Converging and Unique Mechanisms of Mechanotransduction at Adhesion Sites

Han, Mitchell K. L.; Rooij, Johan de

doi:10.1016/j.tcb.2016.03.005

Cited by 65 publications

(57 citation statements)

References 94 publications

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“…Myosin II is a molecular motor that, through its interaction with F-actin, underlies cell contractility and movement (Rao and Maddala, 2006; Maddala et al, 2007; Doyle et al, 2015; Aranjuez et al, 2016; Han and de Rooij, 2016; Mui et al, 2016), and also has an important role in minimizing curvature of cell-surface microdomains (Elliott et al, 2015). Myosin activity has an important role in maintaining lens function as exposure to an MLCK inhibitor induces opacities in lens organ cultures (Maddala et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

N-cadherin regulates signaling mechanisms required for lens fiber cell elongation and lens morphogenesis

Logan

Rajakaruna

Bowen

et al. 2017

Developmental Biology

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Tissue development and regeneration involve high-ordered morphogenetic processes that are governed by elements of the cytoskeleton in conjunction with cell adhesion molecules. Such processes are particularly important in the lens whose structure dictates its function. Studies of our lens-specific N-cadherin conditional knockout mouse (N-cadcKO) revealed an essential role for N-cadherin in the migration of the apical tips of differentiating lens fiber cells along the apical surfaces of the epithelium, a region termed the Epithelial Fiber Interface (EFI), that is necessary for normal fiber cell elongation and the morphogenesis. Studies of the N-cadcKO lens suggest that N-cadherin function in fiber cell morphogenesis is linked to the activation of Rac1 and myosin II, both signaling pathways central to the regulation of cell motility including determining the directionality of cellular movement. The absence of N-cadherin did not disrupt lateral contacts between fiber cells during development, and the maintenance of Aquaporin-0 and increased expression of EphA2 at cell-cell interfaces suggests that these molecules may function in this role. E-cadherin was maintained in newly differentiating fiber cells without interfering with expression of lens-specific differentiation proteins but was not able to replace N-cadherin function in these cells. The dependence of migration of the fiber cell apical domains along the EFI for lens morphogenesis on N-cadherin provides new insight into the process of tissue development.

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Section: Discussionmentioning

confidence: 99%

N-cadherin regulates signaling mechanisms required for lens fiber cell elongation and lens morphogenesis

Logan

Rajakaruna

Bowen

et al. 2017

Developmental Biology

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“…The effect of mechanical force on cellular behavior is an emerging field of study that has garnered significant interest from diverse disciplines, including cell biology, biophysics, cancer biology, vascular biology, and tissue engineering . Researchers are often interested in determining which proteins are key to mechanotransduction pathways and how these proteins transmit and/or detect mechanical cues . Research in this area has predominantly focused on two adhesion structures, namely focal adhesions (FAs) and adherens junctions (AJs), because they serve as linkages between a cell's force‐generating actomyosin network and the extracellular environment .…”

mentioning

confidence: 99%

“…Researchers are often interested in determining which proteins are key to mechanotransduction pathways and how these proteins transmit and/or detect mechanical cues . Research in this area has predominantly focused on two adhesion structures, namely focal adhesions (FAs) and adherens junctions (AJs), because they serve as linkages between a cell's force‐generating actomyosin network and the extracellular environment . Whereas FAs bind to extracellular matrix proteins, AJs adhere to receptors on adjacent cell membranes .…”

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confidence: 99%

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Improving Quality, Reproducibility, and Usability of FRET‐Based Tension Sensors

et al. 2018

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Mechanobiology, the study of how mechanical forces affect cellular behavior, is an emerging field of study that has garnered broad and significant interest. Researchers are currently seeking to better understand how mechanical signals are transmitted, detected, and integrated at a subcellular level. One tool for addressing these questions is a Förster resonance energy transfer (FRET)‐based tension sensor, which enables the measurement of molecular‐scale forces across proteins based on changes in emitted light. However, the reliability and reproducibility of measurements made with these sensors has not been thoroughly examined. To address these concerns, we developed numerical methods that improve the accuracy of measurements made using sensitized emission‐based imaging. To establish that FRET‐based tension sensors are versatile tools that provide consistent measurements, we used these methods, and demonstrated that a vinculin tension sensor is unperturbed by cell fixation, permeabilization, and immunolabeling. This suggests FRET‐based tension sensors could be coupled with a variety of immuno‐fluorescent labeling techniques. Additionally, as tension sensors are frequently employed in complex biological samples where large experimental repeats may be challenging, we examined how sample size affects the uncertainty of FRET measurements. In total, this work establishes guidelines to improve FRET‐based tension sensor measurements, validate novel implementations of these sensors, and ensure that results are precise and reproducible. © 2018 International Society for Advancement of Cytometry

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“…Adherens junctions and desmosomes are adhesive intercellular junctions that mechanically integrate adjacent cells within various types of tissues. [2][3][4][5] As classically defined, the adherens junction is a circumferential belt of adhesive contact that is coupled to the actin cytoskeleton, while desmosomes are spot-weld-like contacts that are linked to intermediate filaments. 6,7 Cadherins are the primary adhesion molecules at both adherens junctions and desmosomes.…”

Section: Molecular Components Of Adhesive Intercellular Junctionsmentioning

confidence: 99%

Cadherin tales: Regulation of cadherin function by endocytic membrane trafficking

Cadwell

Kowalczyk

2016

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Cadherins are the primary adhesion molecules in adherens junctions and desmosomes and play essential roles in embryonic development. Although significant progress has been made in understanding cadherin structure and function, we lack a clear vision of how cells confer plasticity upon adhesive junctions to allow for cellular rearrangements during development, wound healing and metastasis. Endocytic membrane trafficking has emerged as a fundamental mechanism by which cells confer a dynamic state to adhesive junctions. Recent studies indicate that the juxtamembrane domain of classical cadherins contains multiple endocytic motifs, or "switches," that can be used by cellular membrane trafficking machinery to regulate adhesion.The cadherin-binding protein p120-catenin (p120) appears to be the master regulator of access to these switches, thereby controlling cadherin endocytosis and turnover. This review focuses on p120 and other cadherin-binding proteins, ubiquitin ligases, and growth factors as key modulators of cadherin membrane trafficking. K E Y W O R D Sadherens junction, adhesion, cadherin, desmosome, endocytosis, p120-catenin, recycling

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Converging and Unique Mechanisms of Mechanotransduction at Adhesion Sites

Cited by 65 publications

References 94 publications

N-cadherin regulates signaling mechanisms required for lens fiber cell elongation and lens morphogenesis

N-cadherin regulates signaling mechanisms required for lens fiber cell elongation and lens morphogenesis

Improving Quality, Reproducibility, and Usability of FRET‐Based Tension Sensors

Cadherin tales: Regulation of cadherin function by endocytic membrane trafficking

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