Programme of the 21st European Conference on Eye Movements

About ECEM ECEM was initiated by Rudolf Groner (Bern), Dieter Heller (Bayreuth at the time) and Henk Breimer (Tilburg) in the 198 to provide a forum for an interdisciplinary group of scientists interested in eye movements. Since the inaugural meeting in Bern, the conference has been held every two years in different venues across Europe until 2021, when it was planned to take place in Leicester but was cancelled due to the COVID pandemic. It was decided to hold the meeting in Leicester in August 2022 instead, and as an in person meeting rather than an online or hybrid event. Incidentally, the present meeting is the third time the conference has come to the English East Midlands, now in Leicester following previous meetings in the neighbouring cities of Derby and Nottingham. The sites of previous ECEMs and webpages can be found here

The application of eye-tracking in music research

Though eye-tracking is typically a methodology applied in the visual research domain, recent studies suggest its relevance in the context of music research. There exists a community of researchers interested in this kind of research from varied disciplinary backgrounds scattered across the globe. Therefore, in August 2017, an international conference was held at the Max Planck Institute for Empirical Aesthetics in Frankfurt, Germany, to bring this research community together. The conference was dedicated to the topic of music and eye-tracking, asking the question: what do eye movements, pupil dilation, and blinking activity tell us about musical processing? This special issue is constituted of top-scoring research from the conference and spans a range of music-related topics. From tracking the gaze of performers in musical trios to basic research on how eye movements are affected by background music, the contents of this special issue highlight a variety of experimental approaches and possible applications of eye-tracking in music research

RUNX/AML and C/EBP factors regulate CD11a integrin expression in myeloid cells through overlapping regulatory elements

10 Figures. The publication costs of this article were defrayed in part by page charge payment. Therefore, and solely to indicate this fact, this article is hereby marked ‘‘advertisement’’ in accordance with 18 U.S.C. section 1734.The CD11a/CD18 (leukocyte function-associated antigen 1 [LFA-1]) integrin mediates critical leukocyte adhesive interactions during immune and inflammatory responses. The CD11a promoter directs CD11a/CD18 integrin expression, and its activity in lymphoid cells depends on a functional RUNX1/AML-1–binding site (AML-110) within the MS7 sequence. We now report that MS7 contains a C/EBP-binding site (C/EBP-100), which overlaps with AML-110 and is bound by C/EBP factors in myeloid cells. C/EBP and RUNX/AML factors compete for binding to their respective cognate elements and bind to the CD11a promoter MS7 sequence in a cell lineage- and differentiation-dependent manner. In myeloid cells MS7 is primarily recognized by C/EBP factors in proliferating cells whereas RUNX/AML factors (especially RUNX3/AML-2) bind to MS7 in differentiated cells. RUNX3/AML-2 binding to the CD11a promoter correlates with increased RUNX3/AML-2 protein levels and enhanced CD11a/CD18 cell surface expression. The relevance of the AML-110 element is underscored by the ability of AML-1/ETO to inhibit CD11a promoter activity, thus explaining the low CD11a/CD18 expression in t(8;21)–containing myeloid leukemia cells. Therefore, the expression of the CD11a/CD18 integrin in myeloid cells is determined through the differential occupancy of the CD11a proximal promoter by transcription factors implicated in the pathogenesis of myeloid leukemia.From the Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain; Clínica Universitaria, Universidad de Navarra, Spain; Institute of Human Genetics, Aarhus, Denmark; Hospital Universitario Gregorio Maranón, Madrid, Spain; University of Colorado Health Sciences Center, Denver; and Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot Israel. Supported by grants 08.3/0026/2000.1 from Comunidad Auto´noma de Madrid, 01/0063-01 from Fondo de Investigaciones Sanitarias, and SAF2002-04615- C02-01 from Ministerio de Ciencia y Tecnología (A.L.C.). We gratefully acknowledge Drs Ana Aranda and Aurora Sánchez-Pacheco for their very generous help with ChIP assays.Peer reviewe

Localization of the ~12 kDa Mr discrepancy in gel migration of the mouse glucocorticoid receptor to the major phosphorylated cyanogen bromide fragment in the transactivating domain

The intact wild-type mouse glucocorticoid receptor has a theoretical molecular weight of ~86 kDa based on amino acid sequence, but on SDS-polyacrylamide gel electrophoresis it migrates as a protein of ~98 kDa. It is not known where the unusual primary structure or covalent modification responsible for this anomalous migration is located within the amino acid chain. In the course of examining the pattern of fragmentation of 32P-labeled glucocorticoid receptors from Chinese hamster ovary (CHO) cells containing amplified mouse receptor cDNA, we have found a localized region in the amino-terminal half of the receptor that accounts for this anomalous behavior. Cyanogen bromide treatment of the intact receptor produces a 23.4 kDa (theoretical) fragment consisting of residues 108-324 and containing all of the identified phosphorylated serines within the receptor. We find that the only large resolvable 32P-labeled receptor fragment produced after complete cyanogen bromide cleavage of intact receptors migrates with an apparent molecular weight of ~35 kDa. Because the apparent difference between the theoretical and the experimentally observed molecular weights of this cyanogen bromide fragment is essentially the same as the difference between the theoretical and experimental molecular weights of the intact mouse glucocorticoid receptor, we propose that some feature lying within this fragment accounts for slower migration. Although the existence of an additional phosphorylation site lying within the 15 kDa tryptic receptor fragment containing the DNA-binding domain has been contested, we also demonstrate that this fragment of the mouse glucocorticoid receptor is phosphorylated in vivo upon incubation of CHO cells in growth medium containing [32P]orthophosphate.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/30424/1/0000045.pd

Ultrathin Oxide Films by Atomic Layer Deposition on Graphene

In this paper, a method is presented to create and characterize mechanically robust, free standing, ultrathin, oxide films with controlled, nanometer-scale thickness using Atomic Layer Deposition (ALD) on graphene. Aluminum oxide films were deposited onto suspended graphene membranes using ALD. Subsequent etching of the graphene left pure aluminum oxide films only a few atoms in thickness. A pressurized blister test was used to determine that these ultrathin films have a Young's modulus of 154 \pm 13 GPa. This Young's modulus is comparable to much thicker alumina ALD films. This behavior indicates that these ultrathin two-dimensional films have excellent mechanical integrity. The films are also impermeable to standard gases suggesting they are pinhole-free. These continuous ultrathin films are expected to enable new applications in fields such as thin film coatings, membranes and flexible electronics.Comment: Nano Letters (just accepted

RUNX/AML and C/EBP factors regulate CD11a integrin expression in myeloid cells through overlapping regulatory elements

The CD11a/CD18 (leukocyte functionassociated antigen 1 [LFA-1]) integrin mediates critical leukocyte adhesive interactions during immune and inflammatory responses. The CD11a promoter directs CD11a/CD18 integrin expression, and its activity in lymphoid cells depends on a functional RUNX1/AML-1–binding site (AML-110) within the MS7 sequence. We now report that MS7 contains a C/EBPbinding site (C/EBP-100), which overlaps with AML-110 and is bound by C/EBP factors in myeloid cells. C/EBP and RUNX/ AML factors compete for binding to their respective cognate elements and bind to the CD11a promoter MS7 sequence in a cell lineage- and differentiation-dependent manner. In myeloid cells MS7 is primarily recognized by C/EBP factors in proliferating cells whereas RUNX/AMLfactors (especially RUNX3/AML-2) bind to MS7 in differentiated cells. RUNX3/AML-2 binding to the CD11a promoter correlates with increased RUNX3/AML-2 protein levels and enhanced CD11a/CD18 cell surface expression. The relevance of the AML-110 element is underscored by the ability of AML-1/ETO to inhibit CD11a promoter activity, thus explaining the low CD11a/CD18 expression in t(8;21)–containing myeloid leukemia cells. Therefore, the expression of the CD11a/CD18 integrin in myeloid cells is determined through the differential occupancy of the CD11a proximal promoter by transcription factors implicated in the pathogenesis of myeloid leukemia