Jeff Wilusz

Jeff Wilusz

Professor

Room: B321 Microbiology
Phone: 970-491-0652
Lab: 970-491-4881
Fax: 970-491-1815
Email:

Fellow, American Association for the Advancement of Science

Editor-in-Chief, Wiley Interdisciplinary Reviews - RNA

Editorial Board Member, Journal of Biological Chemistry

Editorial Board Member, Molecular and Cellular Biology

Scientific Advisory Board Member, BIOO Scientific

Degrees

  • B.S., Cook College of Rutgers University
  • PhD, Duke University

Research Interests

My research is focused on the regulation of mRNA metabolism in mammalian cells. There are two major areas of study ongoing at this time:

  1. The interface between viral RNAs and the cellular mRNA decay machinery
    1. We have shown that alphavirus transcripts persist in the cytoplasm of mammalian and mosquito cells due to the presence of stabilizing elements in their 3’UTRs (Garneau et al 2007).
    2. We have discovered that a well-known RNA stabilizing factor, HuR, is hijacked by alphavirus RNAs and used to protect them from the decay machinery (Sokoloski et al 2010).
    3. Our results have shown that HuR is relocalized from the nucleus to the cytoplasm during alphavirus infection of mammalian cells (Sokoloski et al 2010).
    4. We have determined that poly(A) tracts, such as those found in the 5’ end of poxviruses are able to stabilize transcripts by binding the cellular Lsm complex to prevent 3’-5’ degradation (Bergman et al 2007)

We are currently investigating how other viruses such as Dengue and Rabies Viruses may modulate mRNA decay mechanisms to favor their transcripts. We are also collaborating with the Arthropod-borne Infectious Disease Laboratories (AIDL) here at CSU to look at the role of RNAi in viral infections.

  1. The role of the oncoprotein Nucleophosmin (NPM) in regulating polyadenylation Polyadenylation is the process by which a poly(A) tail is added to the 3’ end of mRNAs during their transcription. The poly(A) tail influences export, translation and decay of the transcript.
    1. We have determined that the NPM protein is deposited upstream of the poly(A) signal in mammalian cells (Palaniswamy et al 2006).
    2. NPM deposition requires polyadenylation but not cleavage of the nascent mRNA (Palaniswamy et al 2006).

We are now assessing the role of NPM deposition. We hypothesize that NPM acts as a mark of successful processing and may license mature mRNAs for export and translation.