Cited by 145RNA Research and SplicingRNA and protein synthesis mechanismsHemoglobinopathies and Related Disorders

Identification of AUF1 (Heterogeneous Nuclear Ribonucleoprotein D) as a Component of the α-Globin mRNA Stability Complex

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Kiledjian, Megerditch, DeMaria, Christine T., Brewer, Gary, Novick, Kristine·1997·Molecular and Cellular Biology

Abstract

mRNA turnover is an important regulatory component of gene expression and is significantly influenced by ribonucleoprotein (RNP) complexes which form on the mRNA. Studies of human alpha-globin mRNA stability have identified a specific RNP complex (alpha-complex) which forms on the 3' untranslated region (3'UTR) of the mRNA and appears to regulate the erythrocyte-specific accumulation of alpha-globin mRNA. One of the protein activities in this multiprotein complex is a poly(C)-binding activity which consists of two proteins, alphaCP1 and alphaCP2. Neither of these proteins, individually or as a pair, can bind the alpha-globin 3'UTR unless they are complexed with the remaining non-poly(C) binding proteins of the alpha-complex. With the yeast two-hybrid screen, a second alpha-complex protein was identified. This protein is a member of the previously identified A+U-rich (ARE) binding/degradation factor (AUF1) family of proteins, which are also known as the heterogeneous nuclear RNP (hnRNP) D proteins. We refer to these proteins as AUF1/hnRNP-D. Thus, a protein implicated in ARE-mediated mRNA decay is also an integral component of the mRNA stabilizing alpha-complex. The interaction of AUF1/hnRNP-D is more efficient with alphaCP1 relative to alphaCP2 both in vitro and in vivo, suggesting that the alpha-complex might be dynamic rather than a fixed complex. AUF1/hnRNP-D could, therefore, be a general mRNA turnover factor involved in both stabilization and decay of mRNA.

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  1. 10.1128/mcb.11.5.2460-2466.1991 · DOI
  2. Kiledjian, M., C. G. Burd, M. Gorlach, D. S. Portman, and G. Dreyfuss. 1994. Structure and function of hnRNP proteins, p. 127–149. In K. Nagai and I. Mattaj (ed.), RNA-protein interactions: frontiers in molecular biology. Oxford University Press, Oxford, United Kingdom.
  3. 10.1111/j.1432-1033.1995.tb20581.x · DOI
  4. 10.1128/mcb.14.12.8123-8132.1994 · DOI
  5. 10.1128/mcb.13.12.7652-7665.1993 · DOI

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Authors
Kiledjian, M., DeMaria, C. T., Brewer, G., & Novick, K.
Affiliations
  • Rutgers, The State University of New Jersey (US)
  • Atrium Health Wake Forest Baptist (US)
Corresponding author
Kiledjian, Megerditch
Venue
Molecular and Cellular Biology
Published
1997-08
Volume
17
Issue
8
Pages
4870-4876
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W2131483999
Cited by
145
References
68
Citations by year
2025: 1 · 2024: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 3 · 2014: 1 · 2013: 5 · 2012: 5
FWCI
3.47
Type
journal article
Language
en
Open access
Locations
  • Molecular and Cellular Biology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Rutgers University Community Repository (Rutgers University) (submittedVersion)
Funders
  • National Institutes of Health
  • National Cancer Institute (R01CA052443)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
Keywords
AUF1, HNRNPD, alpha-globin mRNA, mRNA stability, mRNA turnover, 3' untranslated region, AU-rich elements, mRNA degradation, alpha complex, ribonucleoprotein complexes
MeSH terms
Heterogeneous Nuclear Ribonucleoprotein D0, DNA-Binding Proteins, Leukemia, Erythroblastic, Acute, Globins, Humans, Poly C, Recombinant Fusion Proteins, Ribonucleoproteins, RNA, Messenger, Transcription Factors, Tumor Cells, Cultured, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, Heterogeneous-Nuclear Ribonucleoproteins, Heterogeneous-Nuclear Ribonucleoprotein D, Macromolecular Substances, Multiprotein Complexes

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