Can 1000 Reviews Be Wrong? Actin, α-Catenin, and Adherens Junctions

Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Cell (Impact Factor: 32.24). 01/2006; 123(5):769-72. DOI: 10.1016/j.cell.2005.11.009
Source: PubMed


Coupling between cell adhesion and the actin cytoskeleton is thought to require a stable link between the cadherin-catenin complex and actin that is mediated by alpha-catenin. In this issue of Cell, the Weis and Nelson groups call this static model into question, showing that alpha-catenin can directly regulate actin dynamics (Drees et al., 2005 and Yamada et al., 2005).

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    • "Adherens junctions form through homophilic interactions between E-cadherins whose cytoplasmic domains are associated with a filamentous actin belt through a large number of adaptor proteins (Abe and Takeichi, 2008). Recently, epithelial protein lost in neoplasm (EPLIN, also known as LIMA1) has been shown to serve as an adaptor in adherens junctions and to form a ternary complex with a-catenin and F-actin without impairing their binding to b-catenin (Gates and Peifer, 2005; Mège et al., 2006; Abe and Takeichi, 2008; Baum and Georgiou, 2011). "
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    ABSTRACT: PINCH1 is a LIM-only domain protein that forms a ternary complex with integrin-linked kinase (ILK) and parvin (IPP complex) downstream of integrins. Here we demonstrate that PINCH-1 gene ablation in the epidermis of mice caused epidermal detachment from the basement membrane, epidermal hyperthickening and progressive hair loss. PINCH-1 deficient keratinocytes also displayed profound adhesion, spreading and migration defects in vitro that were, however, significantly more severe than those of ILK-deficient keratinocytes indicating that PINCH-1 also exerts functions in an ILK-independent manner. By isolating the PINCH-1 interactome, the LIM domain containing and actin-binding protein Epithelial Protein Lost in Neoplasm (EPLIN) was identified as a novel PINCH-1 associated protein. EPLIN localized in a PINCH-1-dependent manner to integrin adhesion sites of keratinocytes in vivo and in vitro and its depletion severely attenuated keratinocyte spreading and migration on collagen and fibronectin without affecting PINCH-1 levels in FAs. Since the low PINCH-1 levels in ILK-deficient keratinocytes were sufficient to recruit EPLIN to integrin adhesions, our findings suggest that PINCH-1 regulates integrin-mediated adhesion of keratinocytes through the interactions with ILK as well as EPLIN.
    Journal of Cell Science 01/2015; 128(5). DOI:10.1242/jcs.162545 · 5.43 Impact Factor
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    • "Not only is the cadherin family member E-cadherin responsible for compaction of the embryo, but it is also a key organizer of adhesion junctions in epithelial tissue [10–12]. Cadherins which are located at the plasma membrane are intracellularly connected to the actin cytoskeleton via special proteins like catenins [13]. Gap junction and cell adhesion proteins are also associated with each other and exhibit a functional cooperation to increase the stability of cell-cell and cell-extracellular matrix structures [14]. "
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    ABSTRACT: The aim of this study was to investigate the effects of experimentally induced diabetes on (a) germ cells, (b) in vitro fertilization (IVF) success rate, and (c) gap junction and cell adhesion molecule gene and protein expressions during the early blastocyst period. Germ cells were obtained from healthy and diabetic rats, analyzed for number, motility, and morphology, and used for IVF. After reaching the early blastocyst stage, the expressions of genes encoding gap junction proteins and cell adhesion molecules were analyzed by quantitative RT-PCR. Histomorphologically and immunohistochemically analyses were also performed. Diabetes significantly affected sperm number and motility and the development of oocytes. Gene expressions of β -catenin and connexin family members and protein expressions of E-cadherin and connexin-43 significantly decreased in groups including germ cells isolated from diabetic rats. Connective tissue growth factor expression increased in groups that included sperm cells isolated from diabetic male rats, whereas mucin-1 expression increased in the group that included oocytes isolated from diabetic female rats paired with sperm cells isolated from healthy male rats. In summary, experimentally induced diabetes was found to influence gap junctions, cell adhesion molecules, and associated proteins which all have important roles in germ cell maturation, fertilization, and development.
    Journal of Diabetes Research 03/2013; 2013:603813. DOI:10.1155/2013/603813 · 2.16 Impact Factor
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    • "These morphogenetic events underlie shape changes and/or movements, mostly dependent on an intact actomyosin cytoskeleton (a network of actin filaments cross-linked with myosin II molecular motors). Actin filaments and myosin II generate tensile forces in individual cells that are transmitted across an entire tissue through adherens junctions (AJs) [1], [2]. During epithelial morphogenesis apical constriction is generated by this type of forces and results in a reduction of the cells' apical domain [3]. "
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    ABSTRACT: Coordination of apical constriction in epithelial sheets is a fundamental process during embryogenesis. Here, we show that DRhoGEF2 is a key regulator of apical pulsation and constriction of amnioserosal cells during Drosophila dorsal closure. Amnioserosal cells mutant for DRhoGEF2 exhibit a consistent decrease in amnioserosa pulsations whereas overexpression of DRhoGEF2 in this tissue leads to an increase in the contraction time of pulsations. We probed the physical properties of the amnioserosa to show that the average tension in DRhoGEF2 mutant cells is lower than wild-type and that overexpression of DRhoGEF2 results in a tissue that is more solid-like than wild-type. We also observe that in the DRhoGEF2 overexpressing cells there is a dramatic increase of apical actomyosin coalescence that can contribute to the generation of more contractile forces, leading to amnioserosal cells with smaller apical surface than wild-type. Conversely, in DRhoGEF2 mutants, the apical actomyosin coalescence is impaired. These results identify DRhoGEF2 as an upstream regulator of the actomyosin contractile machinery that drives amnioserosa cells pulsations and apical constriction.
    PLoS ONE 09/2011; 6(9):e23964. DOI:10.1371/journal.pone.0023964 · 3.23 Impact Factor
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