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Sus1/ENY2: a multitasking protein in eukaryotic gene expression.
- Source :
-
Critical reviews in biochemistry and molecular biology [Crit Rev Biochem Mol Biol] 2012 Nov-Dec; Vol. 47 (6), pp. 556-68. Date of Electronic Publication: 2012 Oct 12. - Publication Year :
- 2012
-
Abstract
- The purpose of this review is to provide a complete overview on the functions of the transcription/export factor Sus1. Sus1 is a tiny conserved factor in sequence and functions through the eukaryotic kingdom. Although it was discovered recently, research done to address the role of Sus1/ENY2 has provided in deep description of different mechanisms influencing gene expression. Initially found to interact with the transcription and mRNA export machinery in yeast, it is now clear that it has a broad role in mRNA biogenesis. Sus1 is necessary for histone H2B deubiquitination, mRNA export and gene gating. Moreover, interesting observations also suggest a link with the cytoplasmatic mRNP fate. Although the role of Sus1 in human cells is largely unknown, preliminary results suggest interesting links to pathological states that range from rare diseases to diabetes. We will describe what is known about Sus1/ENY2 in yeast and other eukaryotes and discuss some exciting open questions to be solved in the future.
- Subjects :
- Animals
Chromatin genetics
Chromatin metabolism
Cytoplasm genetics
Cytoplasm metabolism
Diabetes Mellitus genetics
Diabetes Mellitus metabolism
Exodeoxyribonucleases genetics
Exodeoxyribonucleases metabolism
Histones metabolism
Humans
Nuclear Proteins genetics
Phosphoproteins genetics
Phosphoproteins metabolism
RNA Transport
RNA, Messenger metabolism
RNA-Binding Proteins genetics
Ribonucleoproteins metabolism
Saccharomyces cerevisiae Proteins genetics
Trans-Activators genetics
Trans-Activators metabolism
Transcription Factors genetics
Eukaryotic Cells
Gene Expression Regulation
Nuclear Proteins metabolism
RNA-Binding Proteins metabolism
Saccharomyces cerevisiae Proteins metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1549-7798
- Volume :
- 47
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Critical reviews in biochemistry and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 23057668
- Full Text :
- https://doi.org/10.3109/10409238.2012.730498