Murine GBP-2: A new IFN-y-induced member of the GBP family of GTPases isolated from macrophages

Deborah J. Vestal, Janice E. Buss, Scott R. McKercher, Nancy A. Jenkins, Neal G. Copeland, Gregory S. Kelner, Vinod K. Asundi, Richard A. Maki

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

We have cloned a new member of the interferon (IFN)-induced guanylate- binding protein (GBP) family of GTPases, murine GBP-2 (mGBP-2), from bone marrow-derived macrophages. mGBP-2 is located on murine chromosome 3, where it is linked to mGBP-1. With the identification of mGBP-2 there are now two human and two murine GBPs. Like other GBPs, mGBP-2 RNA and protein are induced by IFN-γ. In addition, mGBP2 shares with the other GBPs important structural features that distinguish this family from other GTPases. First, mGBP-2 contains only two of the three consensus sequences for nucleotide binding found within the classic GTP binding regions of other GTPases. A second amino acid motif found in mGBP-2 is a potential C-terminal site for isoprenoid modification, called a CaaX sequence. mGBP-2 is prenylated, as detected by [3H]mevalonate incorporation, when expressed in COS cells and preferentially incorporates the C-20 isoprenoid geranylgeraniol. Surprisingly, despite having a functional CaaX sequence, mGBP-2 is primarily cytosolic. GBP proteins are very abundant in IFN-exposed cells, but little is known about their function. mGBP2 is expressed by IFN-γ-treated cells from C57B1/6 mice, whereas mGBP-1 is not. Thus, the identification of mGBP-2 makes possible the study of GBP function in the absence of a second family member.

Original languageEnglish (US)
Pages (from-to)977-985
Number of pages9
JournalJournal of Interferon and Cytokine Research
Volume18
Issue number11
DOIs
StatePublished - Nov 1998

ASJC Scopus subject areas

  • Immunology
  • Cell Biology
  • Virology

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