ABSTRACT
Online learning has the potential to enhance open and equitable access to medical education resources globally. Conversely, there are also concerns that it can perpetuate and exacerbate digital inequalities between developed (global North) and developing (global South) countries. In this article, we describe the historical lack of representation of the global South in the design of online medical education, as well as the resulting consequences and potential solutions. We compare the Northern and Southern views of online learning in medical education and identify the different types of barriers to its adoption. We describe how socioeconomic disparities and the historical dominance of the global North over the global South have led to systemic digital inequalities in the design and implementation of online learning in education generally, and in medical education particularly. The lack of representation of global South voices hinders the development of digital learning solutions relevant to local contexts, therefore limiting their effectiveness and sustainability. Thus, we propose approaches to build more equitable partnerships by soliciting local input and local expertise. Further, we discuss the need to maintain local relevance while setting global standards. Overall, we hope to inform and guide the development of more equitable and accessible online education training for a diverse global population.
ABSTRACT
Student engagement is important for classroom management but can be challenging to monitor, especially in large virtual classes. After lessons were moved online due to COVID-19 measures, instructors were unable to directly observe student behaviours, impacting their ability to gauge engagement levels and adjust the pace of delivery for optimal learning outcomes. A widget called MOSH, for Move On/Stay Here, was developed for students to indicate whether they wished to "move on" from or "stay here" on a point of discussion in real-time. By increasing acknowledgment of and response to student feedback, we aimed to enhance the student-instructor feedback loop.
ABSTRACT
BACKGROUND: As digital learning becomes more prevalent and important in health professions education, learning technologists play increasingly central roles in designing and delivering learning materials. However, little is understood about the process by which learning technologists have integrated into the existing teaching and learning ecosystem, and it seems that they remain marginal and undervalued. Our aim in this paper was therefore to examine the process of interprofessional co-development of course materials as experienced by educators and learning technologists. METHODS: Our approach was qualitative, using individual semi-structured interviews (conducted between July 2021 to May 2022) to explore the working relationship between faculty and learning technologists. Transcripts were analysed abductively. RESULTS: We found that the attitudes of both faculty and learning technologists towards collaborating to drive digital adoption in health professions education fell into two main themes: "embrace" and "replace" - and "conflict", which we present as a third theme. Our results revealed that faculty did not take an active and agentic role in developing their digital practices in respect of education delivery. Learning technologists positioned themselves as a resource to support faculty's knowledge and skill gap in digital competence. There was an obvious power differential between the two groups: learning technologists lacked agency and seemed in the position of servants to faculty masters. This created barriers to effective collaboration. CONCLUSIONS: By examining the process of co-development of course materials by faculty and learning technologists, we open up a space to examine the social, relational and organisational complexities associated with interprofessional collaboration in digital health professions education. Our study also has important implications for guiding educational policy to better position learning technologists to effectively collaborate with faculty and realise the potential of digital health professions education.
Subject(s)
Interprofessional Relations , Learning , Humans , Attitude , Educational Status , FacultyABSTRACT
In the digital age, experts in digital learning tools, or learning technologists (LTs), play an increasingly important role in the creation and delivery of online learning in health professions education. However, their expertise in the selection, curation and implementation of digital tools is often underutilized due to imbalanced relationships and lack of effective collaboration between faculty and LTs. Here, we describe how the co-production model can be applied to build equal and synergistic partnerships between faculty and LTs, so as to optimize the use of digital affordances and enhance online learning.
Subject(s)
Education, Distance , Humans , Faculty , Learning , Health EducationABSTRACT
A correction to this article has been published and is linked from the HTML version of this article.
ABSTRACT
Contractile adherens junctions support cell-cell adhesion, epithelial integrity, and morphogenesis. Much effort has been devoted to understanding how contractility is established; however, less is known about whether contractility can be actively downregulated at junctions nor what function this might serve. We now identify such an inhibitory pathway that is mediated by the cytoskeletal scaffold, cortactin. Mutations of cortactin that prevent its tyrosine phosphorylation downregulate RhoA signaling and compromise the ability of epithelial cells to generate a contractile zonula adherens. This is mediated by the RhoA antagonist, SRGAP1. We further demonstrate that this mechanism is co-opted by hepatocyte growth factor to promote junctional relaxation and motility in epithelial collectives. Together, our findings identify a novel function of cortactin as a regulator of RhoA signaling that can be utilized by morphogenetic regulators for the active downregulation of junctional contractility.Epithelial cell-cell adhesions are contractile junctions, but whether contractility can be down-regulated is not known. Here the authors report how tyrosine dephosphorylation of the cytoskeletal scaffold, cortactin, recruits the RhoA antagonist SRGAP1 to relax adherens junctions in response to HGF.
Subject(s)
Adherens Junctions/metabolism , Cortactin/metabolism , GTPase-Activating Proteins/metabolism , Hepatocyte Growth Factor/metabolism , Tyrosine/metabolism , rhoA GTP-Binding Protein/metabolism , Caco-2 Cells , Cell Adhesion , Cortactin/genetics , Cytoskeleton , Down-Regulation , Epithelial Cells/metabolism , HEK293 Cells , Humans , Mutation , Phosphorylation , Signal TransductionABSTRACT
The mechanical properties of the microenvironment play a large role in influencing cellular behavior. In particular, the tradeoff between substrate viscosity and elasticity on collective cell migration by adherent cells is highly physiologically relevant, but remains poorly understood. To investigate the specific effects of viscous substrates, we plated epithelial monolayers onto polydimethylsiloxane substrata with a range of viscosities and elasticities. We found that on viscoelastic substrates the monolayers underwent rapid and coordinated movement to generate cell-free areas. To understand the molecular mechanism of this coordinated movement, we imaged various structural and signaling proteins at cell-cell and cell-matrix junctions. Through quantitative image analysis of monolayer disruption and subcellular protein redistribution, we show that the mechanosensor protein, vinculin, is necessary and sufficient for this viscous response, during which it is lost from focal adhesions and recruited by the cadherin complex to intercellular junctions. In addition, the viscous response is dependent upon and enhanced by actomyosin contractility. Our results implicate vinculin translocation in a molecular switching mechanism that senses substrate viscoelasticity and associates with actomyosin contractility.
Subject(s)
Cell Movement/physiology , Epithelial Cells/physiology , Vinculin/metabolism , Acrylic Resins , Animals , Culture Media , Dogs , Epithelial Cells/cytology , Focal Adhesions/metabolism , Madin Darby Canine Kidney Cells , Mice , Microscopy, Confocal , Models, Biological , Viscoelastic SubstancesABSTRACT
In this study we sought to identify how contractility at adherens junctions influences apoptotic cell extrusion. We first found that the generation of effective contractility at steady-state junctions entails a process of architectural reorganization whereby filaments that are initially generated as poorly organized networks of short bundles are then converted into co-aligned perijunctional bundles. Reorganization requires coronin 1B, which is recruited to junctions by E-cadherin adhesion and is necessary to establish contractile tension at the zonula adherens. When cells undergo apoptosis within an epithelial monolayer, coronin 1B is also recruited to the junctional cortex at the apoptotic/neighbor cell interface in an E-cadherin-dependent fashion to support actin architectural reorganization, contractility, and extrusion. We propose that contractile stress transmitted from the apoptotic cell through E-cadherin adhesions elicits a mechanosensitive response in neighbor cells that is necessary for the morphogenetic event of apoptotic extrusion to occur.
Subject(s)
Actins/metabolism , Adherens Junctions/metabolism , Apoptosis/physiology , Microfilament Proteins/metabolism , Muscle Contraction/physiology , Actin Cytoskeleton/metabolism , Adherens Junctions/physiology , Caco-2 Cells , Cadherins/genetics , Cadherins/metabolism , Cell Line, Tumor , Epithelial Cells/metabolism , Humans , Microfilament Proteins/genetics , RNA Interference , RNA, Small Interfering/geneticsABSTRACT
Epithelial junctions are fundamental determinants of tissue organization, subject to regulation by tyrosine phosphorylation. Homophilic binding of E-cadherin activates tyrosine kinases, such as Src, that control junctional integrity. Protein tyrosine phosphatases (PTPs) also contribute to cadherin-based adhesion and signaling, but little is known about their specific identity or functions at epithelial junctions. Here, we report that the receptor PTP RPTPα (human gene name PTPRA) is recruited to epithelial adherens junctions at the time of cell-cell contact, where it is in molecular proximity to E-cadherin. RPTPα is required for appropriate cadherin-dependent adhesion and for cyst architecture in three-dimensional culture. Loss of RPTPα impairs adherens junction integrity, as manifested by defective E-cadherin accumulation and peri-junctional F-actin density. These effects correlate with a role for RPTPα in cellular (c)-Src activation at sites of E-cadherin engagement. Mechanistically, RPTPα is required for appropriate tyrosine phosphorylation of cortactin, a major Src substrate and a cytoskeletal actin organizer. Expression of a phosphomimetic cortactin mutant in RPTPα-depleted cells partially rescues F-actin and E-cadherin accumulation at intercellular contacts. These findings indicate that RPTPα controls cadherin-mediated signaling by linking homophilic E-cadherin engagement to cortactin tyrosine phosphorylation through c-Src.
Subject(s)
Adherens Junctions/metabolism , Cadherins/metabolism , Epithelial Cells/physiology , Receptor-Like Protein Tyrosine Phosphatases, Class 4/metabolism , src-Family Kinases/metabolism , Actins/metabolism , Adherens Junctions/genetics , CSK Tyrosine-Protein Kinase , Caco-2 Cells , Cell Adhesion/genetics , Cortactin/genetics , Cortactin/metabolism , HEK293 Cells , Humans , Mutation/genetics , Organ Culture Techniques , Organogenesis/genetics , Phosphorylation/genetics , Protein Transport , RNA, Small Interfering/genetics , Receptor-Like Protein Tyrosine Phosphatases, Class 4/genetics , Signal Transduction/geneticsABSTRACT
Cadherin junctions arise from the integrated action of cell adhesion, signaling, and the cytoskeleton. At the zonula adherens (ZA), a WAVE2-Arp2/3 actin nucleation apparatus is necessary for junctional tension and integrity. But how this is coordinated with cadherin adhesion is not known. We now identify cortactin as a key scaffold for actin regulation at the ZA, which localizes to the ZA through influences from both E-cadherin and N-WASP. Using cell-free protein expression and fluorescent single molecule coincidence assays, we demonstrate that cortactin binds directly to the cadherin cytoplasmic tail. However, its concentration with cadherin at the apical ZA also requires N-WASP. Cortactin is known to bind Arp2/3 directly (Weed, S. A., Karginov, A. V., Schafer, D. A., Weaver, A. M., Kinley, A. W., Cooper, J. A., and Parsons, J. T. (2000) J. Cell Biol. 151, 29-40). We further show that cortactin can directly bind WAVE2, as well as Arp2/3, and both these interactions are necessary for actin assembly at the ZA. We propose that cortactin serves as a platform that integrates regulators of junctional actin assembly at the ZA.
Subject(s)
Actin-Related Protein 2/metabolism , Actin-Related Protein 3/metabolism , Adherens Junctions/metabolism , Cortactin/metabolism , Epithelium/metabolism , Wiskott-Aldrich Syndrome Protein Family/metabolism , Actins/metabolism , Antigens, CD , Caco-2 Cells , Cadherins/metabolism , Cell Adhesion , Cell-Free System , Cytoskeleton/metabolism , Green Fluorescent Proteins/metabolism , Humans , Image Processing, Computer-Assisted , Microscopy, Confocal , Microscopy, Fluorescence , Spectrometry, Fluorescence , Wiskott-Aldrich Syndrome Protein, Neuronal/metabolismABSTRACT
α-Catenin exists as part of the cadherin-catenin adhesion complex as well as in a cytoplasmic pool. However, which of these pools is responsible for its biological impact remains controversial. A structure-function analysis in Drosophila melanogaster illuminates how the molecular properties of α-catenin translate into functional outcomes in an intact organism.
Subject(s)
Actin Cytoskeleton/metabolism , Actins/metabolism , Cadherins/metabolism , Cell Adhesion/physiology , Drosophila melanogaster/metabolism , alpha Catenin/metabolism , beta Catenin/metabolism , AnimalsABSTRACT
Alternative RNA splicing in multicellular organisms is regulated by a large group of proteins of mainly unknown origin. To predict the functions of these proteins, classification of their domains at the sequence and structural level is necessary. We have focused on four groups of splicing regulators, the heterogeneous nuclear ribonucleoprotein (hnRNP), serine-arginine (SR), embryonic lethal, abnormal vision (ELAV)-like, and CUG-BP and ETR-like factor (CELF) proteins, that show increasing diversity among metazoa. Sequence and phylogenetic analyses were used to obtain a broader understanding of their evolutionary relationships. Surprisingly, when we characterised sequence similarities across full-length sequences and conserved domains of ten metazoan species, we found some hnRNPs were more closely related to SR, ELAV-like and CELF proteins than to other hnRNPs. Phylogenetic analyses and the distribution of the RRM domains suggest that these proteins diversified before the last common ancestor of the metazoans studied here through domain acquisition and duplication to create genes of mixed evolutionary origin. We propose that these proteins were derived independently rather than through the expansion of a single protein family. Our results highlight inconsistencies in the current classification system for these regulators, which does not adequately reflect their evolutionary relationships, and suggests that a domain-based classification scheme may have more utility.
Subject(s)
Eukaryota/genetics , Evolution, Molecular , RNA Splicing , RNA-Binding Proteins/genetics , Amino Acid Motifs , Amino Acid Sequence , Animals , CCAAT-Enhancer-Binding Protein-delta/chemistry , CCAAT-Enhancer-Binding Protein-delta/genetics , Cluster Analysis , Computational Biology , Consensus Sequence , ELAV Proteins/chemistry , ELAV Proteins/genetics , Heterogeneous-Nuclear Ribonucleoproteins/genetics , Humans , Molecular Sequence Data , Nuclear Proteins/genetics , Phylogeny , Sequence Alignment , Serine-Arginine Splicing FactorsABSTRACT
The epithelial zonula adherens (ZA) is a specialized adhesive junction where actin dynamics and myosin-driven contractility coincide. The junctional cytoskeleton is enriched in myosin II, which generates contractile force to support junctional tension. It is also enriched in dynamic actin filaments, which are replenished by ongoing actin assembly. In this study we sought to pursue the relationship between actin assembly and junctional contractility. We demonstrate that WAVE2-Arp2/3 is a major nucleator of actin assembly at the ZA and likely acts in response to junctional Rac signaling. Furthermore, WAVE2-Arp2/3 is necessary for junctional integrity and contractile tension at the ZA. Maneuvers that disrupt the function of either WAVE2 or Arp2/3 reduced junctional tension and compromised the ability of cells to buffer side-to-side forces acting on the ZA. WAVE2-Arp2/3 disruption depleted junctions of both myosin IIA and IIB, suggesting that dynamic actin assembly may support junctional tension by facilitating the local recruitment of myosin.