Abstract
The basic Helix-Loop-Helix/PER-ARNT-SIM (bHLH-PAS) domain family of transcription factors mediates cellular responses to a variety of internal and external stimuli. As functional transcription factors, these proteins act as bHLH-PAS heterodimers and can be further sub-classified into sensory/activated subunits and regulatory or ARNT-like proteins. This class of proteins act as master regulators of the bHLHPAS superfamily of transcription factors that mediate circadian rhythm gene programs, innate and adaptive immune responses, oxygen-sensing mechanisms and compensate for deleterious environmental exposures. Some contribute to the etiology of human pathologies including cancer because of their effects on cell growth and metabolism. We will review the canonical roles of ARNT and ARNT-like proteins with an emphasis on coactivator selectivity and recruitment. We will also discuss recent advances in our understanding of noncanonical DNA-binding independent or off-target roles of ARNT that are uncoupled from its classic heterodimeric bHLH-PAS binding partners. Understanding the DNA binding-independent functions of ARNT may identify novel therapeutic options for the treatment of a large spectrum of disease states.
Keywords: ARNT, bHLH-PAS, circadian rhythm, cross-talk, environmental sensor, oxygen sensing, transcription factor.
Current Molecular Medicine
Title:The Aryl Hydrocarbon Receptor Nuclear Translocator (ARNT) Family of Proteins: Transcriptional Modifiers with Multi-Functional Protein Interfaces
Volume: 13 Issue: 7
Author(s): M. P. Labrecque, G. G. Prefontaine and T. V. Beischlag
Affiliation:
Keywords: ARNT, bHLH-PAS, circadian rhythm, cross-talk, environmental sensor, oxygen sensing, transcription factor.
Abstract: The basic Helix-Loop-Helix/PER-ARNT-SIM (bHLH-PAS) domain family of transcription factors mediates cellular responses to a variety of internal and external stimuli. As functional transcription factors, these proteins act as bHLH-PAS heterodimers and can be further sub-classified into sensory/activated subunits and regulatory or ARNT-like proteins. This class of proteins act as master regulators of the bHLHPAS superfamily of transcription factors that mediate circadian rhythm gene programs, innate and adaptive immune responses, oxygen-sensing mechanisms and compensate for deleterious environmental exposures. Some contribute to the etiology of human pathologies including cancer because of their effects on cell growth and metabolism. We will review the canonical roles of ARNT and ARNT-like proteins with an emphasis on coactivator selectivity and recruitment. We will also discuss recent advances in our understanding of noncanonical DNA-binding independent or off-target roles of ARNT that are uncoupled from its classic heterodimeric bHLH-PAS binding partners. Understanding the DNA binding-independent functions of ARNT may identify novel therapeutic options for the treatment of a large spectrum of disease states.
Export Options
About this article
Cite this article as:
Labrecque P. M., Prefontaine G. G. and Beischlag V. T., The Aryl Hydrocarbon Receptor Nuclear Translocator (ARNT) Family of Proteins: Transcriptional Modifiers with Multi-Functional Protein Interfaces, Current Molecular Medicine 2013; 13 (7) . https://dx.doi.org/10.2174/15665240113139990042
DOI https://dx.doi.org/10.2174/15665240113139990042 |
Print ISSN 1566-5240 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5666 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Defensins: Key Molecules in Ocular Surface Protection
Current Immunology Reviews (Discontinued) Mutual Modulation of Femarelle and Vitamin D Analog Activities in Human Derived Female Cultured Osteoblasts
Immunology, Endocrine & Metabolic Agents in Medicinal Chemistry (Discontinued) Morphologic and Molecular Backgrounds for Personalized Management of Genito-Urinary Cancers: An Overview
Current Drug Targets Diet-Derived Phytochemicals: From Cancer Chemoprevention to Cardio-Oncological Prevention
Current Drug Targets The Role of Integrins in Glioma Biology and Anti-Glioma Therapies
Current Pharmaceutical Design Use of Recombinant Human Erythropoietin as an Antianemic and Performance Enhancing Drug
Current Pharmaceutical Biotechnology Cells of the Macrophage Lineage and their Role in the Pathogenesis of HIV-1 Infection: An Update
Medicinal Chemistry Reviews - Online (Discontinued) Melatonin and Aromatase in Breast Cancer
Clinical Cancer Drugs Site-related Effects of Relaxin in the Gastrointestinal Tract Through Nitric Oxide Signalling: An Updated Report
Current Protein & Peptide Science Perspectives on mTOR Inhibitors for Castration-Refractory Prostate Cancer
Current Cancer Drug Targets Validation of Human Clinical Genetic Tests
Mini-Reviews in Medicinal Chemistry Editorial [ Hot Topic: Targeting Tumor Angiogenesis: An Update (Guest Editor: Girolamo Ranieri)]
Current Medicinal Chemistry Prognostic Role of Hedgehog-GLI1 Signaling Pathway in Aggressive and Metastatic Breast Cancers
Current Drug Metabolism Potential Gene Therapy Strategies for Cancer Stem Cells
Current Gene Therapy Immunity to Tuberculosis and Novel Therapeutic Strategies
Clinical Immunology, Endocrine & Metabolic Drugs (Discontinued) Cancer T Cell Immunotherapy with Bispecific Antibodies and Chimeric Antigen Receptors
Recent Patents on Anti-Cancer Drug Discovery Pathophysiology of Blood-Spinal Cord Barrier in Traumatic Injury and Repair
Current Pharmaceutical Design Muscular Gene Transfer Using Nonviral Vectors
Current Gene Therapy Counter-Regulatory Role of Bile Acid Activated Receptors in Immunity and Inflammation
Current Molecular Medicine Improved Candidate Biomarker Detection Based on Mass Spectrometry Data Using the Hilbert-Huang Transform
Protein & Peptide Letters