Tropomyosins induce neuritogenesis and determine neurite branching patterns in B35 neuroblastoma cells

Curthoys, Nikki M.; Freittag, Hannah; Connor, Andrea R.; Desouza, Melissa; Brettle, Merryn; Poljak, Anne; Hall, Amelia Weber; Hardeman, Edna C.; Schevzov, Galina; Gunning, Peter W.; Fath, Thomas

doi:10.1016/j.mcn.2013.10.011

Cited by 30 publications

(39 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Loss-offunction mutations in the Tm2 (also known as TmII) gene in Drosophila leads to cell autonomous expansion of neuronal dendritic fields (Li and Gao, 2003). Elevated expression of a range of Tpm isoforms in B35 neuroblastoma cells results in a plethora of phenotypes in differentiated cells, which is consistent with an isoform-specific impact on morphogenesis (Curthoys et al, 2014). Tpm1.7 promotes the formation of filopodia in B35 cells (Creed et al, 2011), which is dependent on the availability of active cofilin.…”

Section: Morphogenesismentioning

confidence: 78%

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Gunning

Hardeman

Lappalainen

et al. 2015

Journal of Cell Science

225

228

View full text Add to dashboard Cite

Tropomyosin (Tpm) isoforms are the master regulators of the functions of individual actin filaments in fungi and metazoans. Tpms are coiled-coil parallel dimers that form a head-to-tail polymer along the length of actin filaments. Yeast only has two Tpm isoforms, whereas mammals have over 40. Each cytoskeletal actin filament contains a homopolymer of Tpm homodimers, resulting in a filament of uniform Tpm composition along its length. Evidence for this 'master regulator' role is based on four core sets of observation. First, spatially and functionally distinct actin filaments contain different Tpm isoforms, and recent data suggest that members of the formin family of actin filament nucleators can specify which Tpm isoform is added to the growing actin filament. Second, Tpms regulate wholeorganism physiology in terms of morphogenesis, cell proliferation, vesicle trafficking, biomechanics, glucose metabolism and organ size in an isoform-specific manner. Third, Tpms achieve these functional outputs by regulating the interaction of actin filaments with myosin motors and actin-binding proteins in an isoform-specific manner. Last, the assembly of complex structures, such as stress fibers and podosomes involves the collaboration of multiple types of actin filament specified by their Tpm composition. This allows the cell to specify actin filament function in time and space by simply specifying their Tpm isoform composition.

show abstract

Section: Morphogenesismentioning

confidence: 78%

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Gunning

Hardeman

Lappalainen

et al. 2015

Journal of Cell Science

225

228

View full text Add to dashboard Cite

show abstract

“…Tpms regulate actin branching by ARP2/3 (Blanchoin et al, 2001) in an isoform-specific manner (Brayford et al, 2016; Kis-Bicskei et al, 2013). They also have differential effects on the activity of the actin filament severing proteins, such as ADF/cofilin (Bryce et al, 2003; Curthoys et al, 2014; Gateva et al, 2017; Robaszkiewicz et al, 2016). The mechanical properties of actin filaments are influenced by the ability of Tpms to allow or block the access of the actin motor protein myosin II (Bryce et al, 2003).…”

Section: Tropomodulins and Tropomyosins Regulate Actin Independently mentioning

confidence: 99%

“…Importantly, recent data highlight the complexity by which Tpm isoforms regulate actin dynamics in cells as compared to in vitro reconstituted systems (Gateva et al, 2017; Ostrowska et al, 2017). Cells overexpression of Tpm3.1 (Bryce et al, 2003) and Tpm4.2 (Curthoys et al, 2014) show increased inactivation of cofilin as indicated by an increase in phosphorylated cofilin over total cofilin levels. In contrast, Tpm3.1, Tpm3.2 (showing close homology to Tpm3.1) and Tpm4.2 did not inhibit severing of in vitro assembled actin filaments by cofilin (Gateva et al, 2017; Ostrowska et al, 2017).…”

Section: Tropomodulins and Tropomyosins Regulate Actin Independently mentioning

confidence: 99%

See 1 more Smart Citation

Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function

Gray

Kostyukova

Fath

2017

Molecular and Cellular Neuroscience

Self Cite

View full text Add to dashboard Cite

Actin is a profoundly influential protein; it impacts, among other processes, membrane morphology, cellular motility, and vesicle transport. Actin can polymerize into long filaments that push on membranes and provide support for intracellular transport. Actin filaments have polar ends: the fast-growing (barbed) end and the slow-growing (pointed) end. Depolymerization from the pointed end supplies monomers for further polymerization at the barbed end. Tropomodulins (Tmods) cap pointed ends by binding onto actin and tropomyosins (Tpms). Tmods and Tpms have been shown to regulate many cellular processes; however, very few studies have investigated their joint role in the nervous system. Recent data directly indicate that they can modulate neuronal morphology. Additional studies suggest that Tmod and Tpm impact molecular processes influential in synaptic signaling. To facilitate future research regarding their joint role in actin regulation in the nervous system, we will comprehensively discuss Tpm and Tmod and their known functions within molecular systems that influence neuronal development.

show abstract

“…Contiguous phase-contrast digital images of the entire well at 20× and 40× objective were acquired using a Olympus CKX41 microscope mounted with Q Imaging 3.3 RTV camera and Olympus CellSens software version 1.8 (Olympus, VIC, Australia). The neurite lengths of randomly selected neurons in each well were then assessed by an independent observer using computer-assisted imaging (NIH-ImageJ2 software) as described previously (Curthoys et al, 2014). Neurite lengths of 30 neurons per treatment per experiment were measured for mouse neurons (n=7), and lengths of 20 neurons per condition in duplicates were measured for human neurons (n=4).…”

Section: Assessment Of Neurite Outgrowth In Cortical Neuronsmentioning

confidence: 99%

Soluble LILRA3 promotes neurite outgrowth and synapses formation through a high-affinity interaction with Nogo 66

Brettle

Lee

et al. 2016

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

Inhibitory proteins, particularly Nogo 66, a highly conserved 66-amino-acid loop of Nogo A (an isoform of RTN4), play key roles in limiting the intrinsic capacity of the central nervous system (CNS) to regenerate after injury. Ligation of surface Nogo receptors (NgRs) and/or leukocyte immunoglobulin-like receptor B2 (LILRB2) and its mouse orthologue the paired immunoglobulin-like receptor B (PIRB) by Nogo 66 transduces inhibitory signals that potently inhibit neurite outgrowth. Here, we show that soluble leukocyte immunoglobulin-like receptor A3 (LILRA3) is a high-affinity receptor for Nogo 66, suggesting that LILRA3 might be a competitive antagonist to these cell surface inhibitory receptors. Consistent with this, LILRA3 significantly reversed Nogo-66-mediated inhibition of neurite outgrowth and promoted synapse formation in primary cortical neurons through regulation of the ERK/MEK pathway. LILRA3 represents a new antagonist to Nogo-66-mediated inhibition of neurite outgrowth in the CNS, a function distinct from its immuneregulatory role in leukocytes. This report is also the first to demonstrate that a member of LILR family normally not expressed in rodents exerts functions on mouse neurons through the highly homologous Nogo 66 ligand.

show abstract

Tropomyosins induce neuritogenesis and determine neurite branching patterns in B35 neuroblastoma cells

Cited by 30 publications

References 63 publications

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function

Soluble LILRA3 promotes neurite outgrowth and synapses formation through a high-affinity interaction with Nogo 66

Contact Info

Product

Resources

About