Research Interests
The organizational paradigm for MAPK activation cascades comes from studies on signal transduction in S. cerevisiae. The prototype enzymes for each of the three kinase families comprising the core enzymes of these conserved cascades were identified through their role in pheromone-induced mating differentiation in this organism. Subsequent genetic and biochemical analyses from our laboratory in collaboration with others defined the enzymatic activities of the core enzymes and revealed their order of function. The core enzymes of this cascade have stable interactions with each other and Ste5, a so-called scaffold protein. One role of the scaffold is to insulate the module and prevent illegitimate crosstalk between the mating differentiation and other MAPK modules. The associations with Ste5 may also be an important part of each activation step, but how the associations affect activities of the core enzymes is not yet known.

Our research continues to exploit well-defined MAPK activation pathways of S. cerevisiae to uncover the molecular mechanisms that govern protein-protein associations within a given module and to learn how these associations influence the mechanics of signal transmission. We are also interested in defining the mechanisms that allow for coordination of signaling through different pathways within the context of these insular modules. To address these issues we rely on biochemical approaches including phosphoprotein analyses and in vitro phosphorylation assays. We also apply recombinant DNA technology and mutagenesis approaches that allow the generation and analysis of variants with altered regulation or specificity. Given the high degree of conservation that has already been documented for these cascades, it is likely that the regulatory principles uncovered through our studies will be generally applicable.

Publications
Errede, B., Ge, Q-Y. (1996). Feedback regulation of MAP kinase signal pathways. Phil. Trans. R. Soc. Lond. B. 351:143-149.

Baur, M., Esch, R.K., & Errede, B. (1997). Cooperative binding interactions are required for function of the Ty1 sterile responsive element. Mol Cell Biol, 17, 4330-4337.

Buehrer, B.M. & Errede, B. (1997). Coordination of the mating and cell-integrity MAP kinase pathways in Saccharomyces cerevisiae. Mol Cell Biol, 17, 6517-6525.

Chandarlapaty, S. and Errede, B. (1998). Ash1, a daughter cell-specific protein, is required for pseudohyphal growth of Saccharomyces cerevisiae. Mol. Cell. Biol. 18:2884-2891.

Rajavel, M., Philip, B. Buehrer, B.M., Errede, B. & Levin, D.E. (1999) Mid2 is a putative Sensor for Cell Integrity Signaling in Saccharomyces cerevisiae. Mol. Cell. Biol., 19:3969-3976.

E-mail: errede@email.unc.edu
Telephone: (919) 966-3664
FAX: (919) 966-4812
Address: 512A Mary Ellen Jones Bldg, CB# 7260 Chapel Hill, NC
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