Kathleen A. Gallo

 

        gallo@psl.msu.edu
        Phone: (517) 355-6475, ext. 1289
        Home Department: Physiology
        Home Page: Physiology

 

 

 

Assistant Professor. B.S. 1984, Catholic University of America; Ph.D. 1992, Harvard University.
Postdoctoral Researcher, 1992-1995 Genentech.


     We are interested in signaling pathways that control the growth of mammalian cells. In particular, we are interested in studying the roles of novel protein kinases using the techniques of cell biology, molecular biology, and biochemistry. We have recently identified a novel protein serine/threonine kinase in human cells called SPRK, for SH3 domain-containing proline-rich kinase. SPRK bears hallmarks of an important signaling molecule, including a kinase catalytic domain SPRK, a src-homology 3 (SH3) domain, leucine/isoleucine “zipper” motifs, a potential nuclear localization signal, and a large carboxyl terminal region rich in proline, serine, and threonine residues. SPRK is the first serine/threonine kinase that contains an SH3 domain. SPRK is readily phosphorylated in response to serum and growth factors. Overexpression of SPRK morphologically transforms fibroblast cell lines that can then form tumors in nude mice. These data suggest that SPRK is involved in a signaling pathway that regulates growth. We are determining the effects of the overexpression of SPRK on important signaling pathways, such as those of the mitogen-activated and related protein kinases. For instance, SPRK is capable of phosphorylating and activating SEK-1, the protein kinase activator of Jun kinase. Our primary goal is to elucidate the role of SPRK and other protein kinases in the signal transduction pathways that regulate cell growth.


Selected Publications

Vacratsis, P.O., and K.A. Gallo. 2000. Zipper-Mediated Oligomerization of the Serine/Threonine Kinase   SPRK/MLK-3 Is Not Required for Its Activation by the GTPase Cdc42 But Is Necessary for Its Activation of the JNK Pathway. J Biol Chem. 2000 Jun 21 [epub ahead of print]
 
Bock, B.C., Vacratsis, P.O., Qamirani E.,and K.A. Gallo. 2000. Cdc42-induced activation of the mixed-lineage kinase SPRK in vivo. Requirement of the Cdc42/Rac interactive binding motif and changes in phosphorylation.  J. Biol Chem. 275: 14231-41.

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