个人简介

B.A., California State University - Sacramento, 1991. Ph.D. University of Wisconsin - Madison, 1997. Postdoctoral: University of California, San Francisco, 1997-2001. Honors and Awards: NIH Postdoctoral Fellow, 2000-2001; Damon Runyon Scholar, 2003-2006. At Oregon since 2001.

研究领域

Biochemistry/Molecular Biology/Biophysics

Research in the Prehoda lab focuses on the biochemical processes that allow cells to respond to changes in their environment. Environmental cues, or “signals”, pass across a cell’s plasma membrane and initiate a molecular program that associates a signal with an appropriate response. For example, during development stem cells respond to signals from neighboring cells by undergoing a series of precise divisions that lead to the multitude of tissues and organs in complex organisms. Our research attempts to uncover the molecular programs that control highly regulated events like these, and elucidate the mechanisms of information transfer that comprise them. In many instances, protein-protein interactions underlie the regulation of complex cellular processes. Because protein-protein interactions are critically important for cellular signaling, many signaling proteins contain specialized domains that are responsible for binding target proteins. Figure caption: Structures of PDZ domain complexes involved in stem cell division. On the left, the PDZ from the protein Par-6 is bound to a carboxy-terminal sequence (N and C-terminii of the ligand are labeled). This mode of binding is enforced by a steric mechanism – residues that would extend past the c-terminus would clash with residues from the domain itself. On the right, an internal sequence is shown bound to the Par-6 PDZ domain. This sequence bypasses the carboxy-terminal requirement by taking advantage of plasticity in the PDZ domain. In recent work, we have shown how PDZ protein interaction domains, one of the most common in the human genome, are regulated, and how they specifically bind to carboxy-terminal sequences. We are also studying how interactions between domains in the same protein lead to the complex signaling observed in cells. For example, in the membrane-associated guanylate kinase (MAGUK) family of proteins an intramolecular interaction between an SH3 and GK domain regulates the ability of each domain to bind ligands. Part of our research program involves determining structures of protein complexes using X-ray crystallography or nuclear magnetic resonance. This structural information is complemented by biochemical, biophysical, and cell biological experiments in order to obtain a complete description of the system under study.

近期论文

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Ordered Multisite Phosphorylation of Lethal Giant Larvae by Atypical Protein Kinase C Graybill C, Prehoda KE Biochemistry doi 10.1021 PDF A NudE/14-3-3 Pathway Coordinates Dynein and the Kinesin Khc73 to Position the Mitotic Spindle Lu MS, Prehoda KE Dev Cell 26:369-380 PDF Formin-mediated actin polymerization cooperates with Mud/Dynein during Frizzled/Dishevelled spindle orientation Johnston CA, Manning L, Lu MS, Golub O, Doe CQ, Prehoda KE J Cell Sci doi: 10.1242/​jcs.129544 PDF Microtubules in distress release arrest. Prehoda KE Dev Cell 23:233-4 PDF Partitioning-defective protein 6 (Par-6) activates atypical protein kinase C (aPKC) by pseudosubstrate displacement. Graybill C, Wee B, Atwood SX, Prehoda KE J Biol Chem 287:21003-11 PDF Structure of an Enzyme-Derived Phosphoprotein Recognition Domain Johnston CA, Doe CQ, Prehoda KE PLoS ONE 7:e36014 PDF Inscuteable Regulates the Pins-Mud Spindle Orientation Pathway Mauser JF, Prehoda KE PLoS ONE 7:e29611 PDF Ultrasensitive synthetic protein regulatory networks using mixed decoys Lu M, Mauser JF, Prehoda KE ACS Synthetic Biology PDF Canoe binds RanGTP to promote PinsTPR/Mud-mediated spindle orientation Wee B, Johnston CA, Prehoda KE, Doe CQ J Cell Bio 195:369-376 PDF Conversion of the enzyme guanylate kinase into a mitotic-spindle orienting protein by a single mutation that inhibits GMP-induced closing Johnston CA, Whitney DS, Volkman BF, Doe CQ, Prehoda KE Proc Natl Acad Sci 108:E973-E978 PDF Asymmetric cortical extension shifts cleavage furrow position in Drosophila neuroblasts Connell M, Cabernard C, Ricketson D, Doe CQ, Prehoda KE Mol Biol Cell 22:4220-4226 PDF Robust spindle alignment in Drosophila neuroblasts by ultrasensitive activation of pins. Smith NR, Prehoda KE Mol Cell 43:540-549 PDF Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments Ricketson R, Johnston CA, Prehoda KE Proc Natl Acad Sci PDF The Fz-Dsh Planar Cell Polarity Pathway Induces Oriented Cell Division via Mud/NuMA in Drosophila and Zebrafish Ségalen M, Johnston CA, Martin CA, Dumortier JG, Prehoda KE, David NB, Doe CQ, Bellaïche Y Dev Cell 19:740-52 PDF A spindle-independent cleavage-furrow positioning pathway Cabernard C, Prehoda KE, Doe CQ Nature 467:91-94 PDF Cell polarity: keeping worms LeGaL. Prehoda KE, Bowerman B Curr Biol 15:R646-8 PDF Polarization of Drosophila Neuroblasts During Asymmetric Division Prehoda KE Cold Spring Harbor Perspectives in Biology PDF Allosteric Control of Regulated Scaffolding in Membrane Associated Guanylate Kinases Marcette J, Hood IV, Johnston CA, Doe CQ, Prehoda KE Biochemistry 48:10014-9 PDF Identification of an Aurora-A/PinsLINKER/ Dlg Spindle Orientation Pathway using Induced Cell Polarity in S2 Cells Johnston CA, Hirono K, Prehoda KE, Doe CQ Cell 138:1150-63