Barbara J. Thomas, Ph. D.

Laboratory of Biochemistry, Center for Cancer Research, National Cancer Institute, National Institutes of Health

Building 37, Room  6128
37 CONVENT DR MSC 4255
BETHESDA MD 20892-4255

Phone: (301) 435-2814
Fax: 301-402-3095

bthomas@mail.nih.gov

Biography:

Barbara Thomas obtained her Ph.D. from the Department of Genetics and Development at the Columbia University College of Physicians and Surgeons. She received her post-doctoral training in the laboratory of Dr. S. Lawrence Zipursky at the University of California, Los Angeles. Dr. Thomas joined the Laboratory of Biochemistry in 1996.


Research:

The G1 phase of the cell cycle represents a critical stage where cells can respond to extracellular cues either to commit to another round of cell division, to withdraw temporarily from the cell cycle, or to terminally differentiate.  Studies from both yeast and mammalian systems suggest that progression through G1 is regulated in response to extra- and intracellular signals which act directly on the cell cycle machinery.  I am interested in exploring the mechanisms involved in regulating G1 progression in vivo, and the requirement for G1 in the developmental decision to proliferate or to differentiate.  To this end, I have been studying a gene, roughex (rux), that is required to arrest cells in G1 in the developing compound eye of Drosophila.
A striking feature of development in the Drosophila eye is the simultaneous synchronization of cell cycle progression in G1 and the onset of pattern formation mediated by intercellular signaling molecules.  The adult eye of Drosophila develops from a tissue called the eye imaginal disc, which is formed during embryogenesis from a small group of cells that are determined to form eye tissue. These cells proliferate steadily during the first two stages of larval growth; differenitation initiates during the third and final stage of larval development within a physical constriction in the eye disc epithelium called the morphogenetic furrow (MF). The onset of differenitation in the MF is marked by a synchronization in cell cycle progression and arrest in the G1 phase of the cell cycle. Thus, anterior to the MF cells are undifferentiated and cycle asynchronously, while posterior to the MF cells begin to differentiate and undergo a single, synchronous cell division. We have previously shown that rux mutants fail to arrest in G1 in the MF, and instead all cells ectopically re-enter S phase. The loss of G1 leads to subsequent defects in pattern formation and cell fate determination.  This suggests that G1 must be actively established and maintained during development by a pathway that requires rux, and that cell fate determination is dependent on G1 arrest.
The rux locus encodes a polypeptide of 335 amino acids with an N-terminal cyclin-binding motif and a C-terminal bipartite NLS. Previous genetic studies indicated that Rux is required to inhibit the kinase activity associated with the G2 cyclin, Cyclin A (CycA). Molecular experiments indicate that Rux functions by binding to and inhibiting CycA-dependent kinase activity, and may function in part by dissociating the cyclin from its kinase partner. Further, in vivo studies show that CycA protein becomes mislocalized to nucleus and is degraded when Rux is overexpressed. We are currently exploring the idea that Rux may target CycA for destruction in G1 cells.
Interestingly, Rux protein itself is degraded in cells that normally re-enter S phase for a final wave of cell division behind the MF. S phase in higher eukaryotes is marked by the expression and activation of a cyclin complex containing the G1 cyclin, CycE. We have shown that Rux also binds CycE, and we propose that Rux is targeted for destruction by a CycE-dependent kinase activity in cells that re-enter S phase. In support of this notion, the mislocalization and subsequent degradation of CycA resulting from Rux overexpression is reversed in cells that also overexpress CycE. This effect is dependent on four consensus sites for phosphorylation by cyclin-dependent kinases present in the Rux protein and a mutant derivative of Rux lacking these sites is stabilized in S phase cells. Interestingly, the CycA-binding-defective version of Rux is also stable in S phase cells, suggesting that this site may also mediate binding to CycE.
A large-scale screen to identify new dominant suppressers of rux has identified a number of novel loci as well as the Drosophila patched (ptc) gene. Ptc functions in the Hedgehog signaling cascade, suggesting that this approach will be useful to identify genes that are required for regulating cell cycle progression in response to developmental signals. The high degree of conservation of cell cycle components between species makes it likely that many of the pathways for regulating cell cycle progression during development will be conserved during evolution.


Recent Publications:

  1. Avedisov SN, Krasnoselskaya I, Mortin M, Thomas BJ.  Roughex mediates G1 arrest through a physical association with Cyclin A. Mol Cell Biol.  2000; 20: 8220-29.
  2. Thomas BJ, and Wassarman DA.  A fly's eye view of biologyTrends Genet.  1999; 15: 184-90.
  3. Thomas BJ, Dong X, Zavitz K, Lane ME, Weigmann K, Finley R, Brent R, Lehner C, Zipursky SL. roughex down-regulates G2 cyclins in G1. Genes Dev 1997; 11: 1289-1298.
  4. Dong X, Zavitz KH, Thomas BJ, Lin M, Campbell S, Zipursky S L. Control of G1 in the developing Drosophila eye: rca1 regulates cyclin A. Genes Dev 1997;11: 94-105.

I also have a listing on the Drosophila Interest Group web site.


Last revised on June 6, 2001, by Zoraida S. Villadiego


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