Next Article in Journal
Antiproliferative Activity of Double Point Modified Analogs of 1,25-Dihydroxyvitamin D2 Against Human Malignant Melanoma Cell Lines
Next Article in Special Issue
The Human Host Defense Ribonucleases 1, 3 and 7 Are Elevated in Patients with Sepsis after Major Surgery—A Pilot Study
Previous Article in Journal
NLRP3 Upregulation in Retinal Pigment Epithelium in Age-Related Macular Degeneration
Previous Article in Special Issue
RNase L Cleavage Products Promote Switch from Autophagy to Apoptosis by Caspase-Mediated Cleavage of Beclin-1
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2016, 17(1), 74; doi:10.3390/ijms17010074

The Roles of RNase-L in Antimicrobial Immunity and the Cytoskeleton-Associated Innate Response

1
Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA
2
Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA
3
Research Services, Baltimore Veterans Affairs Medical Center, Baltimore, MD 21201, USA
4
Department of Biological Sciences, University of Toledo, Toledo, OH 43606, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Ester Boix
Received: 6 November 2015 / Revised: 21 December 2015 / Accepted: 4 January 2016 / Published: 8 January 2016
(This article belongs to the Special Issue Antimicrobial RNases in Host Defense)
View Full-Text   |   Download PDF [1824 KB, uploaded 8 January 2016]   |  

Abstract

The interferon (IFN)-regulated endoribonuclease RNase-L is involved in multiple aspects of the antimicrobial innate immune response. It is the terminal component of an RNA cleavage pathway in which dsRNA induces the production of RNase-L-activating 2-5A by the 2′-5′-oligoadenylate synthetase. The active nuclease then cleaves ssRNAs, both cellular and viral, leading to downregulation of their expression and the generation of small RNAs capable of activating retinoic acid-inducible gene-I (RIG-I)-like receptors or the nucleotide-binding oligomerization domain-like receptor 3 (NLRP3) inflammasome. This leads to IFNβ expression and IL-1β activation respectively, in addition to broader effects on immune cell function. RNase-L is also one of a growing number of innate immune components that interact with the cell cytoskeleton. It can bind to several cytoskeletal proteins, including filamin A, an actin-binding protein that collaborates with RNase-L to maintain the cellular barrier to viral entry. This antiviral activity is independent of catalytic function, a unique mechanism for RNase-L. We also describe here the interaction of RNase-L with the E3 ubiquitin ligase and scaffolding protein, ligand of nump protein X (LNX), a regulator of tight junction proteins. In order to better understand the significance and context of these novel binding partners in the antimicrobial response, other innate immune protein interactions with the cytoskeleton are also discussed. View Full-Text
Keywords: RNase-L; innate immunity; cytoskeleton; actin; interferon; inflammasome; LNX; filamin A RNase-L; innate immunity; cytoskeleton; actin; interferon; inflammasome; LNX; filamin A
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Ezelle, H.J.; Malathi, K.; Hassel, B.A. The Roles of RNase-L in Antimicrobial Immunity and the Cytoskeleton-Associated Innate Response. Int. J. Mol. Sci. 2016, 17, 74.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top