SUMO2/3 modification of activating transcription factor 5 (ATF5) controls its dynamic translocation at the centrosome. 2018

Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
Department of Pharmaceutical Sciences, College of Pharmacy, Washington State University, Spokane, Washington 99202; School of Pharmacy, Shanghai Jiaotong University, Shanghai 200240, China.

Activating transcription factor 5 (ATF5) is a member of the ATF/cAMP response element-binding protein family of transcription factors. ATF5 regulates stress responses and cell survival, proliferation, and differentiation and also plays a role in viral infections, cancer, diabetes, schizophrenia, and the olfactory system. Moreover, it was found to also have a critical cell cycle-dependent structural function at the centrosome. However, the mechanism that controls the localization of ATF5 at the centrosome is unclear. Here we report that ATF5 is small ubiquitin-like modifier (SUMO) 2/3-modified at a conserved SUMO-targeting consensus site in various types of mammalian cells. We found that SUMOylation of ATF5 is elevated in the G1 phase of the cell cycle and diminished in the G2/M phase. ATF5 SUMOylation disrupted the interaction of ATF5 with several centrosomal proteins and dislodged ATF5 from the centrosome at the end of the M phase. Of note, blockade of ATF5 SUMOylation deregulated the centrosome cycle, impeded ATF5 translocation from the centrosome, and caused genomic instability and G2/M arrest in HeLa cells. Our results indicate that ATF5 SUMOylation is an essential mechanism that regulates ATF5 localization and function at the centrosome.

UI MeSH Term Description Entries
D008856 Microscopy, Fluorescence Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye. Fluorescence Microscopy,Immunofluorescence Microscopy,Microscopy, Immunofluorescence,Fluorescence Microscopies,Immunofluorescence Microscopies,Microscopies, Fluorescence,Microscopies, Immunofluorescence
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014452 Ubiquitins A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins. Ubiquitin-Like Protein,Ubiquitin-Like Proteins,Protein, Ubiquitin-Like,Proteins, Ubiquitin-Like,Ubiquitin Like Protein,Ubiquitin Like Proteins
D016297 Mutagenesis, Site-Directed Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion. Mutagenesis, Oligonucleotide-Directed,Mutagenesis, Site-Specific,Oligonucleotide-Directed Mutagenesis,Site-Directed Mutagenesis,Site-Specific Mutagenesis,Mutageneses, Oligonucleotide-Directed,Mutageneses, Site-Directed,Mutageneses, Site-Specific,Mutagenesis, Oligonucleotide Directed,Mutagenesis, Site Directed,Mutagenesis, Site Specific,Oligonucleotide Directed Mutagenesis,Oligonucleotide-Directed Mutageneses,Site Directed Mutagenesis,Site Specific Mutagenesis,Site-Directed Mutageneses,Site-Specific Mutageneses

Related Publications

Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
August 2023, Cell and tissue research,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
September 2012, FEBS letters,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
March 2016, Cell and tissue research,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
June 2012, The Journal of biological chemistry,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
December 2021, Cancer cell international,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
August 2013, Molecular biology of the cell,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
February 2014, The Journal of biological chemistry,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
January 2006, Scandinavian journal of plastic and reconstructive surgery and hand surgery,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
May 1978, The Journal of antibiotics,
Yunsheng Yuan, and Kari Gaither, and Eugene Kim, and Edward Liu, and Ming Hu, and Kathy Lengel, and Dongmeng Qian, and Yidi Xu, and Bin Wang, and Henning Knipprath, and David X Liu
January 2020, PloS one,
Copied contents to your clipboard!