The experimental strategy of his research includes molecular and genetic analysis of cell division genes using Drosophila melanogaster, and biochemical analysis of protein function using biophysical approaches.

Two major projects are currently moving forward in the lab. First, they are characterizing new genes involved in the regulation of centrosome replication in animal cells. Second, using biophysical tools, they are analyzing the mechanism of inhibition of a mitotic microtubule motor protein by a novel anti-cancer drug.

The research goal is to understand how the mitotic spindle checkpoint disengages to permit anaphase chromosome movement. They have found that the microtubule motor protein, dynein, is instrumental in switching the spindle checkpoint off at metaphase. Moreover, dynein complex, including other known checkpoint proteins such as Rod and ZW10, can be seen streaming off of kinetochores during prometaphase. Understanding how the dynamics of kinetochore-associated dynein regulates the spindle checkpoint remains a major interest of the lab. Click here to download the Wojcik lab's latest checkpoint-related paper.

Dr. Wojcik and coworkers have recently uncovered a mutation in the slimb gene that results in over-replication of centrosomes in dividing cells. Extra centrosomes are commonly seen in cancer cells, where they have been shown to contribute to genetic instability. The biochemical pathway that regulates centrosome duplication in animal cells is poorly understood, with few known components. Therefore, the lab is pursuing a genetic and biochemical analysis of the role of slimb in centrosome duplication as a steppingstone to elucidating the regulation of centrosome function. Slimb is a targeting factor for the protein degradation pathway. Their working hypothesis proposes that loss of Slimb function results in the failure to properly degrade a key centrosome regulatory component. In turn, this results in the over-replication of this enigmatic organelle during the cell cycle. Work is currently underway in this laboratory to identify Slimb target proteins that operate in the centrosome replication pathway. Click here to download the Wojcik lab's latest centrosome-related paper.

In a new line of investigation, the lab is investigating the biochemical mechanism of mechanotransduction in motor proteins, such as kinesin. Using state of the art biochemical techniques, including Fourier-transform infrared spectroscopy, they are gaining insight as to how kinesin proteins catalyze ATP hydrolysis and use this energy to move along microtubule tracks in the cell. Click here to download the Wojcik lab's recent Eg5 kinesin paper.

 

Recent Publications

Wojcik EJ, Dalrymple NA, Alford SR, Walker RA, Kim S. Disparity in allosteric interactions of monastrol with Eg5 in the presence of ADP and ATP: a difference FT-IR investigation. Biochemistry Aug 10;43(31):9939-49 (2004)  

Basto R, Scaerou F, Mische S, Wojcik EJ, Lefebvre C, Gomes R, Hays T, Karess R. In vivo dynamics of the rough deal checkpoint protein during Drosophila mitosis. Curr Biol. Jan 6;14(1):56-61 (2004)

Wojcik EJ, Basto R, Serr M, Scaerou F, Karess R, Hays T. Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein. Nat Cell Biol. Nov;3(11):1001-7 (2001)

Wojcik EJ, Glover DM, Hays TS. The SCF ubiquitin ligase protein slimb regulates centrosome duplication in Drosophila. Curr Biol. Sep 21;10(18):1131-4 (2000)  

Robinson JT, Wojcik EJ, Sanders MA, McGrail M, Hays TS. Cytoplasmic dynein is required for the nuclear attachment and migration of centrosomes during mitosis in Drosophila. J Cell Biol. Aug 9;146(3):597-608 (1999)