Mechanism of Actin-Based Motility

Pantaloni, Dominique; Clainche, Christophe Le; Carlier, Marie-France

doi:10.1126/science.1059975

Cited by 631 publications

(499 citation statements)

References 66 publications

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“…CapZb decreases actin polymerization by blocking actin barbed ends, 28,29 and is increased specifically during abstinence. ARP3 and Coronin 1A, both of which increase actin filament assembly, 30,31 are decreased specifically during abstinence.…”

Section: Discussionmentioning

confidence: 99%

Distinct proteomic profiles of amphetamine self-administration transitional states

et al. 2005

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In the rat, continuous access to d-amphetamine (d-AMPH) leads to lengthy bouts of self-administration, voluntary abstinence, and relapse to selfadministration. Previous studies have revealed that the progression from psychostimulant self-administration to abstinence to relapse is mediated in part by the ventral hippocampus. Stimulation of the ventral subiculum (vSub) during voluntary abstinence from d-AMPH self-administration reinstates self-administration and increases nucleus accumbens (NAc) dopamine efflux. Quantitative proteomic examination of the hippocampus from rats naïve to amphetamine, during a self-administration session 'Binge', during voluntarily abstinence 'Abstinent', and after reinstatement of selfadministration 'Relapse', revealed a differential proteomic state during abstinence. Actin-and cytoskeletal-related proteins were over-represented in the changes occurring during abstinence and suggest a decrease in actin filament polymerization. These changes may underlie alterations in neuronal tone during abstinence that could affect both neurotransmission and behavior. These data provide the first classification of addiction-related behaviors based on clustering of quantitative proteomic measurements.

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Section: Discussionmentioning

confidence: 99%

Distinct proteomic profiles of amphetamine self-administration transitional states

et al. 2005

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“…4 Various molecular components of the cytoskeleton, cell adhesion, and signaling systems seem to be involved in the regulation of cell motility. [5][6][7][8] Actinin-1 is an isoform of non-muscular a-actinin preferentially localized on the inner surface of cells, being a component of focal adhesion plaques and cell-to-cell adherence junctions. Actinin-4, another isoform of non-muscular a-actinin, was recently identified as an actin-bundling protein.…”

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confidence: 99%

Actinin-4 expression in ovarian cancer: a novel prognostic indicator independent of clinical stage and histological type

Yamamoto

Tsuda

Honda³

et al. 2007

Modern Pathology

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Actinin-4 is an isoform of non-muscular a-actinin and actin-bundling protein. By enhancing cell motility, actinin-4 shows different biological properties from another isoform of non-muscular actinin 'actinin-1' and variable clinicopathological implications of actinin-4 have been demonstrated in some human malignancies such as breast cancers, lung cancers, and colorectal cancers. We herein described the clinicopathological and prognostic significance of actinin-4 expression in ovarian cancers. Actinin-4 expression was analyzed immunohistochemically in 265 primary ovarian carcinomas: 116 serous, 71 clear cell, 43 endometrioid, and 35 mucinous adenocarcinomas. With reference to endothelial immunoreactivity, cytoplasmic expression of actinin-4 was classified as either low (including negative) or high. Then, various parameters such as patients' characteristics, histopathological findings including E-cadherin and b-catenin immunoreactivity, and clinical outcome, were compared between groups showing differences in the intensity or intracellular distribution of actinin-4 immunoreactivity. High expression of actinin-4 was demonstrated in 137 (57%) cases and was associated with serous histology (P ¼ 0.0075), high histological grade (Po0.0001), an advanced disease stage (P ¼ 0.036), a high degree of residual disease after initial surgery (P ¼ 0.0047), poor patient outcome (5-year survival: 52.4% in the high-expression group vs 71.9% in the low expression group, P ¼ 0.0043 by log-rank test), and also with reduced E-cadherin and preserved b-catenin expressions (P ¼ 0.0097 and 0.017, respectively). Nuclear immunoreactivity for actinin-4 was detected in 20 (7.5%) cases and was associated with low histological grade (P ¼ 0.0079) but not with other variables. Multivariate analysis showed that high actinin-4 expression was an independent prognostic factor for overall survival, as well as a high degree of residual disease and clear-cell histology. Accumulation of actinin-4 in the cytoplasm may be related to a higher propensity for tumor invasiveness and metastasis, probably by enhancing cell motility, and could be a novel prognostic indicator for patients with ovarian carcinomas.

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“…Such movement occurs in response to external guidance cues by means of growth cones; vectorial progress is not uniform but consists of periods of outgrowth, stasis and retraction-elaboration and disassembly of adhesive contacts being important to each phase. At the leading edge of the growth cone is a broad, relatively thin, veil-like lamellipodium, actin polymerisa-tion pushing the plasma membrane forwards (Pantaloni et al 2001;Pollard and Borisy 2003); actin filaments, thus formed, are translocated rearwards, initiating a phenomenon known as retrograde actin flow. The forces required to move the bulk of the growth cone forwards are much greater than can be achieved through actin polymerisation alone, hence a requirement for myosin 2 molecular motors, which act vectorially and power forward outgrowth (Wylie et al 1998;Bridgman et al 2001) and rearward retraction (Amano et al 1998;Wylie and Chantler 2003), as well as retrograde actin flow (Lin et al 1996;Cai et al 2006;Medeiros et al 2006).…”

Section: Neurite Outgrowth and Axonal Guidancementioning

confidence: 99%

Conventional myosins – unconventional functions

et al. 2010

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While the discovery of unconventional myosins raised expectations that their actions were responsible for most aspects of actin-based cell motility, few anticipated the wide range of cellular functions that would remain the purview of conventional two-headed myosins. The three nonsarcomeric, cellular myosins-M2A, M2B and M2C-participate in diverse roles including, but not limited to: neuronal dynamics, axon guidance and synaptic transmission; endothelial cell migration; cell adhesion, polarity, fusion and cytokinesis; vesicle trafficking and viral egress. These three conventional myosins each take on specific, differing functional roles during development and maturity, characteristic of each cell lineage; exact roles depend on the developmental stage of the cell, cellular location, upstream regulatory controls, relative isoform expression, orientation and associated state of the actin cytoscaffolds in which these myosins operate. Here, we discuss the separate yet related roles that characterise the actions of M2A, M2B and M2C in various cell types and show that these conventional myosins are responsible for functions as unconventional as any performed by unconventional myosins.

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Mechanism of Actin-Based Motility

Cited by 631 publications

References 66 publications

Distinct proteomic profiles of amphetamine self-administration transitional states

Distinct proteomic profiles of amphetamine self-administration transitional states

Actinin-4 expression in ovarian cancer: a novel prognostic indicator independent of clinical stage and histological type

Conventional myosins – unconventional functions

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