Identification and characterization of a CRM1/XPO1-dependent nuclear export signal in the human androgen receptor

2016 ◽  
Author(s):  
Stefanie V Schutz ◽  
Axel Merseburger ◽  
Anca Azoitei ◽  
Marcus V Cronauer
Keyword(s):  
Androgen Receptor ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Export Signal ◽  
Identification And Characterization ◽  
Human Androgen Receptor

Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor

2003 ◽  
Vol 2 (6) ◽  
pp. 73
Author(s):  
Anthony J Saporita ◽  
Qiuheng Zhang ◽  
Neema Navai ◽  
Zehra Dincer ◽  
Junghyun Hahn ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Export Signal ◽  
Identification And Characterization

scholarly journals Identification and Characterization of a Ligand-regulated Nuclear Export Signal in Androgen Receptor

2003 ◽  
Vol 278 (43) ◽  
pp. 41998-42005 ◽  
Author(s):  
Anthony J. Saporita ◽  
Qiuheng Zhang ◽  
Neema Navai ◽  
Zehra Dincer ◽  
Junghyun Hahn ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Export Signal ◽  
Identification And Characterization

scholarly journals Characterization of a Novel Transferable CRM-1-Independent Nuclear Export Signal in a Herpesvirus Tegument Protein That Shuttles between the Nucleus and Cytoplasm

2006 ◽  
Vol 80 (20) ◽  
pp. 10021-10035 ◽  
Author(s):  
Janneke Verhagen ◽  
Michelle Donnelly ◽  
Gillian Elliott
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Nuclear Targeting ◽  
Leptomycin B ◽  
Herpesvirus Type ◽  
Close Proximity ◽  
Bovine Herpesvirus Type 1 ◽  
Import And Export ◽  
Export Signal

ABSTRACT A new group of nucleocytoplasmic shuttling proteins has recently been identified in the structural proteins encoded by several alphaherpesvirus UL47 genes. Nuclear import and export signals for the bovine herpesvirus type 1 UL47 protein (VP8 or bUL47) have been described previously. Here, we study the trafficking of bUL47 in detail and identify an import signal different from that shown before. It comprises a 20-residue N-terminal peptide that is fully transferable and targets a large, normally cytosolic protein to the nucleus. A conserved RRPRRS motif within this peptide was shown to be essential but not sufficient for nuclear targeting. Using interspecies heterokaryon assays, we further demonstrate that the export activity of the published leucine-rich nuclear export signal (NES) is also transferable to a large protein but is functionally weak compared to the activity of the HIV-1 Rev NES. We show that nuclear export dictated by this bUL47 NES is sensitive to leptomycin B (LMB) and therefore dependent on the export receptor CRM-1. However, nuclear export of full-length bUL47 is fully resistant to LMB, suggesting the presence of an additional NES. We go on to identify a second NES in bUL47 within a 28-residue peptide that is in close proximity to but entirely separable from the N-terminal import signal, and we use fluorescence loss in photobleaching to confirm its activity. This NES is resistant to leptomycin B, and therefore utilizes an export receptor other than CRM-1. As this new sequence bears little similarity to other export signals so far defined, we suggest it may be involved in bUL47 export from the nucleus via a novel cellular receptor.

scholarly journals Characterization of the Nuclear Export Signal in the Coronavirus Infectious Bronchitis Virus Nucleocapsid Protein

2007 ◽  
Vol 81 (8) ◽  
pp. 4298-4304 ◽  
Author(s):  
Mark L. Reed ◽  
Gareth Howell ◽  
Sally M. Harrison ◽  
Kelly-Anne Spencer ◽  
Julian A. Hiscox
Keyword(s):  
Infectious Bronchitis Virus ◽  
Nuclear Export ◽  
Structural Information ◽  
Protein Complexes ◽  
Nuclear Export Signal ◽  
Leptomycin B ◽  
N Protein ◽  
Infectious Bronchitis ◽  
Export Signal

ABSTRACT The nucleocapsid (N) protein of infectious bronchitis virus (IBV) localizes to the cytoplasm and nucleolus and contains an eight-amino-acid nucleolar retention motif. In this study, a leucine-rich nuclear export signal (NES) (291-LQLDGLHL-298) present in the C-terminal region of the IBV N protein was analyzed by using alanine substitution and deletion mutagenesis to investigate the relative contributions that leucine residues make to nuclear export and where these residues are located on the structure of the IBV N protein. The analysis indicated that Leu296 and Leu298 are required for efficient nuclear export of the protein. Structural information indicated that both of these amino acids are available for interaction with protein complexes involved in this process. However, export of N protein from the nucleus/nucleolus was not inhibited by leptomycin B treatment, indicating that N protein nuclear export is independent of the CRM1-mediated export pathway.

scholarly journals Functional characterization of MODY2 mutations in the nuclear export signal of glucokinase

2018 ◽  
Vol 1864 (7) ◽  
pp. 2385-2394 ◽  
Author(s):  
Angel Gutierrez-Nogués ◽  
Carmen-María García-Herrero ◽  
Josep Oriola ◽  
Olivier Vincent ◽  
María-Angeles Navas
Keyword(s):  
Nuclear Export ◽  
Functional Characterization ◽  
Nuclear Export Signal ◽  
Export Signal

scholarly journals Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP

2021 ◽  
Vol 77 (3) ◽  
pp. 70-78
Author(s):  
Alaa Shaikhqasem ◽  
Kerstin Schmitt ◽  
Oliver Valerius ◽  
Ralf Ficner
Keyword(s):  
Crystal Structure ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Cysteine Residue ◽  
Covalent Modification ◽  
Binding Cleft ◽  
Inhibitor Compounds ◽  
Nuclear Export Receptor ◽  
Export Signal

CRM1 is a nuclear export receptor that has been intensively targeted over the last decade for the development of antitumor and antiviral drugs. Structural analysis of several inhibitor compounds bound to CRM1 revealed that their mechanism of action relies on the covalent modification of a critical cysteine residue (Cys528 in the human receptor) located in the nuclear export signal-binding cleft. This study presents the crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP at 2.58 Å resolution. The results demonstrate that buffer components can interfere with the characterization of cysteine-dependent inhibitor compounds.

Characterization of specific antigenic epitopes and the nuclear export signal of the Porcine circovirus 2 ORF3 protein

2016 ◽  
Vol 184 ◽  
pp. 40-50 ◽  
Author(s):  
Jinyan Gu ◽  
Lun Wang ◽  
Yulan Jin ◽  
Cui Lin ◽  
Huijuan Wang ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Porcine Circovirus ◽  
Orf3 Protein ◽  
Porcine Circovirus 2 ◽  
Export Signal ◽  
Antigenic Epitopes

scholarly journals A nuclear role for the DEAD-box protein Dbp5 in tRNA export

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Azra Lari ◽  
Arvind Arul Nambi Rajan ◽  
Rima Sandhu ◽  
Taylor Reiter ◽  
Rachel Montpetit ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Ribosomal Subunit ◽  
Nucleocytoplasmic Transport ◽  
Alanine Scanning Mutagenesis ◽  
Dead Box ◽  
Nuclear Shuttling ◽  
Export Signal

Dbp5 is an essential DEAD-box protein that mediates nuclear mRNP export. Dbp5 also shuttles between nuclear and cytoplasmic compartments with reported roles in transcription, ribosomal subunit export, and translation; however, the mechanism(s) by which nucleocytoplasmic transport occurs and how Dbp5 specifically contributes to each of these processes remains unclear. Towards understanding the functions and transport of Dbp5 in Saccharomyces cerevisiae, alanine scanning mutagenesis was used to generate point mutants at all possible residues within a GFP-Dbp5 reporter. Characterization of the 456 viable mutants led to the identification of an N-terminal Xpo1-dependent nuclear export signal in Dbp5, in addition to other separation-of-function alleles, which together provide evidence that Dbp5 nuclear shuttling is not essential for mRNP export. Rather, disruptions in Dbp5 nucleocytoplasmic transport result in tRNA export defects, including changes in tRNA shuttling dynamics during recovery from nutrient stress.

scholarly journals Characterization of a Nuclear Export Signal within the Human T Cell Leukemia Virus Type I Transactivator Protein Tax

2003 ◽  
Vol 278 (24) ◽  
pp. 21814-21822 ◽  
Author(s):  
Timothy Alefantis ◽  
Kate Barmak ◽  
Edward W. Harhaj ◽  
Christian Grant ◽  
Brian Wigdahl
Keyword(s):  
Nuclear Export ◽  
Leukemia Virus ◽  
Nuclear Export Signal ◽  
Type I ◽  
Cell Leukemia Virus Type ◽  
Human T Cell ◽  
T Cell Leukemia Virus ◽  
Transactivator Protein ◽  
Export Signal
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