Synergistic activation of c-fos promoter activity by Raf and Ral GDP dissociation stimulator

Okazaki, Mitsuko; Kishida, Shosei; Hinoi, Takao; Hasegawa, Tohru; Tamada, Masako; Kataoka, Tohru; Kikuchi, Akira

doi:10.1038/sj.onc.1200860

Cited by 66 publications

(74 citation statements)

References 28 publications

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“…To begin to define the role of Ral activation in growth control, we examined the consequences of Ral expression on gene regulatory responses that are downstream of Ras activation and required for oncogenic Ras-induced transformation. The activation of SRE-dependent gene expression, induction of cyclin D1 protein expression, and activation of NF-B transcription factors have all been defined as critical events mediating Ras transformation (15,29,49) and are convergence points for multiple Ras-dependent signals (18,41,43,64).…”

Section: Resultsmentioning

confidence: 99%

Ral GTPases Contribute to Regulation of Cyclin D1 through Activation of NF-κB

Henry

Moskalenko

Kaur

et al. 2000

Molecular and Cellular Biology

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Section: Resultsmentioning

confidence: 99%

Ral GTPases Contribute to Regulation of Cyclin D1 through Activation of NF-κB

Henry

Moskalenko

Kaur

et al. 2000

Molecular and Cellular Biology

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“…First, co-expression of isolated Ras-binding domains of RGL and RGL2/Rlf inhibited Ras, but not Raf, transforming activity in NIH3T3 cells (Okazaki et al, 1996;Peterson et al, 1996). Second, although constitutively activated Ral alone does not cause transformed foci, one study reported that its co-expression enhanced Ras transformation, whereas dominant negative Ral impaired Ras focus-forming activity (Urano et al, 1996).…”

Section: Ras Mediates Its Actions Through Interaction With Multiple Ementioning

confidence: 99%

Increasing complexity of Ras signaling

et al. 1998

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The initial discovery that ras genes endowed retroviruses with potent carcinogenic properties and the subsequent determination that mutated ras genes were present in a wide variety of human cancers, prompted a strong suspicion that the growth-promoting actions of mutated Ras proteins contribute to their aberrant regulation of growth stimulatory signaling pathways. In 1993, a remarkable convergence of experimental observations from genetic analyses of Drosophila, S. cerevisiae and C. elegans as well as biochemical and biological studies in mammalian cells came together to de®ne a clear role for Ras in signal transduction. What emerged was an elegant linear signaling pathway where Ras functions as a relay switch that is positioned downstream of cell surface receptor tyrosine kinases and upstream of a cytoplasmic cascade of kinases that included the mitogen-activated protein kinases (MAPKs). Activated MAPKs in turn regulated the activities of nuclear transcription factors. Thus, a signaling cascade where every component between the cell surface and the nucleus was de®ned and conserved in worms,¯ies and man. This was a remarkable achievement in our e orts to appreciate how the aberrant function of Ras proteins may contribute to the malignant growth properties of the cancer cell. However, the identi®cation of this pathway has proven to be just the beginning, rather than the culmination, of our understanding of Ras in signal transduction. Instead, we now appreciate that this simple linear pathway represents but a minor component of a very complex signaling circuitry. Ras signaling has emerged to involve a complex array of signaling pathways, where cross-talk, feedback loops, branch points and multi-component signaling complexes are recurring themes. The simplest concept of a signaling cascade, where each component simply relays the same message to the next, is clearly not the case. In this review, we summarize our current understanding of Ras signal transduction with an emphasis on new complexities associated with the recognition and/or activation of cellular e ectors, and the diverse array of signaling pathways mediated by interaction between Ras and Ras-subfamily proteins with multiple e ectors.

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“…To make the glutathione S-transferase-Ral binding domain of RalBP1 (GST-RalBD), cDNA covering amino acids 391-499 of rat RalBP1 (23) was PCRamplified with specific primers harboring the BamHI site at 5Ј terminus and the EcoRI site at 3Ј terminus and cloned into pGEX4T-1 (Amersham Biosciences). pCGN-HA-RalB, pCGN-RalB G23V , pCGNRalB S28N , pBJ-Myc-RalBP1, pBJ-Myc-RalBP1-(364 -647), pBJ-HA-POB1 were as described (19,24,25). The 5Ј and 3Ј junctional regions between the insert and the vector of each construct were sequenced to ensure that the inserts were introduced properly.…”

Section: Methodsmentioning

confidence: 99%

Regulation of Endocytosis of Activin Type II Receptors by a Novel PDZ Protein through Ral/Ral-binding Protein 1-dependent Pathway

Matsuzaki¹,

Hanai²,

Kishi³

et al. 2002

Journal of Biological Chemistry

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Using yeast two-hybrid screening, we have identified a mouse Postsynaptic density 95/Discs large/Zona occludens-1 (PDZ) protein that interacts with activin type II receptors (ActRIIs). We named the protein activin receptor-interacting protein 2 (ARIP2). ARIP2 was found to have one PDZ domain in the NH 2 -terminal region and interact specifically with ActRIIs among the receptors for the transforming growth factor ␤ family by the PDZ domain. Interestingly, overexpression of ARIP2 enhances endocytosis of ActRIIs and reduces activin-induced transcription in Chinese hamster ovary K1 cells. In addition, immunofluorescence co-localization studies indicated the direct involvement of ARIP2 in the intracellular translocation of ActRIIs by PDZ domain-mediated interaction. Moreover, we have identified that the COOH-terminal region of ARIP2 interacts with Ralbinding protein 1 (RalBP1). RalBP1 is a potential effector protein of small GTP-binding protein Ral and regulates endocytosis of epidermal growth factor and insulin receptors. The studies using deletion mutants of RalBP1 and constitutively GTP and GDP binding forms of Ral indicate that ARIP2 regulates endocytosis of ActRIIs through the Ral/RalBP1-dependent pathway, and the GDP-GTP exchange of Ral is critical for this regulation.Activin, a member of the TGF-␤ 1 superfamily, has a broad range of physiological activities including hematopoiesis, bone morphogenesis, neurogenesis, and hormone action (1-5). These various actions on cell proliferation, differentiation, and apoptosis are dependent upon target cells. Activin transduces its signal via heteromeric complexes composed of two different serine/threonine kinase receptors, termed type I and type II (6 -8). Upon ligand binding, the type II receptor transphosphorylates and activates the type I receptor kinase at the membrane region. Then, the type I receptor cytoplasmic domain interacts with intracellular signaling molecules, Smads, which regulate transcription of selected genes in a cell-specific manner (9, 10).In the current model, the functions of the ActRIIs are limited to ligand binding, type I receptor recruitment, and transphosphorylation. However, it is speculated that there are specific roles of the ActRIIs in activin signaling. For example, the serine/threonine kinase domains of ActRIIs are constitutively activated, and ActRIIs exist as homooligomers (probably homodimers) even in the absence of ligands (11,12). These data suggest the existence of a strict monitoring mechanism for type II receptor kinase activity. Furthermore, multiple forms of ActRIIs exist; two subtypes of activin type II receptors, ActRIIA and ActRIIB, each of which is encoded by individual genes, are known (13,14). Several alternative splicing variants have also been found in each subtype (14 -16). For example, activin type IIA-N receptor, a splicing product of ActRIIA, is specifically expressed in neural cells and is thought to mediate neuronalspecific activin action. In a previous report, we noted the identification of a PDZ protein called a...

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Synergistic activation of c-fos promoter activity by Raf and Ral GDP dissociation stimulator

Cited by 66 publications

References 28 publications

Ral GTPases Contribute to Regulation of Cyclin D1 through Activation of NF-κB

Ral GTPases Contribute to Regulation of Cyclin D1 through Activation of NF-κB

Increasing complexity of Ras signaling

Regulation of Endocytosis of Activin Type II Receptors by a Novel PDZ Protein through Ral/Ral-binding Protein 1-dependent Pathway

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