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Lynn Cooley, Ph.D.

Professor of Genetics and Cell Biology
Director of Combined Program in the Biological & Biomedical Sciences

Cooley lab website
FlyTrap website
Phone: (203) 785-5067
Lab: (203) 737-2953/2675
Fax: (203) 785-6333
e-mail: lynn.cooley@yale.edu

Department of Genetics
Yale University School of Medicine
333 Cedar Street
PO Box 208005
New Haven, CT 06520-8005

<Courier Address>
333 Cedar Street, SHM I-363
New Haven, CT 06510-3206



Our research is focused on the cell biology of Drosophila oogenesis during which maternal products for directing early embryogenesis are deposited in oocytes. We have relied on female sterile mutants in which the movement of cytoplasm from nurse cells into oocytes via ring canals is disrupted. These mutants have led to the discovery that egg chamber development requires precise control of cytoskeletal structures in both the nurse cells and oocytes.

Ring canals. Several cytoplasm transport mutants revealed protein components of intercellular junctions called ring canals that connect nurse cells to each other and to the oocyte. We have found that growth of ring canals during development requires actin dynamics similar to what occurs at the leading edge of motile cells. We are continuing to characterize germline ring canal cell biology, as well as studying the function and prevalence of ring canals in somatic cells.

Oocyte microtubule dynamics. One mutant we are studying has an oocyte-specific phenotype in which cell shape is unstable and the movement of ooplasm is perturbed. Both phenotypes correlate with abnormal microtubule distribution in growing oocytes. The cloning of the affected gene is nearing completion.

Flytrap. In a new approach to discovering proteins required for oogenesis, we are carrying out a large-scale protein- trapping screen in which fusions between Green Fluorescent Protein and endogenous proteins are generated (see http://flytrap.med.yale.edu). The cellular and subcellular patterns of GFP-fusion protein expression provide instant insight into protein function. Since the GFP coding sequence is introduced by a transposon, we can identify the trapped protein by sequencing genomic DNA flanking the insertion site. The expression patterns along with gene sequences provide a powerful starting point for genetic and functional analyses of proteins used during development.

 

Figures A and B

Figure A:  Stage 10 egg chamber. Actin associated with plasma membranes and ring canals is labeled in red and nuclei are blue.
Figure B:  A single ring canal embedded in surrounding plasma membrane. Actin is red and HtsRC, a ring canal-specific protein, is green.

 

Selected Publications
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Kelso RJ, Buszczak M, Quinones AT, Castiblanco C, Mazzalupo S, Cooley L. (2004)  Flytrap, a database documenting a GFP protein-trap insertion screen in Drosophila melanogaster. Nucl Acids Res. 32: D418-420.  

Sokol NS, Cooley L. (2003)  Drosophila Filamin is required for follicle cell motility during oogenesis. Devel Biol. 260: 260-272.  

Kelso RJ, Hudson AM, Cooley L. (2002)  Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation. J Cell Biol. 156: 703-713.  

Hudson AM, Cooley L. (2002)  A subset of dynamic actin rearrangements in Drosophila requires the Arp2/3 complex. J Cell Biol. 156: 677-87.  

Buszczak M, Segraves WA, Cooley L. (2002)  Loss of midway, encoding a Drosophila acyl coenzyme A: diacylglycerol acyltransferase, leads to premature egg chamber apoptosis. Genetics 160: 1511-1518.  

Hudson AM, Cooley L. (2002)  Understanding the function of actin-binding proteins through genetic analysis of Drosophila oogenesis. Annu Rev Genet. 36: 455-488.  






Lynn Cooley