Kathleen A. Gallo
Professor
  • Ph.D. 1992, Harvard University
  • Postdoctoral Researcher 1992-1995, Genentech

gallok@msu.edu
4180 Biomedical & Physical Sci
Michigan State University
East Lansing, MI 48824-1319
Office: 517-355-6475 ext 1159
Lab: 517-355-6475 ext 1378

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Kathleen A. Gallo

Research Interests

Protein phosphorylation is a dynamic and reversible event essential to the proper functioning of physiological processes, including cell proliferation and programmed cell death. Because protein phosphorylation is a regulatory event, it follows that the protein kinases that catalyze phosphorylation, should themselves be subject to regulation. The improper regulation of protein kinases has been implicated in many human pathologies, including cancer. The overall goal of the Gallo Laboratory is to understand the molecular basis by which protein kinases and their signaling pathways are regulated in normal cells and in cancer.

The mixed-lineage kinases (MLKs) are a family of serine/threonine kinases that function as mitogen-activated protein kinase kinase kinases (MKKKs) to activate the JNK pathway. In some experimental settings, the MLKs may also activate the ERK, p38 MAPK and nuclear factor Kappa B (NF-kappa B) pathways. The MLKs have garnered attention as important mediators of apoptosis, particularly in neuronal cells.

Our lab is using MLK3 as a paradigm to study the mixed lineage family of protein kinases.MORE

Recent Publications

Gallo KA. (2006) Targeting HSP90 to halt neurodegeneration. Chem Biol. 13(2):115-6. Link to reprint

Mata IF, Wedemeyer WJ, Farrer MJ, Taylor JP, Gallo KA. (2006) LRRK2 in Parkinson's disease: protein domains and functional insights. Trends Neurosci. 29(5):286-93. Review. Link to reprint

Schachter KA, Du Y, Lin A, Gallo KA. (2006) Dynamic positive feedback phosphorylation of mixed lineage kinase 3 by JNK reversibly regulates its distribution to Triton-soluble domains. J Biol Chem. 281(28):19134-44. Link to reprint

Du Y, Bock BC, Schachter KA, Chao M, Gallo KA. (2005) Cdc42 induces activation loop phosphorylation and membrane targeting of MLK3. J Biol Chem. Dec 30;280(52):42984-93. Link to reprint

Zhang H, Wu W, Du Y, Santos SJ, Conrad SE, Watson JT, Grammatikakis N, Gallo KA. (2004) Hsp90/p50cdc37 is required for mixed-lineage kinase (MLK) 3 signaling. J Biol Chem. 279(19):19457-63. Link to reprint

Gallo, K. A. and Johnson, G.L. (2002) Signalling: Mixed-lineage kinase control of JNK and p38 MAPK pathways. Nature Reviews Molecular Cell Biology 3: 663-72. Link to reprint

Vacratsis, P. O., Phinney, B. S., Gage, D. A., and Gallo, K. A. (2002) Identification of in vivo phosphorylation sites of MLK3 by mass spectrometry and phosphopeptide mapping. Biochemistry 41, 5613-24. Link to reprint

Parameswaran, N., C.S. Hall, B.C. Bock, H.V. Sparks, K.A. Gallo, and W.S. Spielman (2002) Mixed lineage kinase 3 inhibits phorbol myristoyl acetate-induced DNA synthesis but not osteopontin expression in rat mesangial cells. Molecular and Cellular Biochem 241: 37-43 MORE