Identification of a neural α-catenin as a key regulator of cadherin function and multicellular organization

Hirano, Shinji; Kimoto, Naomi; Shimoyama, Yutaka; Hirohashi, Setsuo; Takeichi, Masatoshi

doi:10.1016/0092-8674(92)90103-j

Cited by 538 publications

(365 citation statements)

References 26 publications

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“…Rac activity is required for the translocation of cadherins and catenins to cell-cell contact sites and for the recruitment of F-actin to adherens junctions [Hirano et al, 1992;Takaishi et al, 1997]. The expression of a DN-Rac mutant decreased cadherin-mediated cell-cell contacts in both primary keratinocytes and MDCKII cells [Hirano et al, 1992;Jou and Nelson, 1998]. We previously found that polyamine depletion decreased Rac1 activity [Ray et al, 2003], and the expression of CA-MEK1 restored Rac1 activity, migration and the ACS in these cells [Vaidya et al, 2005].…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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MEK/ERK regulates adherens junctions and migration through Rac1

Ray

Vaidya

Johnson

2006

Cell Motil. Cytoskeleton

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Polyamine depletion with the ornithine decarboxylase inhibitor a-difluoromethyl ornithine (DFMO), prevents Rac1 activation causing the formation of a thick actin cortex at the cell periphery and inhibits migration of intestinal epithelial cells. In the present study, we demonstrate that MEK activation by EGF increased Rac1 activation, dissociation of intercellular contacts, and migration in both control and polyamine-depleted cells, while U0126, a specific inhibitor of MEK1, prevented disruption of junctions as well as EGF-induced Rac1 activation. Constitutively active MEK1 (CA-MEK) expression altered cell-cell contacts in control and polyamine depleted cells. The expression of constitutively active Rac1 (CA-Rac1) restored b-catenin to the cell periphery and prevented the formation of actin cortex and caused the appearance of F-actin stress fibers in polyamine-depleted cells. Inhibition of Rac activation by NSC23766, a specific inhibitor of Tiam1, an upstream guanidine nucleotide exchange factor for Rac1, reproduced the b-catenin localization and actin structure of polyamine-depleted cells. Tiam1 localized more extensively with b-catenin at the cell periphery in CA-Rac1 cells compared to vector cells. Polyamine depletion decreased the expression of E-cadherin to a greater extent compared to b-catenin. Subcellular fractionation further confirmed our immuno-localization and western blotting observations. These data suggest that EGF acting through MEK1/ERK to activate Rac1 regulates cell-cell contacts. Thus, decreased migration in polyamine depleted cells may be due to the inhibition of Tiam1 activation of Rac1 and the subsequent decreased expression of b-catenin and E-cadherin leading to reduced cell-cell contacts. Cell Motil.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

MEK/ERK regulates adherens junctions and migration through Rac1

Ray

Vaidya

Johnson

2006

Cell Motil. Cytoskeleton

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“…Integrin receptors bind talin [133] and α-actinin [134] and other cytoskeleton-associated proteins [65,68,117], selectins bind α-actinin [135], and cadherins bind catenins [136]. In the case of integrin receptors it has been shown that one of the elements that regulates cytoskeleton association is clustering of the receptors within the plane of the membrane [65].…”

Section: Syndecan-cytoskeleton Associationmentioning

confidence: 99%

Syndecans: multifunctional cell-surface co-receptors

Carey

1997

Biochemical Journal

621

497

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This review will summarize our current state of knowledge of the structure, biochemical properties and functions of syndecans, a family of transmembrane heparan sulphate proteoglycans. Syndecans bind a variety of extracellular ligands via their covalently attached heparan sulphate chains. Syndecans have been proposed to play a role in a variety of cellular functions, including cell proliferation and cell–matrix and cell–cell adhesion. Syndecan expression is highly regulated and is cell-type- and developmental-stage-specific. The main function of syndecans appears to be to modulate the ligand-dependent activation of primary signalling receptors at the cell surface. Principal functions of the syndecan core proteins are to target the heparan sulphate chains to the appropriate plasma-membrane compartment and to interact with components of the actin-based cytoskeleton. Several functions of the syndecans, including syndecan oligomerization and actin cytoskeleton association, have been localized to specific structural domains of syndecan core proteins.

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“…The following antibodies were used: mouse mAb CCD7-1 to chicken cadherin-7 and mouse mAb CCD6B-1 or a rabbit antibody (anti-6B) to chicken cadherin-6B ; mouse mAbs HECD-1 (Shimoyama et al 1989) and SHE78-7 (Takara Shuzo co., Ltd) to human E-cadherin; rat mAb NCAT-2 to aN-catenin (Hirano et al 1992); mouse mAb 5H10 to bcatenin (gift from Dr M.J. Wheelock); mouse mAb 7E-1B8 to PSD-95 (Af®nity Bioreagents Inc.); mouse mAb K28/86.2 to PSD-95 family proteins (Upstate Biotechnology Inc.); rabbit pAb to PSD-95 (gift from Dr Y. Hata); and mouse mAb 1D12 to synaptotagmin (Takahashi et al 1991). For detection of primary antibodies, we used Cy3-conjugated antibodies (Chemicon International, Inc.), biotinylated antibodies, Alexa 488-conjugated streptoavidin (Molecular probes, Inc.), or FITC-conjugated streptoavidin (Amersham Pharmacia Biotech).…”

Section: Antibodiesmentioning

confidence: 99%