scholarly journals Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella

2008 ◽  
Vol 180 (6) ◽  
pp. 1233-1244 ◽  
Author(s):  
Maria Nemethova ◽  
Sonja Auinger ◽  
J. Victor Small
Keyword(s):  
Electron Microscopy ◽  
Cell Migration ◽  
Actin Cytoskeleton ◽  
Myosin Ii ◽  
Light And Electron Microscopy ◽  
Proximal Part ◽  
Stress Fiber ◽  
B16 Melanoma ◽  
Cell Edge ◽  
Fiber Assembly

Filopodia are rodlike extensions generally attributed with a guidance role in cell migration. We now show in fish fibroblasts that filopodia play a major role in generating contractile bundles in the lamella region behind the migrating front. Filopodia that developed adhesion to the substrate via paxillin containing focal complexes contributed their proximal part to stress fiber assembly, and filopodia that folded laterally contributed to the construction of contractile bundles parallel to the cell edge. Correlated light and electron microscopy of cells labeled for actin and fascin confirmed integration of filopodia bundles into the lamella network. Inhibition of myosin II did not subdue the waving and folding motions of filopodia or their entry into the lamella, but filopodia were not then integrated into contractile arrays. Comparable results were obtained with B16 melanoma cells. These and other findings support the idea that filaments generated in filopodia and lamellipodia for protrusion are recycled for seeding actomyosin arrays for use in retraction.

scholarly journals Molecular Architecture of Synaptic Actin Cytoskeleton in Hippocampal Neurons Reveals a Mechanism of Dendritic Spine Morphogenesis

2010 ◽  
Vol 21 (1) ◽  
pp. 165-176 ◽  
Author(s):  
Farida Korobova ◽  
Tatyana Svitkina
Keyword(s):  
Electron Microscopy ◽  
Actin Cytoskeleton ◽  
Actin Filament ◽  
Dendritic Spines ◽  
Dendritic Spine ◽  
Myosin Ii ◽  
Capping Protein ◽  
Dominant Feature ◽  
Presynaptic Boutons ◽  
Spine Morphogenesis

Excitatory synapses in the brain play key roles in learning and memory. The formation and functions of postsynaptic mushroom-shaped structures, dendritic spines, and possibly of presynaptic terminals, rely on actin cytoskeleton remodeling. However, the cytoskeletal architecture of synapses remains unknown hindering the understanding of synapse morphogenesis. Using platinum replica electron microscopy, we characterized the cytoskeletal organization and molecular composition of dendritic spines, their precursors, dendritic filopodia, and presynaptic boutons. A branched actin filament network containing Arp2/3 complex and capping protein was a dominant feature of spine heads and presynaptic boutons. Surprisingly, the spine necks and bases, as well as dendritic filopodia, also contained a network, rather than a bundle, of branched and linear actin filaments that was immunopositive for Arp2/3 complex, capping protein, and myosin II, but not fascin. Thus, a tight actin filament bundle is not necessary for structural support of elongated filopodia-like protrusions. Dynamically, dendritic filopodia emerged from densities in the dendritic shaft, which by electron microscopy contained branched actin network associated with dendritic microtubules. We propose that dendritic spine morphogenesis begins from an actin patch elongating into a dendritic filopodium, which tip subsequently expands via Arp2/3 complex-dependent nucleation and which length is modulated by myosin II-dependent contractility.

scholarly journals Tension is required but not sufficient for focal adhesion maturation without a stress fiber template

2012 ◽  
Vol 196 (3) ◽  
pp. 363-374 ◽  
Author(s):  
Patrick W. Oakes ◽  
Yvonne Beckham ◽  
Jonathan Stricker ◽  
Margaret L. Gardel
Keyword(s):  
Focal Adhesion ◽  
Myosin Ii ◽  
Focal Adhesions ◽  
Stress Fiber ◽  
Matrix Remodeling ◽  
Force Transmission ◽  
Fiber Assembly ◽  
Wide Range ◽  
Structural Template

Focal adhesion composition and size are modulated in a myosin II–dependent maturation process that controls adhesion, migration, and matrix remodeling. As myosin II activity drives stress fiber assembly and enhanced tension at adhesions simultaneously, the extent to which adhesion maturation is driven by tension or altered actin architecture is unknown. We show that perturbations to formin and α-actinin 1 activity selectively inhibited stress fiber assembly at adhesions but retained a contractile lamella that generated large tension on adhesions. Despite relatively unperturbed adhesion dynamics and force transmission, impaired stress fiber assembly impeded focal adhesion compositional maturation and fibronectin remodeling. Finally, we show that compositional maturation of focal adhesions could occur even when myosin II–dependent cellular tension was reduced by 80%. We propose that stress fiber assembly at the adhesion site serves as a structural template that facilitates adhesion maturation over a wide range of tensions. This work identifies the essential role of lamellar actin architecture in adhesion maturation.

scholarly journals LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell migration

2017 ◽  
Vol 28 (8) ◽  
pp. 1054-1065 ◽  
Author(s):  
Yu-Hung Lin ◽  
Yen-Yi Zhen ◽  
Kun-Yi Chien ◽  
I-Ching Lee ◽  
Wei-Chi Lin ◽  
...  
Keyword(s):  
Cell Migration ◽  
Hela Cells ◽  
Myosin Ii ◽  
Focal Adhesions ◽  
Stress Fiber ◽  
Stress Fibers ◽  
Actin Stress Fiber ◽  
Nonmuscle Myosin ◽  
Head Region ◽  
Nonmuscle Myosin Ii

Nonmuscle myosin II (NM-II) is an important motor protein involved in cell migration. Incorporation of NM-II into actin stress fiber provides a traction force to promote actin retrograde flow and focal adhesion assembly. However, the components involved in regulation of NM-II activity are not well understood. Here we identified a novel actin stress fiber–associated protein, LIM and calponin-homology domains 1 (LIMCH1), which regulates NM-II activity. The recruitment of LIMCH1 into contractile stress fibers revealed its localization complementary to actinin-1. LIMCH1 interacted with NM-IIA, but not NM-IIB, independent of the inhibition of myosin ATPase activity with blebbistatin. Moreover, the N-terminus of LIMCH1 binds to the head region of NM-IIA. Depletion of LIMCH1 attenuated myosin regulatory light chain (MRLC) diphosphorylation in HeLa cells, which was restored by reexpression of small interfering RNA–resistant LIMCH1. In addition, LIMCH1-depleted HeLa cells exhibited a decrease in the number of actin stress fibers and focal adhesions, leading to enhanced cell migration. Collectively, our data suggest that LIMCH1 plays a positive role in regulation of NM-II activity through effects on MRLC during cell migration.

Cell migration from the chick olfactory placode: a light and electron microscopic study

Development ◽  
1982 ◽  
Vol 69 (1) ◽  
pp. 47-59
Author(s):  
A. S. Mendoza ◽  
W. Breipohl ◽  
F. Miragall
Keyword(s):  
Electron Microscopy ◽  
Cell Migration ◽  
Light And Electron Microscopy ◽  
Olfactory Mucosa ◽  
Electron Microscopic ◽  
Olfactory Placode ◽  
The Third ◽  
Epitheloid Cells ◽  
Migration Of Cells ◽  
Number Of Cells

The diflferentiation of the olfactory placode in the chick has been studied using light and electron microscopy. Special attention was paid to the appearance of neuronal cells within the placodal ectodermal thickening, the migration of cells out of this tissue and the appearance of the first fila olfactoria in the differentiating olfactory mucosa. Between the third and fifth day of incubation a large number of cells is observed leaving the base of the invaginating olfactory placode, often in contact with thin axon bundles. These cells are characterized by a well-developed Golgi apparatus, a considerable number of mitochondria and dense-core vesicles. The morphology of these migrating cells resembles that of cells observed near the basement membrane within the developing olfactory epithelium and is clearly different from the mesenchymal cells which are filled with polyribosomes. At the sixth day of incubation thick axon bundles can be observed within the epithelium and the underlying lamina propria. The possible fate of the migrated epitheloid cells is discussed.

scholarly journals Leaf anatomy of Cordiera sessilis (Vell.) Kuntze (RUBIACEAE)

2016 ◽  
Vol 38 (3) ◽  
pp. 355
Author(s):  
Thaiz Rodrigues Teixeira ◽  
Marlúcia Souza Pádua ◽  
Ana Hortência Fonsêca Castro
Keyword(s):  
Electron Microscopy ◽  
Leaf Anatomy ◽  
Distal Part ◽  
Leaf Surface ◽  
Vascular System ◽  
Species Recognition ◽  
Light And Electron Microscopy ◽  
Proximal Part ◽  
Brazilian Cerrado ◽  
Crystal Sand

A study on the leaf anatomy of Cordiera sessilis (Rubiaceae), a native medicinal shrub from Brazilian Cerrado was carried out to identify features that may be useful in species recognition. Leaves were collected, fixed and processed by usual techniques, and studied by light and electron microscopy. Quantitative analyzes of stomata and trichomes were performed. In addition to the typical anatomical characteristics of Rubiaceae leaves, two types of vascular patterns were identified in the petiole: in distal part, the vascular system is arranged cylindrically surrounded by sclerenchyma sheath and in proximal part the vascular system is arranged in U-shape coupled to sclerified cells. The micromorphological organization of leaf surface, epicuticular wax types, the petiole pattern and histochemical characteristics as the presence of druses, crystal sand and alkaloids and absence of raphides in the mesophyll, midrib and petiole are considerate representative characteristics of C. sessilis and may be useful in the species recognition. 

scholarly journals Angiogenin Enhances Cell Migration by Regulating Stress Fiber Assembly and Focal Adhesion Dynamics

PLoS ONE ◽  
2011 ◽  
Vol 6 (12) ◽  
pp. e28797 ◽  
Author(s):  
Saisai Wei ◽  
Xiangwei Gao ◽  
Juan Du ◽  
Jinfeng Su ◽  
Zhengping Xu
Keyword(s):  
Cell Migration ◽  
Focal Adhesion ◽  
Stress Fiber ◽  
Fiber Assembly

scholarly journals Dynamic trafficking and turnover of Jam-C is essential for endothelial cell migration

2019 ◽  
Author(s):  
Katja B. Kostelnik ◽  
Amy Barker ◽  
Christopher Schultz ◽  
Vinothini Rajeeve ◽  
Ian J. White ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Cell Migration ◽  
Intracellular Trafficking ◽  
Light And Electron Microscopy ◽  
Endothelial Cell Migration ◽  
Leukocyte Trafficking ◽  
Lysosomal Degradation ◽  
Blood Constituents ◽  
Junctional Proteins ◽  
Junctional Complexes

AbstractJunctional complexes between endothelial cells form a dynamic barrier that hinder passive diffusion of blood constituents into interstitial tissues. Re-modelling of junctions is an essential process during leukocyte trafficking, vascular permeability and angiogenesis. However, for many junctional proteins the mechanisms of junctional remodelling have yet to be determined. Here we used receptor mutagenesis, HRP and APEX-2 proximity labelling, alongside light and electron microscopy, to map the intracellular trafficking routes of junctional adhesion molecule-C (Jam-C). We found that Jam-C co-traffics with receptors associated with changes in permeability, such as VE-Cadherin, NRP-1 and 2, but not with junctional proteins associated with the transmigration of leukocytes. Dynamic Jam-C trafficking and degradation is necessary for junctional remodelling during cell migration and angiogenesis. By identifying new trafficking machinery we show that a key point of regulation is the ubiquitylation of Jam-C by the E3 ligase CBL, this controls the rate of recycling versus lysosomal degradation.

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