Museum for all - More than a Slogan?

Der Internationale Museumstag 2020 stand unter dem Motto „Das Museum für alle – Museen für Vielfalt und Inklusion“. Doch wer ist alle? Im Mittelpunkt des Beitrags steht eine Zielgruppe, die nicht nur in archäologischen und kulturhistorischen Museen in Deutschland kaum einbezogen wird – Menschen mit psychischen, neurologischen oder kognitiven Beeinträchtigungen. Der Artikel ist aus der Praxis heraus entstanden und als Werkstattbericht zu verstehen. Anhand von drei Praxisbeispielen aus dem Kulturhistorischen Museum Magdeburg werden Stolpersteine und Gelingensfaktoren aufgezeigt. Darüber hinaus sollen mögliche Gründe für die Marginalisierung dieser Zielgruppen in deutschen Museen identifiziert werden. Im Fokus steht dabei die personale Vermittlung für Gruppen. Selbstverständlich ebenfalls sehr wichtig, aber nicht Gegenstand des Artikels, sind Angebote für Individualbesucher*innen. Darüber hinaus ist die Gruppe der Menschen mit Beeinträchtigungen sehr vielfältig, sodass zwar allgemeine Empfehlungen abgeleitet werden können, aber immer auch individuelle Bedürfnisse zu berücksichtigen sind.The motto of the International Museum Day 2020 was “The Museum for Everyone – Museums for Diversity and Inclusion.” But who is everyone? The focus of this article is a target group that is hardly included in archaeological and cultural history museums in Germany – people with psychological, neurological or cognitive disabilities. The article grows out of practice and should be understood as a workshop report. Using three practical examples from the Magdeburg Cultural History Museum, obstacles and success factors are highlighted. In addition, possible reasons for the marginalization of these target groups in German museums are to be identified. The article focuses on programs designed for groups. Also very important are of course offers for individual visitors. In addition it needs to be kept in mind that the group of people with disabilities is very diverse. Therefore, general recommendations may be derived from the experiences presented in this paper, but individual needs always must be taken into account

Bildungswert und Living History

van Norden J. Bildungswert und Living History. In: Eschwege K, Köster G, Lippok J, Kulturhistorisches Museum Magdeburg, eds. Living History - Lernen im historischen Gewand. Jubiläumsschrift zum 25-jährigen Bestehen der historischen Spielstadt "Megedeborch" im Kulturhistorischen Museum Magdeburg. Magdeburger Museumsschriften. Vol 22. 1st ed. Magdeburg: Kulturhistorisches Museum Magdeburg; 2023: 25-31

Dynamic subcellular localization of the mono-ADP-ribosyltransferase ARTD10 and interaction with the ubiquitin receptor p62

BACKGROUND: ADP-ribosylation is a posttranslational modification catalyzed in cells by ADP-ribosyltransferases (ARTD or PARP enzymes). The ARTD family consists of 17 members. Some ARTDs modify their substrates by adding ADP-ribose in an iterative process, thereby synthesizing ADP-ribose polymers, the best-studied example being ARTD1/PARP1. Other ARTDs appear to mono-ADP-ribosylate their substrates and are unable to form polymers. The founding member of this latter subclass is ARTD10/PARP10, which we identified as an interaction partner of the nuclear oncoprotein MYC. Biochemically ARTD10 uses substrate-assisted catalysis to modify its substrates. Our previous studies indicated that ARTD10 may shuttle between the nuclear and cytoplasmic compartments. We have now addressed this in more detail. RESULTS: We have characterized the subcellular localization of ARTD10 using live-cell imaging techniques. ARTD10 shuttles between the cytoplasmic and nuclear compartments. When nuclear, ARTD10 can interact with MYC as measured by bimolecular fluorescence complementation. The shuttling is controlled by a Crm1-dependent nuclear export sequence and a central ARTD10 region that promotes nuclear localization. The latter lacks a classical nuclear localization sequence and does not promote full nuclear localization. Rather this non-conventional nuclear localization sequence results in an equal distribution of ARTD10 between the cytoplasmic and the nuclear compartments. ARTD10 forms discrete and dynamic bodies primarily in the cytoplasm but also in the nucleus. These contain poly-ubiquitin and co-localize in part with structures containing the poly-ubiquitin receptor p62/SQSTM1. The co-localization depends on the ubiquitin-associated domain of p62, which mediates interaction with poly-ubiquitin. CONCLUSIONS: Our findings demonstrate that ARTD10 is a highly dynamic protein. It shuttles between the nuclear and cytosolic compartments dependent on a classical nuclear export sequence and a domain that mediates nuclear uptake. Moreover ARTD10 forms discrete bodies that exchange subunits rapidly. These bodies associate at least in part with the poly-ubiquitin receptor p62. Because this protein is involved in the uptake of cargo into autophagosomes, our results suggest a link between the formation of ARTD10 bodies and autophagy. LAY ABSTRACT: Post-translational modifications refer to changes in the chemical appearance of proteins and occur, as the name implies, after proteins have been synthesized. These modifications frequently affect the behavior of proteins, including alterations in their activity or their subcellular localization. One of these modifications is the addition of ADP-ribose to a substrate from the cofactor NAD(+). The enzymes responsible for this reaction are ADP-ribosyltransferases (ARTDs or previously named PARPs). Presently we know very little about the role of mono-ADP-ribosylation of proteins that occurs in cells. We identified ARTD10, a mono-ADP-ribosyltransferase, as an interaction partner of the oncoprotein MYC. In this study we have analyzed how ARTD10 moves within a cell. By using different live-cell imaging technologies that allow us to follow the position of ARTD10 molecules over time, we found that ARTD10 shuttles constantly in and out of the nucleus. In the cytosol ARTD10 forms distinct structures or bodies that themselves are moving within the cell and that exchange ARTD10 subunits rapidly. We have identified the regions within ARTD10 that are required for these movements. Moreover we defined these bodies as structures that interact with p62. This protein is known to play a role in bringing other proteins to a structure referred to as the autophagosome, which is involved in eliminating debris in cells. Thus our work suggests that ARTD10 might be involved in and is regulated by ADP-riboslyation autophagosomal processes