An anchorage-dependent signal distinct from p42/44 MAP kinase activation is required for cell cycle progression

Gall, Maude Le; Grall, Dominique; Chambard, Jean-Claude; Pouysségur, Jacques; E, Van Obberghen-Schilling

doi:10.1038/sj.onc.1202057

Cited by 47 publications

(43 citation statements)

References 25 publications

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“…1). It is known that the ability of mitogens to activate ERK is anchorage dependent and that loss of responsiveness is complete by 12 h (Le Gall et al, 1998). However, in the case of Akt activation, we found that loss of serum or insulin responsiveness occurs immediately following anchorage removal.…”

Section: Activation Of Akt Is Strictly Adhesion Dependent In Ccl39 Cellscontrasting

confidence: 48%

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Adhesion‐dependent control of Akt/protein kinase B occurs at multiple levels

Gall

Chambard

Grall

et al. 2003

Journal Cellular Physiology

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The protein kinase Akt, also known as Protein Kinase B, has been implicated in the survival of several cell types challenged with various apoptotic stimuli. In CCL39 lung fibroblasts, apoptosis is induced by anchorage and mitogen removal. Mitogeninduced activation of Akt is highly anchorage dependent in these cells and removal of adhesion is accompanied by a rapid loss in responsiveness to soluble agonists followed by a significant decrease in Akt abundance. Loss of the protein appears to be independent of kinase activation since the expression of a constitutively active form, gag-Akt, is also dependent upon cell adhesion. Although the disappearance of Akt is coincident with the induction of programmed cell death, it cannot be fully prevented by treatment of cells with the caspase inhibitor ZVAD or by sustained activation of the anti-apoptotic Raf/ERK pathway, in cells expressing an inducible DRaf-1:ER construct. In addition, a previously unrecognized decrease in Akt mRNA levels following anchorage removal occurs suggesting that anchorage-dependent transcriptional and/or post-transcriptional mechanisms contribute to the adhesiondependent regulation of Akt expression.

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Section: Activation Of Akt Is Strictly Adhesion Dependent In Ccl39 Cellscontrasting

confidence: 48%

“…Following centrifugation, cells were resuspended in serum-free DMEM containing 1% bovine serum albumin (BSA) at 10 5 cells per ml and transferred to spinner flasks, as previously described (Le Gall et al, 1998).…”

Section: Cells and Culture Conditionsmentioning

confidence: 99%

Adhesion‐dependent control of Akt/protein kinase B occurs at multiple levels

Gall

Chambard

Grall

et al. 2003

Journal Cellular Physiology

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“…These results, combined with the results using U0126, suggest that while MEK may be important for cyclin D1 expression on permissive substrates, it is not sufficient to induce cyclin D1 on polymerized collagen. Evidence showing that activation of ERK in suspended CCL9 cells fails to activate cyclin D1 expression have suggested that other adhesion-dependent signals in addition to ERK may be required in some cell types to induce cyclin D1 (66). One potential mechanism by which ERK is prevented from signaling to cyclin D1 on collagen gel, suggested by the vastly different cell shapes on these substrates, might be cytoskeletal differences between cells adherent to collagen film or collagen gels and the ability to form intracellular cytoskeletal scaffolds important for interaction between signaling proteins.…”

Section: Discussionmentioning

confidence: 99%

The Role of Collagen Structure in Mitogen Stimulation of ERK, Cyclin D1 Expression, and G1-S Progression in Rat Hepatocytes

Fassett

Tobolt

Nelsen

et al. 2003

Journal of Biological Chemistry

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Adhesion to type 1 collagen can elicit different cellular responses dependent upon whether the collagen is in a fibrillar form (gel) or monomeric form (film). Hepatocytes adherent to collagen film spread extensively, express cyclin D1, and increase DNA synthesis in response to epidermal growth factor, whereas hepatocytes adherent to collagen gel have increased differentiated function, but lower DNA synthesis. The signaling mechanisms by which different forms of type I collagen modulate cell cycle progression are unknown. When ERK MAP kinase activation was analyzed in hepatocytes attached to collagen film, two peaks of ERK activity were demonstrated. Only the second peak, which correlated with an increase of cyclin D1, was required for G 1 -S progression. Notably, this second peak of ERK activity was absent in cells adherent to collagen gel, but not required in the presence of exogenous cyclin D1. Expression of activated mutants of the Ras/Raf/MEK signaling pathway in cells adherent to collagen gel restored ERK phosphorylation and DNA synthesis, but differentially affected cell shape. Although Ras, Raf, and MEK all increased expression of cyclin D1 on collagen film, only Ras and Raf significantly up-regulated cyclin D1 levels on collagen gel. These results demonstrate that adhesion to polymerized collagen induces growth arrest by inhibiting the Ras/ERK-signaling pathway to cyclin D1 required in late G 1 .

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“…Activation of p42/p44MAPK, 9 ± 12 or p60 src pathways 13 induce cyclin D 1 expression in a cell adhesion dependent fashion. 14 Integrins are heterodimeric cell surface receptors that mediate cell adhesion to the extracellular matrix (ECM) and transduce biochemical signals, including activation of focal adhesion kinase (FAK). 15 ± 19 Neutralizing antibodies against integrins induce cell detachment followed by apoptosis in epithelial cells.…”

Section: Introductionmentioning

confidence: 99%

Bcl-2 induces cyclin D1 promoter activity in human breast epithelial cells independent of cell anchorage

Lin

Lee

et al. 2001

Cell Death Differ

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Cyclin D 1 expression is co-regulated by growth factor and cell adhesion signaling. Cell adhesion to the extracellular matrix activates focal adhesion kinase (FAK), which is essential for cyclin D 1 expression. Upon the loss of cell adhesion, cyclin D 1 expression is downregulated, followed by apoptosis in normal epithelial cells. Since bcl-2 prevents apoptosis induced by the loss of cell adhesion, we hypothesized that bcl-2 induces survival signaling complementary to cell adhesion-mediated gene regulation. In the present study, we investigated the role of bcl-2 on FAK activity and cyclin D 1 expression. We found that bcl-2 overexpression induces cyclin D 1 expression in human breast epithelial cell line MCF10A independent of cell anchorage. Increased cyclin D 1 expression in stable bcl-2 transfectants is not related to bcl-2-increased G 1 duration, but results from cyclin D 1 promoter activation. Transient transfection studies confirmed anchorage-independent bcl-2 induction of cyclin D 1 promoter activity in human breast epithelial cell lines (MCF10A, BT549, and MCF-7). We provide evidence that bcl-2 induction of cyclin D 1 expression involves constitutive activation of focal adhesion kinase, regardless of cell adhesion. The present study suggests a potential oncogenic activity for bcl-2 through cyclin D 1 induction, and provides an insight into the distinct proliferation-independent pathway leading to increased cyclin D 1 expression in breast cancer.Cell Death and Differentiation (2001) 8, 44 ± 50.

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An anchorage-dependent signal distinct from p42/44 MAP kinase activation is required for cell cycle progression

Cited by 47 publications

References 25 publications

Adhesion‐dependent control of Akt/protein kinase B occurs at multiple levels

Adhesion‐dependent control of Akt/protein kinase B occurs at multiple levels

The Role of Collagen Structure in Mitogen Stimulation of ERK, Cyclin D1 Expression, and G1-S Progression in Rat Hepatocytes

Bcl-2 induces cyclin D1 promoter activity in human breast epithelial cells independent of cell anchorage

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