Supporting Catholic Education through Effective School/University Partnerships: Two Models from the 2012 Catholic Higher Education Collaborative Conference

This essay was developed from a panel presentation by Henk and Maney, as well as other key professional colleagues, delivered at the 2012 CHEC Conference. The essay describes the formation and initial work of a consortium of five institutions of higher education in the greater Milwaukee area, including Alverno College, Cardinal Stritch University, Marian University, Marquette University, and Mount Mary College

Supporting Catholic Education through Effective School/University Partnerships: Two Models from the 2012 Catholic Higher Education Collaborative Conference

The following article contains two essays based on presentations to the 2012 CHEC conference on Catholic school governance held at Marquette University in October 2012. The essays outline two models of deep collaboration between Catholic institutions of higher education and Catholic K-12 schools designed to support and foster improvements in Catholic education. The first essay, “Higher Education Working Together to Help Catholic Schools: The Greater Milwaukee Catholic Education Consortium,” written by William A. Henk and Jennifer A. Maney, provides an overview of the Greater Milwaukee Catholic Education Consortium (GMCEC), an ongoing collaborative effort between the archdiocese of Milwaukee and the region’s five Catholic colleges and universities. Building a strong partnership among multiple institutions has allowed the GMCEC to leverage the individual strengths of each member institution to provide a variety of supports to Catholic schools within the diocese. The essay outlines the early history of the collaboration, the key areas of engagement, and some emerging outcomes and ongoing challenges associated with efforts to scaffold supports for diocesan schools. Following this essay are excerpts from a panel discussion among the five presidents of the institutions of higher education that are part of the consortium

Deficiency of the B cell-activating factor receptor results in limited CD169+ macrophage function during viral infection

The B cell-activating factor (BAFF) is critical for B cell development and humoral immunity in mice and humans. While the role of BAFF in B cells has been widely described, its role in innate immunity remains unknown. Using BAFF receptor (BAFFR)-deficient mice, we characterized BAFFR-related innate and adaptive immune functions following infection with vesicular stomatitis virus (VSV) and lymphocytic choriomeningitis virus (LCMV).Weidentified a critical role for BAFFR signaling in the generation and maintenance of the CD169+ macrophage compartment. Consequently, Baffr-/- mice exhibited limited induction of innate type I interferon production after viral infection. Lack of BAFFR signaling reduced virus amplification and presentation following viral infection, resulting in highly reduced antiviral adaptive immune responses. As a consequence, BAFFR-deficient mice showed exacerbated and fatal disease after viral infection. Mechanistically, transient lack of B cells in Baffr-/- animals resulted in limited lymphotoxin expression, which is critical for maintenance of CD169+ cells. In conclusion, BAFFR signaling affects both innate and adaptive immune activation during viral infections. © 2015, American Society for Microbiology

EB1 Targets to Kinetochores with Attached, Polymerizing Microtubules

Microtubule polymerization dynamics at kinetochores is coupled to chromosome movements, but its regulation there is poorly understood. The plus end tracking protein EB1 is required both for regulating microtubule dynamics and for maintaining a euploid genome. To address the role of EB1 in aneuploidy, we visualized its targeting in mitotic PtK1 cells. Fluorescent EB1, which localized to polymerizing ends of astral and spindle microtubules, was used to track their polymerization. EB1 also associated with a subset of attached kinetochores in late prometaphase and metaphase, and rarely in anaphase. Localization occurred in a narrow crescent, concave toward the centromere, consistent with targeting to the microtubule plus end–kinetochore interface. EB1 did not localize to kinetochores lacking attached kinetochore microtubules in prophase or early prometaphase, or upon nocodazole treatment. By time lapse, EB1 specifically targeted to kinetochores moving antipoleward, coupled to microtubule plus end polymerization, and not during plus end depolymerization. It localized independently of spindle bipolarity, the spindle checkpoint, and dynein/dynactin function. EB1 is the first protein whose targeting reflects kinetochore directionality, unlike other plus end tracking proteins that show enhanced kinetochore binding in the absence of microtubules. Our results suggest EB1 may modulate kinetochore microtubule polymerization and/or attachment