Athens by Sound

Architecture is not only that which is built. Architecture is made up of different aspects, both material and immaterial. The atmosphere, the sounds, the smells, the possibility of interaction between human bodies: these all constitute characteristics of space, characteristics that are assuming an increasing importance within architectural research worldwide. Within this field of thought about “Architecture Beyond Building”, we focus on one particular non-material spatial phenomenon that lies ‘beyond the built’: sound. We have created, thus, an interactive sonic map of Athens, which presents, in an unexpected way, fragments of the atmosphere of the city. What would a non-visual map look like? What would it feel like if you wandered within a forest of headphones, playing sounds from different places in Athens? How would it feel if you found yourself in a ‘map’ that only appeared when you walked in it? What would it be like if the map only appeared when you invited one more person to be with you? The Greek pavilion addresses these questions through an atmospheric interactive ‘game’, presenting fragments of sounds and visual sequences of Athens. The visitor recreates the space around him through his own presence and movement. The map appears only where he walks, and/or when he invites one more person to sit next to him. The bodies of the visitors react with one another and with the space itself, creating a dynamic, changing field. This walk in the pavilion takes you “out there”, through invisible Athens. The pavilion brings forth the aspects of architecture that are ‘beyond the material’: the ‘beyond the built’, the almost unreachable, elusive aspects of space, such as sound, non-visual senses, atmosphere. It challenges, thus, the limits of architecture, the limits of what can be mapped and re-located and what cannot. An edited collection by A. Karandinou, C. Achtypi, S. Giamarelos, including texts by: Ιntothepill, Katie Lloyd Thomas, Martin Parker, Panayiotis Tournikiotis, Mark Wigley, Dorian Wiszniewski, Leslie Kavanaugh, Stephen Cairns, Jonathan Hill, Vassilis Ganiatsas, Anastasios Kotsiopoulos, Constance Classen, Stavros Stavrides, Ole Bouman, William Mitchell, Richard Coyne, Neil Spiller, Kas Oosterhuis, Nora Schueler, Zissis Kotionis, Stelarc, Andreas Angelidakis, Aristide Antonas, Slavoj Žižek, Nikolaos Laskaris, Argyris Rokas, Andreas Kourkoulas, John Peponis, Yorgos Ioannou, Yorgos Tzirtzilakis, Konstantinos Vita, Dionyssis Kapsalis, United Visual Artists, Platon Rivellis, and Dimitris Filippidis. Contributors to the Greek National Participation to the 11th International Architecture Exhibition La Biennale di Venezia "Out there. Architecture beyond building" (2008) Organised by: Hellenic Ministry of Culture [yppo.gr] General Directorate of Modern Culture Directorate of Visual Arts Department for the Promotion of Contemporary Art Curators: Anastasia Karandinou Christina Achtypi Stylianos Giamarelos Video works by Intothepill net [intothepill.net] Artists: Yiannis Grigoriadis Yiannis Isidorou Lina Theodorou Sound Recording / Sound Design Dimitris Miyakis [movement.gr] Vangelis Lympouridis Exhibition Graphics / Catalogue Design Company [company-london.com] Design and Implementation of interactive environment 2monochannels [2monochannels.com] Audiovisual and interactive systems design / acoustic design / construction supervision Iraklis Lampropoulos Giorgos Lampropoulos Software programming Vassilis Boukis Electronic subsystem design Michail Kritsotakis Electrical Design Giorgos Satolias Interconnection of interactive elements Vangelis Lympouridis [inter-axions.com] Dimitris Miyakis Light design L+DG lighting architects [lightingdg.com] Thomas Gravanis Christina Frangeti Construction Gavrilos Michalis [gavrilos.gr] Digital printing Polichromo [polichromo.com] Translations Rachel Howard Nikos Masourides Catalogue photographs Intothepill – Internet video platform Catalogue published by futura publications Marketing communication Chryssa Vrouzi Communication associate Katerina Stamidi Photographer Cathy Cunliffe [cathycunliffeΑΤgmail.com] For their financial and material support for the Greek participation at the 11th International Exhibition of Architecture, La Biennale di Venezia, we express our deepest thanks to the sponsors: Alexander S. Onassis Public Benefit Foundation [onassis.gr] Akzonobel [akzonobel.com] Carteco - Architectural Materials & Design [carteco.gr] L+DG Lighting Architects [lightingdg.com] Plaisio [plaisio.gr] Polichromo Advertising Applications [polichromo.com] iGuzzini illuminazione [iguzzini.com] Diathlasis Architectural Lighting [diathlasis.gr

A Critical Role for FBXW8 and MAPK in Cyclin D1 Degradation and Cancer Cell Proliferation

Cyclin D1 regulates G1 progression. Its transcriptional regulation is well understood. However, the mechanism underlying cyclin D1 ubiquitination and its subsequent degradation is not yet clear. We report that cyclin D1 undergoes increased degradation in the cytoplasm during S phase in a variety of cancer cells. This is mediated by phosphorylation at Thr286 through the activity of the Ras/Raf/MEK/ERK cascade and the F-box protein FBXW8, which is an E3 ligase. The majority of FBXW8 is expressed in the cytoplasm during G1 and S phase. In contrast, cyclin D1 accumulates in the nucleus during G1 phase and exits into the cytoplasm in S phase. Increased cyclin D1 degradation is linked to association with FBXW8 in the cytoplasm, and enhanced phosphorylation of cyclin D1 through sustained ERK1/2 signaling. Depletion of FBXW8 caused a significant accumulation of cyclin D1, as well as sequestration of CDK1 in the cytoplasm. This resulted in a severe reduction of cell proliferation. These effects could be rescued by constitutive nuclear expression of cyclin D1-T286A. Thus, FBXW8 plays an essential role in cancer cell proliferation through proteolysis of cyclin D1. It may present new opportunities to develop therapies targeting destruction of cyclin D1 or its regulator E3 ligase selectively

Epstein-Barr Virus Nuclear Antigen 3C Facilitates G1-S Transition by Stabilizing and Enhancing the Function of Cyclin D1

EBNA3C, one of the Epstein-Barr virus (EBV)-encoded latent antigens, is essential for primary B-cell transformation. Cyclin D1, a key regulator of G1 to S phase progression, is tightly associated and aberrantly expressed in numerous human cancers. Previously, EBNA3C was shown to bind to Cyclin D1 in vitro along with Cyclin A and Cyclin E. In the present study, we provide evidence which demonstrates that EBNA3C forms a complex with Cyclin D1 in human cells. Detailed mapping experiments show that a small N-terminal region which lies between amino acids 130–160 of EBNA3C binds to two different sites of Cyclin D1- the N-terminal pRb binding domain (residues 1–50), and C-terminal domain (residues 171–240), known to regulate Cyclin D1 stability. Cyclin D1 is short-lived and ubiquitin-mediated proteasomal degradation has been targeted as a means of therapeutic intervention. Here, we show that EBNA3C stabilizes Cyclin D1 through inhibition of its poly-ubiquitination, and also increases its nuclear localization by blocking GSK3β activity. We further show that EBNA3C enhances the kinase activity of Cyclin D1/CDK6 which enables subsequent ubiquitination and degradation of pRb. EBNA3C together with Cyclin D1-CDK6 complex also efficiently nullifies the inhibitory effect of pRb on cell growth. Moreover, an sh-RNA based strategy for knock-down of both cyclin D1 and EBNA3C genes in EBV transformed lymphoblastoid cell lines (LCLs) shows a significant reduction in cell-growth. Based on these results, we propose that EBNA3C can stabilize as well as enhance the functional activity of Cyclin D1 thereby facilitating the G1-S transition in EBV transformed lymphoblastoid cell lines

Systems

© 2002 SAGE Publications. All rights reserved. Not for commercial use or unauthorized distribution. CHILDCARE: an intelligent collaborative environment for out-of-hospital child healthcare G. Ganiatsas, K. Starida

Integration of Caenorhabditis elegans MAPK pathways mediating immunity and stress resistance by MEK-1 MAPK kinase and VHP-1 MAPK phosphatase

The p38 and JNK classes of mitogen-activated protein kinases (MAPKs) have evolutionarily conserved roles in the control of cellular responses to microbial and abiotic stresses. The mechanisms by which crosstalk between distinct p38 and c-Jun N-terminal kinase (JNK) MAPK pathways occurs with resultant integration of signaling information have been difficult to establish, particularly in the context of whole organism physiology. In Caenorhabditis elegans a PMK-1 p38 MAPK pathway is required for resistance to bacterial infection, and a KGB-1 JNK-like MAPK pathway has recently been shown to mediate resistance to heavy metal stress. Here, we show that two components of the KGB-1 pathway, MEK-1 MAPK kinase (MAPKK), a homolog of mammalian MKK7, and VHP-1 MAPK phosphatase (MKP), a homolog of mammalian MKP7, also regulate pathogen resistance through the modulation of PMK-1 activity. The regulation of p38 and JNK-like MAPK pathways mediating immunity and heavy metal stress by common MAPKK and MKP signaling components suggests pivotal roles for MEK-1 and VHP-1 in the integration of diverse stress signals contributing to pathogen resistance in C. elegans. In addition, these data point to mechanisms in multicellular organisms by which signals transduced by distinct MAPK pathways may be subject to physiological integration at the level of regulation of MAPK activity by MAPKKs and MKPs

p38 Mitogen-Activated Protein Kinase-Dependent Activation of Protein Phosphatases 1 and 2A Inhibits MEK1 and MEK2 Activity and Collagenase 1 (MMP-1) Gene Expression

Degradation of collagenous extracellular matrix by collagenase 1 (also known as matrix metalloproteinase 1 [MMP-1]) plays a role in the pathogenesis of various destructive disorders, such as rheumatoid arthritis, chronic ulcers, and tumor invasion and metastasis. Here, we have investigated the role of distinct mitogen-activated protein kinase (MAPK) pathways in the regulation of MMP-1 gene expression. The activation of the extracellular signal-regulated kinase 1 (ERK1)/ERK2 (designated ERK1,2) pathway by oncogenic Ras, constitutively active Raf-1, or phorbol ester resulted in potent stimulation of MMP-1 promoter activity and mRNA expression. In contrast, activation of stress-activated c-Jun N-terminal kinase and p38 pathways by expression of constitutively active mutants of Rac, transforming growth factor β-activated kinase 1 (TAK1), MAPK kinase 3 (MKK3), or MKK6 or by treatment with arsenite or anisomycin did not alone markedly enhance MMP-1 promoter activity. Constitutively active MKK6 augmented Raf-1-mediated activation of the MMP-1 promoter, whereas active mutants of TAK1 and MKK3b potently inhibited the stimulatory effect of Raf-1. Activation of p38 MAPK by arsenite also potently abrogated stimulation of MMP-1 gene expression by constitutively active Ras and Raf-1 and by phorbol ester. Specific activation of p38α by adenovirus-delivered constitutively active MKK3b resulted in potent inhibition of the activity of ERK1,2 and its upstream activator MEK1,2. Furthermore, arsenite prevented phorbol ester-induced phosphorylation of ERK1,2 kinase-MEK1,2, and this effect was dependent on p38-mediated activation of protein phosphatase 1 (PP1) and PP2A. These results provide evidence that activation of signaling cascade MKK3-MKK3b→p38α blocks the ERK1,2 pathway at the level of MEK1,2 via PP1-PP2A and inhibits the activation of MMP-1 gene expression