Section: Rotations

Postdoctoral Position Available

Michelle Kelliher, Ph.D.

Academic Role: Associate Professor

Faculty Appointment(s) In:
   Cancer Biology
   Molecular Genetics and Microbiology

Other Affiliation(s):
   Center for AIDS Research
   Interdisciplinary Graduate Program
   Program in Immunology and Virology

Potential Rotation Projects

Mechanism(s) of Leukemogenesis

Project 1: We have used retroviral insertional mutagenesis to identify genes that collaborate with the basic helix-loop-helix b(HLH) tal-1/scl oncogene. Using genomic DNA from retrovirally-infected tumors, you will use inverse PCR to isolate and identify the collaborating oncogenes.

Project 2: Using IPCR, we have identified the notch 1 locus as a frequent site for retroviral integration in Mo-MLV-infected tal-1/scl transgenic mice. To test whether expression of an activated notch1 allele accelerates tal-1/scl-induced leukemogenesis, you will reconstitute mice with wt or tal-1/scl hematopoietic precursors infected with a control or an activated notch1 retrovirus. The effects of notch and tal-1/scl expression on thymocyte development will be examined. If disease acceleration is observed, tumor cell lines will be established from mice to examine how notch1 and tal-1/scl proteins collaborate to induce disease in mice.

TNF signaling in mouse development and cancer

Project 1: Using Affymetrix oligonucleotide arrays, we have identified a number of novel, TNF-responsive genes. To determine the contribution of these genes to mouse development and TNF signaling, we have used gene targeting in embryonic stem cells to generate mice deficient for one of these genes. Sensitivity to TNF-induced cell death as well as IKK, jnk and p38 MAP kinase activation in response to TNF needs to be examined in murine embryonic fibroblasts derived from this mouse.

Project 2: The death domain kinase RIP1 mediates the NF-kB repsonse to TNF, yet the kinase activity of RIP1 does not appear required. These studies suggest RIP1 may mediate IKK activation by recruiting another as yet unidentified kinase. Using biochemical approaches, you will isolate and identify proteins that interact with RIP1.

Office: LRB-421
Phone: 508-856-8620
E-mail: Michelle.Kelliher@umassmed.edu
Keywords: Genetic Systems, Cancer Biology, Signal Transduction

More on Michelle Kelliher's Research Research | Figures | Publications | Rotations View All Sections on One Page

Postdoctoral Position Available A postdoctoral position is available to study in this laboratory. Contact Dr. Kelliher for additional details.