Cell–extracellular matrix dynamics

Doyle, Andrew D.; Nazari, Shayan S.; Yamada, Kenneth M.

doi:10.1088/1478-3975/ac4390

Cited by 50 publications

(37 citation statements)

References 87 publications

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“…Given these observations, it is notable that exosome release was required for neural folds to adhere to fibronectin, suggesting that NCC extracellular vesicles might also carry integrins. Supporting this idea, binding of integrin receptors to fibronectin anchors focal adhesions, which stabilize cell protrusions and provide traction to migratory cells ( Doyle et al, 2022 ). Disrupting this would explain the change in shape ( Fig.…”

Section: Discussionmentioning

confidence: 99%

Chick cranial neural crest cells release extracellular vesicles that are critical for their migration

Gustafson

Roffers-Agarwal

Gammill

2022

Journal of Cell Science

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The content and activity of extracellular vesicles purified from cell culture media or bodily fluids have been studied extensively; however, the physiological relevance of exosomes within normal biological systems is poorly characterized, particularly during development. Although exosomes released by invasive, metastatic cells alter migration of neighboring cells in culture, it is unclear whether cancer cells misappropriate exosomes released by healthy, differentiated cells or reactivate dormant developmental programs that include exosome cell-cell communication. Using chick cranial neural fold cultures, we show that migratory neural crest cells, a developmentally critical cell type and model for metastasis, release and deposit CD63-positive, 30-100 nm particles into the extracellular environment. Neural crest cells contain ceramide-rich multi-vesicular bodies and produce larger vesicles positive for migrasome markers as well. We conclude that neural crest cells produce extracellular vesicles including exosomes and migrasomes. When Rab27a plasma membrane docking is inhibited, neural crest cells become less polarized and rounded, leading to a loss of directional migration and reduced speed. These results indicate that neural crest cell exosome release is critical for migration.

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Section: Discussionmentioning

confidence: 99%

Chick cranial neural crest cells release extracellular vesicles that are critical for their migration

Gustafson

Roffers-Agarwal

Gammill

2022

Journal of Cell Science

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“…On binding its partner molecule, integrin activates by extending the extracellular domains of both subunits and separating their cytoplasmic tails. Activation stimulates integrin clustering and assembly of the focal adhesion complex, a large cytoplasmic signaling hub comprising hundreds of proteins, including integrin receptors and their interactors, proteins regulating the actin cytoskeleton, force transducers like talin and vinculin, and many other regulatory elements (20). Focal adhesion structures transmit to the ECM, the force generated by the cytoskeleton and in turn allow the cell to respond to the mechanical changes occurring in the matrix itself.…”

Section: Integrins Mediate Cell Interaction With the Microenvironment...mentioning

confidence: 99%

“…Focal adhesion structures transmit to the ECM, the force generated by the cytoskeleton and in turn allow the cell to respond to the mechanical changes occurring in the matrix itself. Integrin activation thus mediates bidirectional signaling, and it increases ECM binding affinity while stimulating intracellular mechanisms that regulate cell motility and migration or differentiation (20).…”

Section: Integrins Mediate Cell Interaction With the Microenvironment...mentioning

confidence: 99%

Dynamics and physiological meaning of complexes between ion channels and integrin receptors: the case of Kv11.1

Becchetti

Duranti

Arcangeli

2022

American Journal of Physiology-Cell Physiology

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The cellular functions are regulated by a complex interplay of diffuse and local signals. Experimental work in cell physiology has led to recognize that understanding a cell's dynamics requires a deep comprehension of local fluctuations of cytosolic regulators. Macromolecular complexes are major determinants of local signaling. Multi-enzyme assemblies limit the diffusion restriction to reaction kinetics by direct exchange of metabolites. Likewise, close coupling of ion channels and transporters modulate the ion concentration around a channel mouth or transporter binding site. Extreme signal locality is brought about by conformational coupling between membrane proteins, as is typical of mechanotransduction. A paradigmatic case is integrin-mediated cell adhesion. Sensing the extracellular microenvironment and providing an appropriate response is essential in growth and development and has innumerable pathological implications. The process involves bidirectional signal transduction by complex supra-molecular structures that link integrin receptors to ion channels and transporters, growth factor receptors, cytoskeletal elements and other regulatory elements. The dynamics of such complexes is only beginning to be understood. A thoroughly studied example is the association between integrin receptors and the voltage-gated K+ channels Kv11.1. These channels are widely expressed in early embryos, where their physiological roles are poorly understood and apparently different from the shaping of action potential firing in the adult. Hints about these roles come from studies in cancer cells, where Kv11.1 is often overexpressed and appears to re-assume functions, such as controlling cell proliferation/differentiation, apoptosis and migration. Kv11.1 is implicated in these processes through its linking to integrin subunits.

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“…The dynamic assembly and disassembly of focal adhesions at the front edge and trailing edge of the cell, respectively, are tightly coupled with actomyosin contractility to facilitate efficient cell migration (Vicente-Manzanares and Horwitz, 2011). During migration, focal adhesions are necessary for mechanical force sensation and generation, as well as serve as signaling hubs that transduce signals to the cell and to the environment (Balaban et al, 2001; Doyle et al, 2022; Eke and Cordes, 2015; Hoffman, 2014; Oakes and Gardel, 2014; Turner, 2000; Zaidel-Bar et al, 2007a). Over the past 40 years, numerous proteins have been discovered and identified as focal adhesion proteins (Burridge, 2017; Legerstee and Houtsmuller, 2021; Wozniak et al ., 2004; Wu, 2007; Zaidel-Bar et al ., 2007a).…”

Section: Introductionmentioning

confidence: 99%

Focal adhesion-based cell migration is differentially regulated in vivo versus in vitro by Paxillin phosphorylation

Xue¹,

Varady²,

Waddell³

et al. 2022

Preprint

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SummaryFocal adhesions are important subcellular structures that physically link the cell to the extracellular matrix (ECM), thus facilitating efficient cell migration. Although in vitro cell culture studies have provided a wealth of information regarding focal adhesion biology, it is critical to understand how focal adhesions are dynamically regulated in their native environment. We developed a zebrafish transplantation system in which we could efficiently visualize focal adhesion structures during single cell migration in vivo with high-resolution live cell imaging. By comparing focal adhesions between this in vivo system and the traditional in vitro cell culture model, we show differential regulation of a core focal adhesion protein, Paxillin. We find that a key site of phosphoregulation on Paxillin, tyrosine 118 (Y118), exhibits reduced phosphorylation in migrating cells in vivo in both zebrafish and mouse melanoma models, contrary to the pivotal role for this phosphorylation event in cell culture studies. Furthermore, direct modulation of this residue by site directed mutagenesis leads to opposite cell migration phenotypes in vivo versus in vitro in both migrating cancer cells and macrophages. Unexpectedly, expression of a non-phosphorylatable version of Y118-Paxillin promotes cell migration in vivo, despite inhibiting cell migration in the in vitro cell culture conditions. To further understand the mechanism of this regulation, we find that the upstream kinase, focal adhesion kinase (FAK), is downregulated in cells in vivo, and that cells expressing non-phosphorylatable Y118-Paxillin exhibit increased interactions between Paxillin and CRKII, an adaptor protein known to promote cell migration signaling. Collectively, our findings provide significant new insight into how focal adhesions are regulated in cells migrating in their native environment.

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Cell–extracellular matrix dynamics

Cited by 50 publications

References 87 publications

Chick cranial neural crest cells release extracellular vesicles that are critical for their migration

Chick cranial neural crest cells release extracellular vesicles that are critical for their migration

Dynamics and physiological meaning of complexes between ion channels and integrin receptors: the case of Kv11.1

Focal adhesion-based cell migration is differentially regulated in vivo versus in vitro by Paxillin phosphorylation

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