Office: Life Sciences Building 283
Deepa Dabir is an Assistant Professor of Biology at Loyola Marymount University.
University of Pennsylvania: Ph.D., Biology 2006
University of Pune, India: M.S., Biotechnology 2000
St. Xavier's College, Mumbai: B.Sc., Life Sciences/Biochemistry 1998
Areas of Expertise (8)
Industry Expertise (2)
Mia40 serves as an electron sink in the Mia40-Erv1 import pathwayJournal of Biological Chemistry
A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation.
A Small Molecule Inhibitor of Redox-Regulated Protein Translocation into MitochondriaDevelopmental Cell
The mitochondrial disulfide relay system of Mia40 and Erv1/ALR facilitates import of the small translocase of the inner membrane (Tim) proteins and cysteine-rich proteins. A chemical screen identified small molecules that inhibit Erv1 oxidase activity, thereby facilitating dissection of the disulfide relay system in yeast and vertebrate mitochondria.
Meiosis I Arrest Abnormalities Lead to Severe Oligozoospermia in Meiosis 1 Arresting Protein (M1ap)-Deficient MiceBiology of Reproduction
Meiosis 1 arresting protein (M1ap) is a novel vertebrate gene expressed exclusively in germ cells of the embryonic ovary and the adult testis. In male mice, M1ap expression, which is present from spermatogonia to secondary spermatocytes, is evolutionarily conserved and has a specific spatial and temporal pattern suggestive of a role during germ cell development. To test its function mice deficient in M1ap were created.
Role of Twin Cys-Xaa(9)-Cys Motif Cysteines in Mitochondrial Import of the Cytochrome c Oxidase Biogenesis Factor Cmc1Journal of Biological Chemistry
The Mia40 import pathway facilitates the import and oxidative folding of cysteine-rich protein substrates into the mitochondrial intermembrane space. Here we describe the in vitro and in organello oxidative folding of Cmc1, a twin CX(9)C-containing substrate, which contains an unpaired cysteine.
Role of astrocytes in the pathogenesis of tauopathiesDissertations available from ProQuest
Filamentous tau inclusions in neurons, astrocytes and oligodendrocytes are the neuropathological hallmark of both sporadic and familial tauopathies. The identification of pathogenic tau mutations in familial tsuopathies, termed frontotemporal dementia with parkinsonism linked to chromosome-17, provide unequivocal support for the hypothesis that defects in the tau gene are sufficient alone to cause neurodegeneration.