the FtsWI complex is dependent upon the cytoplasmic domain of FtsL, a component of the conserved FtsQLB complex. Once assembled, FtsWI is activated by the arrival of FtsN, which acts through FtsQLB and FtsA that are also essential for their recruitment. However, the mechanism of activation of FtsWI by FtsN is not clear. Here, we identify a region of FtsL that plays a key role in the activation of FtsWI which we designate AWI (Activation of FtsWI) and present evidence that FtsL acts through FtsI. Our results suggest that FtsN switches FtsQLB from a recruitment complex to an activator with FtsL interacting with FtsI to activate FtsW. Since FtsQLB and FtsWI are widely conserved in bacteria this mechanism is likely to be also widely conserved.SignificanceA critical step in bacterial cytokinesis is the activation of septal peptidoglycan synthesis at the Z ring. Although FtsN is the trigger and acts through FtsQLB and FtsA to activate FtsWI the mechanism is unclear. Here we find an essential role for FtsL in activating septal PG synthesis and find that it acts on FtsI. Our results suggest a model where FtsWI is recruited in an inactive form by FtsQLB and upon FtsN arrival, FtsQLB undergoes a conformational change so that a region of FtsL, that we designate the AWI domain, becomes available to interact with FtsI and activate the FtsWI complex. This mechanism for activation of the divisome has similarities to activation of the elongasome and is likely to be widely conserved in bacteria.

Septins are a family of eukaryotic GTP-binding proteins that associate into linear rods, which, in turn, polymerize end-on-end into filaments, and further assemble into other, more elaborate super-structures at discrete subcellular locations. Hence, septin-based ensembles are considered elements of the cytoskeleton. One function of these structures that has been well-documented in studies conducted in budding yeast Saccharomyces cerevisiae is to serve as a scaffold that recruits regulatory proteins, which dictate the spatial and temporal control of certain aspects of the cell division cycle. In particular, septin-associated protein kinases couple cell cycle progression with cellular morphogenesis. Thus, septin-containing structures serve as signaling platforms that integrate a multitude of signals and coordinate key downstream networks required for cell cycle passage. This review summarizes what we currently understand about how the action of septin-associated protein kinases and their substrates control information flow to drive the cell cycle into and out of mitosis, to regulate bud growth, and especially to direct timely and efficient execution of cytokinesis and cell abscission. Thus, septin structures represent a regulatory node at the intersection of many signaling pathways. In addition, and importantly, the activities of certain septin-associated protein kinases also regulate the state of organization of the septins themselves, creating a complex feedback loop.

The aim of this paper is to investigate, by means of a numerical simulation, the effect of the half-life of cytoskeletal elements (CEs) on superposition of several waves representing concentrations of running, pausing, and off-track anterograde and retrograde CE populations. The waves can be induced by simultaneous microinjections of radiolabeled CEs in different locations in the vicinity of a neuron body; alternatively, the waves can be induced by microinjecting CEs at the same location several times, with a time interval between the injections. Since the waves spread out as they propagate downstream, unless their amplitude decreases too fast, they eventually superimpose. As a result of superposition and merging of several waves, for the case with a large half-life of CEs, a single wave is formed. For the case with a small half-life the waves vanish before they have enough time to merge.

Intermediate filaments represent the most abundant cytoskeletal element in mature neurons. Mutations and/or accumulations of neuronal intermediate filament proteins are frequently observed in several human neurodegenerative disorders. Although it is now admitted that disorganization of the neurofilament network may be directly involved in neurodegeneration, certain type of perikaryal intermediate filament aggregates confer protection in motor neuron disease. The use of various mouse models provided a better knowledge of the role played by the disorganization of intermediate filaments in the pathogenesis of neurodegenerative disorders, but the mechanisms leading to the formation of these aggregates remain elusive. Here, we will review some neurodegenerative diseases involving intermediate filaments abnormalities and possible mechanisms susceptible to provoke them.

Septins are a family of eukaryotic GTP-binding proteins that associate into linear rods, which, in turn, polymerize end-on-end into filaments, and further assemble into other, more elaborate super-structures at discrete subcellular locations. Hence, septin-based ensembles are considered elements of the cytoskeleton. One function of these structures that has been well-documented in studies conducted in budding yeast Saccharomyces cerevisiae is to serve as a scaffold that recruits regulatory proteins, which dictate the spatial and temporal control of certain aspects of the cell division cycle. In particular, septin-associated protein kinases couple cell cycle progression with cellular morphogenesis. Thus, septin-containing structures serve as signaling platforms that integrate a multitude of signals and coordinate key downstream networks required for cell cycle passage. This review summarizes what we currently understand about how the action of septin-associated protein kinases and their substrates control information flow to drive the cell cycle into and out of mitosis, to regulate bud growth, and especially to direct timely and efficient execution of cytokinesis and cell abscission. Thus, septin structures represent a regulatory node at the intersection of many signaling pathways. In addition, and importantly, the activities of certain septin-associated protein kinases also regulate the state of organization of the septins themselves, creating a complex feedback loop.

The large heliozoan Echinosphaerium extends a number of needle-like axopodia by which it captures food organisms. Every axopodium contains a bundle of several hundreds of axonemal microtubules as a cytoskeletal element. When the tip of a poly-L-lysine-coated glass micro-needle came into contact with the distal part of an axopodium, a rapid axopodial contraction (2.6 mm/s) occurred with a concomitant bending of the needle toward the cell body. In this report, we measured the force of the axopodial contraction by utilizing the relation between force and bending displacement of the micro-needle, and examined a possibility that the axopodial contraction is ascribed to the axopodial tension (surface tension and/or cytoplasmic elasticity) that is developed as a result of microtubule degradation. The force of the axopodial contraction was estimated in the order of 10(-9) N. Treatment with 10 mM colchicine induced disassembly of the axopodial microtubules and a resulting slow retraction of the axopodia (0.1 μm/s) occurred. The force of the slow retraction was also measured by the same procedure to estimate the axopodial tension, and was in the order of 10(-11) N. It was thus demonstrated that the motive force for axopodial contraction cannot be explained as an axopodial tension generated as a result of disassembly of the microtubules.

Oscillation of the Min proteins is a key regulator of the division plane in many bacteria including the model organism E. coli. The coupled oscillation of these proteins between the ends of the cell restricts the formation of the Zring, an essential cytoskeletal element that serves as a scaffold for the cytokinesis machinery, to a narrow region at midcell. The oscillation was discovered following the fusion of the Min proteins to green fluorescent protein. Importantly, the Min system is readily manipulated allowing rapid advances in understanding key aspects of the oscillation. In addition, details of the biochemistry of the Min proteins have pmerged that provide the basis for their dynamic interaction with the membrane. Furthermore, the in vivo description of the oscillations along with the biochemical details of the Min proteins have provided the fuel for mathematical approaches to try and understand the critical features have underlie this oscillatory system. The simplicity and ease of manipulating the Min system make it a tractable model to obtain a complete understanding of a self-organizing system.

Recent application of fluorescence microscopy to the study of the bacterial cell cycle has revealed the existence of a cytoskeletal element – once thought to occur only in eukaryotic cells – that mediates cytokinesis, and possibly another involved in chromosome segregation.

Specification of one neurite as the axon is the first milestone achieved as neuronal polarity is established. It is clear that regional changes in the cytoskeleton underlie axonal differentiation, but is one cytoskeletal element any more crucial than the others? Although early studies implicated microtubules, more recent studies have focused on the actin cytoskeleton as the potential hub for factors that influence axonal differentiation. Now, studies on a novel protein called CRMP-2 have shifted attention back to microtubules.

Background Microtubules, microfilaments, and neurofilaments are cytoskeletal elements that affect cell morphology, cellular processes, and mechanical structures in neural cells. The objective of the current study was to investigate the contribution of each type of cytoskeletal element to the mechanical properties of axons of dorsal root and sympathetic ganglia cells in chick embryos. Results Microtubules, microfilaments, and neurofilaments in axons were disrupted by nocodazole, cytochalasin D, and acrylamide, respectively, or a combination of the three. An atomic force microscope (AFM) was then used to compress the treated axons, and the resulting corresponding force-deformation information was analyzed to estimate the mechanical properties of axons that were partially or fully disrupted. Conclusion We have found that the mechanical stiffness was most reduced in microtubules-disrupted-axons, followed by neurofilaments-disrupted- and microfilaments-disrupted-axons. This suggests that microtubules contribute the most of the mechanical stiffness to axons.