Raymond L. Erikson, Ph.D.
American Cancer Society Prof. of Cellular and Developmental Biology
The Biological Laboratories
16 Divinity Ave.
Cambridge, MA 02138
4 postdoctoral fellows, 0 graduate students
The research in the Erikson laboratory is focused on studies of protein kinases required for the completion of cell division. Protein kinases are enzymes that add a phosphate group to other proteins. The addition of the phosphate group usually modifies the function of a protein so that it acts differently than the non-phosphorylated form. Moreover, there are other enzymes that remove the phosphate group, thus the functional changes in the protein are transient, which is important for the timing and orderly progression of events in cell division.
We study an enzyme, called polo-like-kinase that is required for cell division and adds phosphate groups (proteins) to substrates at critical times during cell division. The modified substrates carry out their role and then the phosphate group is removed. We have identified several novel substrates that polo-like-kinase phosphorylates including one in a cell structure called the Golgi that must be modified each time a cell undergoes division (also called mitosis). Other studies have resulted in the identification of sites in polo-like-kinase that are essential for its proper localization. Our studies have also shown that the localization of the enzyme to specific sites in the cell is essential for cell division.
- Lee, K.S., Grenfell, T.Z., Yarm, F.R. and Erikson, R.L.: Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. Proc. Natl. Acad. Sci. USA, 95:9301-9306, 1998.
- Gallina, A., Simoncini, L., Garbelli, S., Percivalle, E., Pedrali-Noy, G., Lee, K.S., Erikson, R.L., Plachter, B., Gerna, G. and Milanesi, G.: Polo-like kinase 1 as a target for human cytomegalovirus pp65 lower matrix protein. J. Virol., 73:1468-78, 1999.
- Lee,K.S., Song, S. and Erikson, R.L.: The polo-box-dependent induction of ectopic septal structures by a mammalian polo kinase, Plk, in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA, 96:14360-14365, 1999.
- Song, S., Grenfell, T. Z., Garfield, S., Erikson, R.L. and Lee, K.S.: Essential function of the polo-box of cdc5 in subcellular localization and induction of cytokinetic structures. Mol. Cell. Biol., 20:286-298, 2000.
- Lin, C.Y., Madsen, M.L., Yarm, F.R., Jang, Y.J., Liu, X., and Erikson, R.L.: Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2. Proc Natl Acad Sci USA, 97:12589-12594, 2000.
- Welch, D.R., Sakamaki, T., Pioquinto, R., Leonard, T.O., Goldberg, S.F., Hon, Q., Erikson, R.L., Rieber, M., Rieber, M.S., Hicks, D.J., Bonventre, J.V., and Alessandrini, A.: Transfection of constitutively active mitogen-activated protein/extracellular signal-regulated kinase kinase confers tumorigenic and metastatic potentials to NIH3T3 cells. Cancer Res., 60:1552-1556, 2000.
- SÄtterlin, C., Lin, C.Y., Feng, Y., Ferris, D.K., Erikson, R.L., and Malhorta, V.: Polo-like kinase is required for the fragmentation of pericentriolar Golgi stacks during mitosis.
- Ma, S., Liu, M.A., Yuan, Y-L.O., and Erikson, R.L.: The serum-inducible kinase is a G1 phase polo-like kinase inhibited by the calcium- and integrin-binding protein CIB .
- Jang, Y.J., Lin, C.Y., and Erikson, R.L.: Regulation of mammaliam polo-like kinase and function of its C-terminal domain (submitted).
- Liu, X., Terada, Y. and Erikson, R.L.: Mammalian polo-like kinase, Plk, is activated by okadaic acid treatment in the absence of Cdc2 activity.
Virology webpage updated 12/02/2009