▪ Continuum Models of Mesenchymal Cell Migration and Sprouting Angiogenesis

2010 ◽  
pp. 238-261 ◽  
Keyword(s):  
Cell Migration ◽  
Mesenchymal Cell ◽  
Continuum Models ◽  
Sprouting Angiogenesis

Mechanics and Mechanisms of 3D Mesenchymal Cell Migration

2020 ◽  
Author(s):  
Andrew D. Doyle ◽  
Daniel J. Sykora ◽  
Gustavo G. Pacheco ◽  
Matthew L. Kutys ◽  
Kenneth M. Yamada
Keyword(s):  
Cell Migration ◽  
Mesenchymal Cell

scholarly journals Rudhira/BCAS3 couples microtubules and intermediate filaments to promote cell migration for angiogenic remodeling

2019 ◽  
Vol 30 (12) ◽  
pp. 1437-1450 ◽  
Author(s):  
Divyesh Joshi ◽  
Maneesha S. Inamdar
Keyword(s):  
Cell Migration ◽  
Intermediate Filaments ◽  
Cross Talk ◽  
Control Cell ◽  
The Novel ◽  
Mouse Development ◽  
Cytoskeleton Organization ◽  
Sprouting Angiogenesis ◽  
Promote Cell Migration ◽  
Necessary And Sufficient

Blood vessel formation requires endothelial cell (EC) migration that depends on dynamic remodeling of the cytoskeleton. Rudhira/Breast Carcinoma Amplified Sequence 3 (BCAS3) is a cytoskeletal protein essential for EC migration and sprouting angiogenesis during mouse development and is implicated in metastatic disease. Here, we report that Rudhira mediates cytoskeleton organization and dynamics during EC migration. Rudhira binds to both microtubules (MTs) and vimentin intermediate filaments (IFs) and stabilizes MTs. Rudhira depletion impairs cytoskeletal cross-talk, MT stability, and hence focal adhesion disassembly. The BCAS3 domain of Rudhira is necessary and sufficient for MT-IF cross-linking and cell migration. Pharmacologically restoring MT stability rescues gross cytoskeleton organization and angiogenic sprouting in Rudhira-depleted cells. Our study identifies the novel and essential role of Rudhira in cytoskeletal cross-talk and assigns function to the conserved BCAS3 domain. Targeting Rudhira could allow tissue-restricted cytoskeleton modulation to control cell migration and angiogenesis in development and disease.

scholarly journals Different translation dynamics of β-and γ-actin regulates cell migration

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Pavan Vedula ◽  
Satoshi Kurosaka ◽  
Brittany MacTaggart ◽  
Qin Ni ◽  
Garegin Papoian ◽  
...  
Keyword(s):  
Cell Migration ◽  
Amino Acid ◽  
Single Molecule ◽  
Amino Acid Level ◽  
Focal Adhesions ◽  
Mesenchymal Cell ◽  
Cell Periphery ◽  
Pronounced Difference ◽  
Coding Sequence

β- and γ-cytoplasmic actins are ubiquitously expressed in every cell type and are nearly identical at the amino acid level but play vastly different roles in vivo. Their essential roles in embryogenesis and mesenchymal cell migration critically depend on the nucleotide sequences of their genes, rather than their amino acid sequence, however it is unclear which gene elements underlie this effect. Here we address the specific role of the coding sequence in β- and γ-cytoplasmic actins' intracellular functions, using stable polyclonal populations of immortalized mouse embryonic fibroblasts with exogenously expressed actin isoforms and their 'codon-switched' variants. When targeted to the cell periphery using the β-actin 3′UTR, β-actin and γ-actin have differential effects on cell migration. These effects directly depend on the coding sequence. Single molecule measurements of actin isoform translation, combined with fluorescence recovery after photobleaching, demonstrate a pronounced difference in β- and γ-actins' translation elongation rates in cells, leading to changes in their dynamics at the focal adhesions, impairments in actin bundle formation, and reduced cell anchoring to the substrate during migration. Our results demonstrate that coding sequence-mediated differences in actin translation play a key role in cell migration.

scholarly journals Sphingosine 1-Phosphate (S1P) Receptors 1 and 2 Coordinately Induce Mesenchymal Cell Migration through S1P Activation of Complementary Kinase Pathways

2013 ◽  
Vol 288 (8) ◽  
pp. 5398-5406 ◽  
Author(s):  
Patrick Quint ◽  
Ming Ruan ◽  
Larry Pederson ◽  
Moustapha Kassem ◽  
Jennifer J. Westendorf ◽  
...  
Keyword(s):  
Cell Migration ◽  
Mesenchymal Cell ◽  
S1p Receptors ◽  
Sphingosine 1 Phosphate

scholarly journals Effects of Bis-diamine to Cardiac Mesenchymal Cell Migration of the Chick Embryo

1995 ◽  
Vol 35 (2) ◽  
pp. 215-222
Author(s):  
Hiroshi SUMIDA ◽  
Harukazu NAKAMURA ◽  
Tatsuhiro MATSUO ◽  
Mineo YASUDA
Keyword(s):  
Cell Migration ◽  
Chick Embryo ◽  
Mesenchymal Cell

scholarly journals Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration

2020 ◽  
Author(s):  
Ah-Lai Law ◽  
Shamsinar Jalal ◽  
Fuad Mosis ◽  
Tommy Pallett ◽  
Ahmad Guni ◽  
...  
Keyword(s):  
Cell Migration ◽  
Binding Sites ◽  
Leading Edge ◽  
Mesenchymal Cell ◽  
Negative Regulators ◽  
Binding Partner ◽  
Direct Binding ◽  
The Stability ◽  
Wave Complex ◽  
Lamellipodia Formation

AbstractCell migration is important for development and its aberrant regulation contributes to many diseases. The Scar/WAVE complex is essential for Arp2/3 mediated lamellipodia formation during mesenchymal cell migration and several coinciding signals activate it. However, so far, no direct negative regulators are known. We have identified Nance-Horan Syndrome-like 1 protein (NHSL1) as a novel, direct binding partner of the Scar/WAVE complex, which co-localise at protruding lamellipodia. This interaction is mediated by the Abi SH3 domain and two binding sites in NHSL1. Furthermore, active Rac binds to NHSL1 at two regions that mediate leading edge targeting of NHSL1 suggesting that Rac recruits NHSL1. Surprisingly, NHSL1 inhibits cell migration through its interaction with the Scar/WAVE complex. Mechanistically, NHSL1 may reduce cell migration efficiency by impeding Arp2/3 activity, as measured in cells using a novel Arp2/3 FRET-FLIM biosensor, resulting in reduced F-actin content of lamellipodia, and consequently impairing the stability of lamellipodia protrusions.

scholarly journals Migrating fibroblasts reorient directionality by a metastable, PI3K-dependent mechanism

2012 ◽  
Vol 197 (1) ◽  
pp. 105-114 ◽  
Author(s):  
Erik S. Welf ◽  
Shoeb Ahmed ◽  
Heath E. Johnson ◽  
Adam T. Melvin ◽  
Jason M. Haugh
Keyword(s):  
Cell Migration ◽  
Total Internal Reflection ◽  
Mesenchymal Cell ◽  
Lateral Spreading ◽  
Pi3k Signaling ◽  
Spatial Cues ◽  
Cell Protrusion ◽  
Pi3k Inhibition ◽  
Phosphoinositide 3 Kinase ◽  
Dependent Mechanism

Mesenchymal cell migration as exhibited by fibroblasts is distinct from amoeboid cell migration and is characterized by dynamic competition among multiple protrusions, which determines directional persistence and responses to spatial cues. Localization of phosphoinositide 3-kinase (PI3K) signaling is thought to play a broadly important role in cell motility, yet the context-dependent functions of this pathway have not been adequately elucidated. By mapping the spatiotemporal dynamics of cell protrusion/retraction and PI3K signaling monitored by total internal reflection fluorescence microscopy, we show that randomly migrating fibroblasts reorient polarity through PI3K-dependent branching and pivoting of protrusions. PI3K inhibition did not affect the initiation of newly branched protrusions, nor did it prevent protrusion induced by photoactivation of Rac. Rather, PI3K signaling increased after, not before, the onset of local protrusion and was required for the lateral spreading and stabilization of nascent branches. During chemotaxis, the branch experiencing the higher chemoattractant concentration was favored, and, thus, the cell reoriented so as to align with the external gradient.

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