Cadherin adhesome at a glance

Zaidel-Bar, Ronen

doi:10.1242/jcs.111559

Cited by 121 publications

(108 citation statements)

References 95 publications

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“…Given the complexity of the cell cortex, with its more than 60 adaptor proteins and over 70 regulatory components (Zaidel-Bar, 2013), diminishing its bulk should not be the sole mechanism to reduce cortical tension. In fact, cases of increased F-actin density at cell-cell contacts have been reported (for example, see Chu et al, 2004), and in mouse oocytes, reduction of cortical tension at cell contacts is associated with higher F-actin density, yet an exclusion of myosin II from contacts (Chaigne et al, 2013).…”

Section: Molecular Binding Energies and Cell Adhesionmentioning

confidence: 99%

Cell adhesion strength from cortical tension – an integration of concepts

Winklbauer

2015

Journal of Cell Science

101

162

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Morphogenetic mechanisms such as cell movement or tissue separation depend on cell attachment and detachment processes, which involve adhesion receptors as well as the cortical cytoskeleton. The interplay between the two components is of stunning complexity. Most strikingly, the binding energy of adhesion molecules is usually too small for substantial cell-cell attachment, pointing to a main deficit in our present understanding of adhesion. In this Opinion article, I integrate recent findings and conceptual advances in the field into a coherent framework for cell adhesion. I argue that active cortical tension is best viewed as an integral part of adhesion, and propose on this basis a non-arbitrary measure of adhesion strength -the tissue surface tension of cell aggregates. This concept of adhesion integrates heterogeneous molecular inputs into a single mechanical property and simplifies the analysis of attachment-detachment processes. It draws attention to the enormous variation of adhesion strengths among tissues, whose origin and function is little understood.

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Section: Molecular Binding Energies and Cell Adhesionmentioning

confidence: 99%

Cell adhesion strength from cortical tension – an integration of concepts

Winklbauer

2015

Journal of Cell Science

101

162

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“…nectins [17], growth factors receptors and integrins). In spite of extensive progress in the identification of cytoskeletal proteins found at junctions [18,19], the precise F-actin organization and the specific actin remodelling functions at cadherin contacts lack in-depth understanding. A pool of G-actin at junctions [20] has unknown functions, but may provide a local pool of monomers for filament remodelling.…”

Section: Junctional Actinmentioning

confidence: 99%

Spatial integration of E-cadherin adhesion, signalling and the epithelial cytoskeleton

Braga

2016

Current Opinion in Cell Biology

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“…Given that both cell-cell and cell-substrate adhesion must be dynamic (Guillot and Lecuit, 2013;Wolfenson et al, 2013), to allow tissue growth and remodeling, and stable, to provide mechanical strength, these interactions are highly regulated. Numerous proteins have been identified that link adhesive proteins to the cytoplasmic components (Guillot and Lecuit, 2013;Wolfenson et al, 2013;Zaidel-Bar, 2013). In the present study, we used a relatively new biotin-tagging method (Roux et al, 2012) to expand the list of proteins that are proximal to the cell adhesion protein E-cadherin.…”

Section: Introductionmentioning

confidence: 99%

“…The interactions with actin are indirect and occur through extensively studied catenin proteins that bind to the intracellular domain of E-cadherin, namely b-catenin and a-catenin, and also through several cateninassociated actin-binding proteins, including vinculin, formin-1 and VASP (reviewed by Meng and Takeichi, 2009). Many proteins have been localized to adherens junctions by biochemical and microscopic techniques (Smith et al, 2011;Zaidel-Bar, 2013), but there have been relatively few attempts at global proteomic analysis.…”

Section: Introductionmentioning

confidence: 99%

Biotin ligase tagging identifies proteins proximal to E-cadherin, including lipoma preferred partner, a regulator of epithelial cell-cell and cell-substrate adhesion

Itallie

Tietgens

Aponte

et al. 2013

Journal of Cell Science

116

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Known proteins associated with the cell-adhesion protein Ecadherin include catenins and proteins involved in signaling, trafficking and actin organization. However, the list of identified adherens junction proteins is likely to be incomplete, limiting investigation into this essential cell structure. To expand the inventory of potentially relevant proteins, we expressed Ecadherin fused to biotin ligase in MDCK epithelial cells, and identified by mass spectrometry neighboring proteins that were biotinylated. The most abundant of the 303 proteins identified were catenins and nearly 40 others that had been previously reported to influence cadherin function. Many others could be rationalized as novel candidates for regulating the adherens junction, cytoskeleton, trafficking or signaling. We further characterized lipoma preferred partner (LPP), which is present at both cell contacts and focal adhesions. Knockdown of LPP demonstrated its requirement for Ecadherin-dependent adhesion and suggested that it plays a role in coordination of the cell-cell and cell-substrate cytoskeletal interactions. The analysis of LPP function demonstrates proof of principle that the proteomic analysis of E-cadherin proximal proteins expands the inventory of components and tools for understanding the function of E-cadherin.

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Cadherin adhesome at a glance

Cited by 121 publications

References 95 publications

Cell adhesion strength from cortical tension – an integration of concepts

Cell adhesion strength from cortical tension – an integration of concepts

Spatial integration of E-cadherin adhesion, signalling and the epithelial cytoskeleton

Biotin ligase tagging identifies proteins proximal to E-cadherin, including lipoma preferred partner, a regulator of epithelial cell-cell and cell-substrate adhesion

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