Interested post-doctoral applicants should note that there are many ongoing projects in the lab, and we are open to new ideas. Current post-docs in the lab have backgrounds in diverse topics that include protein chemistry, small RNAs in Drosophila, pre-mRNA splicing in human disease, X-ray crystallography of bacterial macromolecular structures, bioinformatics of mammalian-cell lncRNAs, and metabolism of human tRNases and miRNAs. Thus, we make a great team for developing multi-pronged and innovative approaches to study mammalian-cell metabolic pathways. What is written under Projects in the Maquat-lab web site offers simply a taste of what we have done, and what is written below offers just the tip of the iceberg of what we are interested in doing.
Opportunities are available to research the function of new and already identified NMD factors (Lejeune et al., 2003, Mol. Cell 12:675-687), factor roles in NMD (Chiu et al., 2003, RNA 9:77-87; Brumbaugh et al., 2004, Mol. Cell 14:585-598; Matsuda et al., 2007, Nat. Struct. Mol. Biol. 14:974-979; Kurosaki and Maquat, 2013, Proc. Natl. Acad. Sci. USA 110:3357-3362) and, in collaboration with Rob Singer (Albert Einstein College of Medicine), the spatial difference in cells between nucleus-associated and cytoplasmic NMD (Sato et al., 2008, Mol Cell 29:255-262; Trcek et al., 2013, Genes Dev 27:541-551). We are also interested in how cells utilize NMD for new purposes, and how NMD interfaces with other pathways of RNA and protein metabolism.
Opportunities are additionally available to study a related mRNA decay pathway that we have named Staufen1(STAU)-mediated mRNA decay (SMD) (Kim et al., 2005, Cell 120:195-208; Kim et al., 2007, EMBO J. 26:2670-2681). We aim to determine what defines intramolecular and intermolecular STAU-binding sites (Gong and Maquat, 2011, Nature, 470:284-288; Wang et al., 2013, Genes Dev 27: 793-804; Gong et al., 2013, Nat. Struct. Mol. Biol, in press; Elbarbary et al., 2013, Genes Dev 27:1495-1510) and how SINEs have evolved to constructively influence RNA processes.
We are also interested in how different dsRNA-binding proteins work together and in competition with one another. As one example, we are pursuing our finding that STAU1 binding to 3'UTR inverted Alu elements competes with binding of the largely nuclear paraspeckle protein p54nrb and the largely cytoplasmic protein kinase R (PKR) to mediate, respectively, the nuclear export and cytoplasmic translation of a number of mRNAs that contain these elements (Elbarbary et al., 2013, Genes Dev 27:1495-1510). What other dsRNA-binding proteins compete with STAU to influence cellular RNA metabolism, and how do other classes of 3'UTR inverted Alu elements identified by Elbarbary et al. (2013) differentially affect mRNA metabolism? We are simultaneously investigating why 3'UTR inverted Alu elements fail to trigger SMD.
Successful post-doctoral applicants will join a well-equipped group of interactive lab members with diverse backgrounds and broad expertise in newly remodeled labs. The University of Rochester is unique for its sizeable community of RNA researchers, its Center for RNA Biology: From Genome to Therapeutics, and its RNA Structure and Function Cluster, all of which include members of the Medical Center, in which the Maquat lab resides, as well as the College of Arts, Sciences and Engineering across the street.
Interested individuals should send a C.V., including a description of past and on-going research, and the names and contact information of three references to Dr. Maquat.
- A post-translational regulatory switch on UPF1 controls targeted mRNA degradation. Genes Dev. 28, 1900-16. (2014 Sep 01).
- 'Black sheep' that don't leave the double-stranded RNA-binding domain fold. Trends Biochem Sci. 39, 328-40. (2014 Jul 01).
- Defective secretory-protein mRNAs take the RAPP. Trends Biochem Sci. 39, 154-6. (2014 Apr 01).