Vida Praitis

 

Fax: 
641-269-4984
Associate Professor of Biology
On-Campus Address: 
Science 1820
Education / Degrees: 
B.A., Swarthmore College
Ph.D. 1995, Massachusetts Inst. of Technology; Biology
Post-doctoral training, Molecular Genetics and Cell Biology, University of Chicago, Illinois, 1995-2001
Publications: 
TitleURLSynopsis
SMA-1 is an apically-localized β-spectrin essential for epithelial cell sheet morphogenesis in C. elegansPraitis, V., Ciccone, E.* and Austin J. (2005). SMA-1 is an apically-localized β-spectrin essential for epithelial cell sheet morphogenesis in C. elegans. Developmental Biology 283:157-170.
Creation of Low-copy Integrated Transgenic Lines in C. elegansPraitis, V., Casey, E*., Collar, D*., and Austin, J. (2001). Creation of Low-copy Integrated Transgenic Lines in C. elegans. Genetics 157:1217-1226.
sma-1 encodes a βH-spectrin homolog required for Caenorhabditis elegans morphogenesisMcKeown C. †, Praitis, V. †, and Austin, J. (1998). sma-1 encodes a βH-spectrin homolog required for Caenorhabditis elegans morphogenesis. Development 125:2087-2098.
A codon change in β-tubulin which drastically affects microtubile structure in Drosophila fails to produce a significant phenotype in S. CerevisaePraitis, V., Katz, W. and Solomon, F. (1991). A codon change in β-tubulin which drastically affects microtubile structure in Drosophila fails to produce a significant phenotype in S. Cerevisae. Molecular and Cell. Biology 11:4726-4731.
Methods for studying the cytoskeleton in yeast. in The Cytoskeleton: a Practical ApproachSolomon, F., Connell, L., Praitis, V., Weinstein, B., and Kirkpatrick, D. (1991) Methods for studying the cytoskeleton in yeast. in The Cytoskeleton: a Practical Approach. Editors K.L. Carraway and C.A.C. Carraway. IRL Press, Oxford.
A genetic analysis of microtubule assembly and function in yeastSolomon, F., Guenette, S., Kirkpatrick, D., Praitis, V., Weinstein, B. and Archer, J. (1992) A genetic analysis of microtubule assembly and function in yeast. in Chromosome Segregation and Aneuploidy, Editors B. Vig, Springer-Verlag, Berlin. pp.199-210.
Courses Taught: 
Biology 150: Introduction to Biological Inquiry, "Cell Fate: Calvin or Hobbes?"
Biology 251: Molecules, Cells, and Organisms, with Lab
Biology 345: Advanced Genetics, with Lab
Biology 355: Developmental Genetics, with Lab
Biology 370: Topics in Cell Biology
Biology 295: Special Topic, "Bioinformatics"
Biology 395: Advanced Special Topic, "Animal Development"
Biology 395: Advanced Special Topic, "Mechanisms of Developmental Biology"
Biological Chemistry 262L: Introduction to Biological Chemistry Lab
Tutorial: "Trouble Helix: How Modern Genetics Has Changed Our View of Humanity"
Primary Academic Interest: 
Cell & Molecular Biology

For Publications: * Undergraduate co-authors; † Both authors contributed equally to this work.

Cell & Molecular Biology

Directed changes in the shape of epithelial sheets are required to create many of the major tissues in animals, including the intestinal system, kidneys, lungs, and skin. Although our understanding of epithelial sheet morphogenesis has advanced in recent years, we still have much to learn about this fundamental developmental process. Research in my laboratory focuses on understanding at a cellular and molecular level the mechanisms by which epithelial sheets change shape during their development. I have chosen to study epithelial shape change in the model system C. elegans because it occurs in a simple, predictable fashion, allowing us to characterize this process at a genetic, cellular and organismal level. During C. elegans embryogenesis epithelial cells elongate over four-fold, driven by dramatic changes in the organization of all major cytoskeletal structures. Because the forces that drive cell shape change act on the apical membrane skeleton of epithelial cells, this structure must be both strong and dynamic. One protein that localizes to the apical membrane skeleton and is required for epithelial cell shape change is SMA-1 spectrin, an ortholog of Drosophila H-spectrin and human V-spectrin. sma-1 mutants fail to elongate properly during embryogenesis. Our analysis of sma-1mutants has shown that SMA-1 has two discreet functions in epithelial elongation: to maintain the association of actin at the apical membrane and to preserve changes in the organization of the apical membrane. Ongoing research aims to better understand these roles for SMA-1 spectrin and to identify the proteins that interact with SMA-1 in epithelial morphogenesis. As a result of these studies, we will gain fundamental insights into how changes in the apical membrane skeleton contribute to epithelial cell elongation, a process fundamental to the development of all animals.

Biological Chemistry

Chair of the Biological Chemistry major, 2007-2010.