Two Forms of Neuronal Actin

Choo, Q. L.; Bray, Dennis

doi:10.1111/j.1471-4159.1978.tb12451.x

Cited by 31 publications

(19 citation statements)

References 17 publications

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“…Although β-actin is believed to comprise one-half to two-thirds of the cytoplasmic actin in the mammalian brain [24], [25], we showed that total actin levels are maintained during development in CNS- Actb KO embryos due to an upregulation of γ- and α sm -actin. However, CNS- Actb KO mice presented with significant perinatal lethality, with only 32% surviving to adulthood.…”

Section: Discussionmentioning

confidence: 60%

Restricted Morphological and Behavioral Abnormalities following Ablation of β-Actin in the Brain

Cheever¹,

Li²,

Ervasti

2012

PLoS ONE

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The local translation of β-actin is one mechanism proposed to regulate spatially-restricted actin polymerization crucial for nearly all aspects of neuronal development and function. However, the physiological significance of localized β-actin translation in neurons has not yet been demonstrated in vivo. To investigate the role of β-actin in the mammalian central nervous system (CNS), we characterized brain structure and function in a CNS-specific β-actin knock-out mouse (CNS-ActbKO). β-actin was rapidly ablated in the embryonic mouse brain, but total actin levels were maintained through upregulation of other actin isoforms during development. CNS-ActbKO mice exhibited partial perinatal lethality while survivors presented with surprisingly restricted histological abnormalities localized to the hippocampus and cerebellum. These tissue morphology defects correlated with profound hyperactivity as well as cognitive and maternal behavior impairments. Finally, we also identified localized defects in axonal crossing of the corpus callosum in CNS-ActbKO mice. These restricted defects occurred despite the fact that primary neurons lacking β-actin in culture were morphologically normal. Altogether, we identified novel roles for β-actin in promoting complex CNS tissue architecture while also demonstrating that distinct functions for the ubiquitously expressed β-actin are surprisingly restricted in vivo.

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Section: Discussionmentioning

confidence: 60%

Restricted Morphological and Behavioral Abnormalities following Ablation of β-Actin in the Brain

Cheever¹,

Li²,

Ervasti

2012

PLoS ONE

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“…α-Actin isoforms are notable for their muscle-specific expression and constituting the thin filaments of the sarcomere, the functional unit of muscle cells. The cytoplasmic βand γactin are highly expressed in brain at roughly equal levels [38][39][40] and therefore of more interest for neuritogenesis. Although over 98% homologous and having nearly similar biochemical activities, β-, and γactin show distinct mRNA and protein localizations and have distinct transcriptional and post-translational modifications that may be of importance to actin dynamics in the neuron.…”

Section: Building a Growth Cone-actinmentioning

confidence: 99%

The cytoskeleton and neurite initiation

Flynn

2013

BioArchitecture

121

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Neurons begin their life as simple spheres, but can ultimately assume an elaborate morphology with numerous, highly arborized dendrites, and long axons. This is achieved via an astounding developmental progression which is dependent upon regulated assembly and dynamics of the cellular cytoskeleton. As neurites emerge out of the soma, neurons break their spherical symmetry and begin to acquire the morphological features that define their structure and function. Neurons regulate their cytoskeleton to achieve changes in cell shape, velocity, and direction as they migrate, extend neurites, and polarize. Of particular importance, the organization and dynamics of actin and microtubules directs the migration and morphogenesis of neurons. This review focuses on the regulation of intrinsic properties of the actin and microtubule cytoskeletons and how specific cytoskeletal structures and dynamics are associated with the earliest phase of neuronal morphogenesis—neuritogenesis.

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“…When cultured under conditions described previously (Choo and Bray, 1978), such cells form an extensive network of neurites in a few days. Radioactive labelling was carried out in medium containing a reduced level of leucine (0.1 mM), and supplemented with [3H]leucine at 1 mCi per 5 ml of medium.…”

Section: Tissue Culture Of Neuronesmentioning

confidence: 99%

Isolation of a Ca²⁺‐Dependent Actin‐Fragmenting Protein from Brain, Spinal Cord, and Cultured Neurones

Petrucci

Thomas

Bray

1983

Journal of Neurochemistry

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Extracts of ox spinal cord and chicken brain were fractionated by ion-exchange chromatography and assayed for their ability to reduce the viscosity of muscle F-actin solutions. Two distinct peaks of activity were obtained, one of which was further purified by affinity chromatography on a DNAase-actin Sepharose column. Following molecular exclusion chromatography, the actin component appeared as a complex of 1 molecule of a protein with molecular weight 90,000 and 2 molecules of actin (42,000). This tightly bound complex was resistant to most methods of protein separation, but was resolvable into its component proteins by sodium dodecyl sulphate acrylamide gel electrophoresis. The protein of molecular weight 90,000 could be eluted from such a gel in a fully active form. The activity of the protein from ox spinal cord was closely similar to that of gelsolin, an actin-fragmenting protein originally isolated from rabbit lung macrophages. Like gelsolin, the protein from ox spinal cord produced fragmentation of muscle F-actin filaments at Ca2+ concentrations greater than 10(-7) M, and had a nucleating effect on the polymerisation of muscle actin; the latter was measured most easily by the enhancement of fluorescence of muscle actin conjugated to N-(1-pyrenyl)iodoacetamide. Nucleation was more effective in the presence of Ca2+, but also occurred in its absence, and the same was true of complex formation between the 90,000 protein and muscle G-actin. On the basis of its actin-fragmenting activity, we estimate that the 90,000 molecular weight protein constitutes 0.2% of the protein initially extracted from ox spinal cord. A very similar protein, indistinguishable in its action on actin but containing variable amounts of a protein of molecular weight 85,000 as well as 90,000, was isolated from chicken brain. A similar protein was also detected in pure cultures of sympathetic neurones by enrichment on a DNAase-actin affinity column and by immune blotting and by immunofluorescence. We conclude that a protein similar, if not identical to macrophage gelsolin is present in neurones and that it probably plays a part in the actin-based movements of these cells.

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Two Forms of Neuronal Actin

Cited by 31 publications

References 17 publications

Restricted Morphological and Behavioral Abnormalities following Ablation of β-Actin in the Brain

Restricted Morphological and Behavioral Abnormalities following Ablation of β-Actin in the Brain

The cytoskeleton and neurite initiation

Isolation of a Ca²⁺‐Dependent Actin‐Fragmenting Protein from Brain, Spinal Cord, and Cultured Neurones

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Two Forms of Neuronal Actin

Cited by 31 publications

References 17 publications

Restricted Morphological and Behavioral Abnormalities following Ablation of β-Actin in the Brain

Restricted Morphological and Behavioral Abnormalities following Ablation of β-Actin in the Brain

The cytoskeleton and neurite initiation

Isolation of a Ca2+‐Dependent Actin‐Fragmenting Protein from Brain, Spinal Cord, and Cultured Neurones

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Isolation of a Ca²⁺‐Dependent Actin‐Fragmenting Protein from Brain, Spinal Cord, and Cultured Neurones