Associate Professor in Molecular Cell & Developmental Biology
Main Office: PAT 241
Alternate Office: PAT 235
The University of Texas at Austin
1 University Station C0930
Austin, TX 78712-1095
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We are interested in defining the molecular basis of the lysosomal disorder known as the Chediak-Higashi Syndrome. This disease is caused by mutations in a very large gene and result in the loss of a large protein known as Lyst. The size and low abundance of this protein have impaired the detailed analysis of its function and how its absence leads to the dysfunction of lysosomes in CHS patients.
We have established a simple model system to study the molecular function of Lyst and closely related proteins in the organism Dictyostelium discoideum. We have shown that the loss of a similar protein in this organism results in the same lysosomal defect. We are currently using the wide array of molecular tools available in this model system to dissect the function of Lyst-related proteins. We hope to use this as a starting point to understand better the human disease and design potential therapies.
We are also interested in understanding how eukaryotic cells accomplish the last stage of the cell cycle: cytokinesis. We have identified several proteins important for cytokinesis and have generated knockout mutants lacking these proteins. We then analyze the phenotype of these mutants using a variety of cell biological techniques including imaging
of GFP-labeled proteins. One of these proteins called LvsA plays a role in membrane traffic, while another called INCENP binds to chromosomes and microtubules. The analysis of proteins like these will help delineate the molecular mechanisms involved in cell division.
|2007||Kypri, E., Schmauch, C., Maniak, M., and De Lozanne, A. , The BEACH protein LvsB is localized on postlysosomes and limits their fusion with other lysosomal compartments. , Traffic 8:774-783 view.|
|2007||Chen, Q., Lakshmikanth, G. S., Spudich, J. A., and De Lozanne, A. , Localization of DdINCENP at the cleavage furrow depends on Kif12, an MKLP1 homologue, and on its interaction with the actin cytoskeleton. , Mol. Biol. Cell 18:3366-3374 view.|
|2006||Malchow D, Lusche DF, Schlatterer C, De Lozanne A, Muller-Taubenberger A, The contractile vacuole in Ca2+-regulation in Dictyostelium: its essential function for cAMP-induced Ca2+-influx, BMC Developmental Biology 6:31-38 view.|
|2006||Chen, Q., Li, H. and De Lozanne, A. , Contractile ring-independent localization of DdINCENP, a protein essential for spindle stability and cytokinesis, Mol. Biol. Cell 17:779-788 view.|
|2004||Wu, W. , Yanik, J., Siano, M. and De Lozanne, A., Structure-Function Analysis of the Beach Protein L vs A, Traffic 5 :346-355 view.|
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