Virtual Biology: Teaching Histology in the Age of Facebook

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/154528/1/fsb2027002001.pd

Duplications in nomenclature

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/62822/1/389539a0.pd

Introduction to the special collection on biomedical education

The recent COVID‐19 crisis has posed a severe challenge to the educational system worldwide. Hearing from many of our colleagues, how they together with their students approached and overcame these hurdles, is inspiring. Educators in many biomedical fields, who thought that they require in‐person teacher‐to‐learner contacts to carry out their teaching missions, found ways to continue. That is not to say that these new, mainly remote ways of teaching are always better or equivalent to traditional approaches, but they are providing an alternative that gets the job done. Most importantly, novel avenues of teaching are being found and the educational process continues. To quote a statement that is often falsely attributed to Charles Darwin, “It is not the most intellectual of species that survives; it is not the strongest that survives; but the species that survives is the one that is able best to adapt and adjust to the changing environment in which it finds itself.

Introduction to the special collection on biomedical education

The recent COVID‐19 crisis has posed a severe challenge to the educational system worldwide. Hearing from many of our colleagues, how they together with their students approached and overcame these hurdles, is inspiring. Educators in many biomedical fields, who thought that they require in‐person teacher‐to‐learner contacts to carry out their teaching missions, found ways to continue. That is not to say that these new, mainly remote ways of teaching are always better or equivalent to traditional approaches, but they are providing an alternative that gets the job done. Most importantly, novel avenues of teaching are being found and the educational process continues. To quote a statement that is often falsely attributed to Charles Darwin, “It is not the most intellectual of species that survives; it is not the strongest that survives; but the species that survives is the one that is able best to adapt and adjust to the changing environment in which it finds itself.

The virtual microscopy database—sharing digital microscope images for research and education

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/146335/1/ase1774_am.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/146335/2/ase1774.pd

Drosophila contactin, a homolog of vertebrate contactin, is required for septate junction organization and paracellular barrier function

Septate junctions (SJs) in epithelial and neuronal cells play an important role in the formation and maintenance of charge and size selective barriers. They form the basis for the ensheathment of nerve fibers i

Cross-Species Analyses Identify the BNIP-2 and Cdc42GAP Homology (BCH) Domain as a Distinct Functional Subclass of the CRAL_TRIO/Sec14 Superfamily

The CRAL_TRIO protein domain, which is unique to the Sec14 protein superfamily, binds to a diverse set of small lipophilic ligands. Similar domains are found in a range of different proteins including neurofibromatosis type-1, a Ras GTPase-activating Protein (RasGAP) and Rho guanine nucleotide exchange factors (RhoGEFs). Proteins containing this structural protein domain exhibit a low sequence similarity and ligand specificity while maintaining an overall characteristic three-dimensional structure. We have previously demonstrated that the BNIP-2 and Cdc42GAP Homology (BCH) protein domain, which shares a low sequence homology with the CRAL_TRIO domain, can serve as a regulatory scaffold that binds to Rho, RhoGEFs and RhoGAPs to control various cell signalling processes. In this work, we investigate 175 BCH domain-containing proteins from a wide range of different organisms. A phylogenetic analysis with ∼100 CRAL_TRIO and similar domains from eight representative species indicates a clear distinction of BCH-containing proteins as a novel subclass within the CRAL_TRIO/Sec14 superfamily. BCH-containing proteins contain a hallmark sequence motif R(R/K)h(R/K)(R/K)NL(R/K)xhhhhHPs (‘h’ is large and hydrophobic residue and ‘s’ is small and weekly polar residue) and can be further subdivided into three unique subtypes associated with BNIP-2-N, macro- and RhoGAP-type protein domains. A previously unknown group of genes encoding ‘BCH-only’ domains is also identified in plants and arthropod species. Based on an analysis of their gene-structure and their protein domain context we hypothesize that BCH domain-containing genes evolved through gene duplication, intron insertions and domain swapping events. Furthermore, we explore the point of divergence between BCH and CRAL-TRIO proteins in relation to their ability to bind small GTPases, GAPs and GEFs and lipid ligands. Our study suggests a need for a more extensive analysis of previously uncharacterized BCH, ‘BCH-like’ and CRAL_TRIO-containing proteins and their significance in regulating signaling events involving small GTPases