Influence of Serine O-Glycosylation or O-Phoshorylation Close to the vJun Nuclear Localisation Sequence on Nuclear Import

ChemBioChem ◽  
2005 ◽  
Vol 7 (1) ◽  
pp. 88-97 ◽  
Author(s):  
Stefanie Schlummer ◽  
Robin Vetter ◽  
Norman Kuder ◽  
Andreas Henkel ◽  
Yong-Xiang Chen ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Nuclear Localisation ◽  
Nuclear Localisation Sequence

scholarly journals Mask family proteins ANKHD1 and ANKRD17 regulate YAP nuclear import and stability

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Clara Sidor ◽  
Nerea Borreguero-Munoz ◽  
Georgina C Fletcher ◽  
Ahmed Elbediwy ◽  
Oriane Guillermin ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Nuclear Export ◽  
Tissue Growth ◽  
Ankyrin Repeat ◽  
Molecular Function ◽  
Liquid Droplets ◽  
Transcriptional Coactivator ◽  
Nuclear Localisation ◽  
Cytoplasmic Transport ◽  
Nuclear Localisation Sequence

Mask family proteins were discovered in Drosophila to promote the activity of the transcriptional coactivator Yorkie (Yki), the sole fly homolog of mammalian YAP (YAP1) and TAZ (WWTR1). The molecular function of Mask, or its mammalian homologs Mask1 (ANKHD1) and Mask2 (ANKRD17), remains unclear. Mask family proteins contain two ankyrin repeat domains that bind Yki/YAP as well as a conserved nuclear localisation sequence (NLS) and nuclear export sequence (NES), suggesting a role in nucleo-cytoplasmic transport. Here we show that Mask acts to promote nuclear import of Yki, and that addition of an ectopic NLS to Yki is sufficient to bypass the requirement for Mask in Yki-driven tissue growth. Mammalian Mask1/2 proteins also promote nuclear import of YAP, as well as stabilising YAP and driving formation of liquid droplets. Mask1/2 and YAP normally colocalise in a granular fashion in both nucleus and cytoplasm, and are co-regulated during mechanotransduction.

scholarly journals Nuclear-capture of endosomes drives depletion of nuclear G-actin to promote SRF/MRTF gene expression and cancer cell invasiveness

2020 ◽  
Author(s):  
Sergi Marco ◽  
Matthew Neilson ◽  
Madeleine Moore ◽  
Arantxa Pérez-García ◽  
Holly Hall ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nuclear Import ◽  
Tyrosine Kinases ◽  
Target Genes ◽  
Serum Response Factor ◽  
Actin Binding ◽  
Cell Scattering ◽  
Nuclear Localisation Sequence ◽  
Related Transcription Factor ◽  
Cell Invasiveness

Abstract Signals are relayed from receptor tyrosine kinases (RTKs) at the cell surface to effector systems in the cytoplasm and nucleus, and coordination of this process is important for the execution of migratory phenotypes, such as cell scattering and invasion. The endosomal system influences how RTK signalling is coded, but the ways in which it transmits these signals to the nucleus to influence gene expression are not yet clear. Here we show that an RTK, cMET promotes Rab17-dependent endocytosis of EphA2, another RTK, followed by centripetal transport of EphA2-positive endosomes. EphA2 then mediates physical capture of endosomes on the outer surface of the nucleus; a process involving interaction between the nuclear import machinery and a nuclear localisation sequence in EphA2’s cytodomain. Nuclear capture of EphA2 promotes RhoG-dependent phosphorylation of the actin-binding protein, cofilin to oppose nuclear import of G-actin. The resulting depletion of nuclear G-actin drives transcription of Myocardin-related transcription factor (MRTF)/serum-response factor (SRF)-target genes to implement cell scattering and the invasive behaviour of cancer cells.

scholarly journals Mask family proteins ANKHD1 and ANKRD17 regulate YAP nuclear import, stability and phase separation

2019 ◽  
Author(s):  
Clara Sidor ◽  
Nerea Borreguero-Munoz ◽  
Georgina C Fletcher ◽  
Ahmed Elbediwy ◽  
Hannah Vanyai ◽  
...  
Keyword(s):  
Phase Separation ◽  
Nuclear Import ◽  
Nuclear Export ◽  
Tissue Growth ◽  
Ankyrin Repeat ◽  
Liquid Droplets ◽  
Transcriptional Coactivator ◽  
Cytoplasmic Transport ◽  
Nuclear Localisation Sequence ◽  
Kh Domain

AbstractThe Mask family of multiple ankyrin repeat and KH domain proteins were discovered in Drosophila to promote the activity of the transcriptional coactivator Yorkie (Yki), the sole fly homolog of mammalian YAP (YAP1) and TAZ (WWTR1). The molecular function of Mask, or its mammalian homologs Mask1 (ANKHD1) and Mask2 (ANKRD17), remains unclear. Mask family proteins contain two Ankyrin repeat domains that bind Yki/YAP as well as a conserved nuclear localisation sequence (NLS) and nuclear export sequence (NES), suggesting a role in nucleo-cytoplasmic transport. Here we show that Mask acts to promote nuclear import of Yki, and that addition of an ectopic NLS to Yki is sufficient to bypass the requirement for Mask in Yki-driven tissue growth. Mammalian Mask1/2 proteins also promote nuclear import of YAP, as well as stabilising YAP and driving colloidal phase separation into large liquid droplets. Mask1/2 and YAP normally colocalise in a granular fashion in both nucleus and cytoplasm, and are co-regulated during mechanotransduction. Our results suggest that Mask family proteins promote YAP nuclear import and phase separation to regulate YAP stability and transcriptional activity.

scholarly journals Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Sergi Marco ◽  
Matthew Neilson ◽  
Madeleine Moore ◽  
Arantxa Perez-Garcia ◽  
Holly Hall ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Tyrosine Kinases ◽  
Target Genes ◽  
Serum Response Factor ◽  
Actin Binding ◽  
Cell Scattering ◽  
Nuclear Localisation Sequence ◽  
Related Transcription Factor ◽  
Endosomal System ◽  
Serum Response

AbstractSignals are relayed from receptor tyrosine kinases (RTKs) at the cell surface to effector systems in the cytoplasm and nucleus, and coordination of this process is important for the execution of migratory phenotypes, such as cell scattering and invasion. The endosomal system influences how RTK signalling is coded, but the ways in which it transmits these signals to the nucleus to influence gene expression are not yet clear. Here we show that hepatocyte growth factor, an activator of MET (an RTK), promotes Rab17- and clathrin-dependent endocytosis of EphA2, another RTK, followed by centripetal transport of EphA2-positive endosomes. EphA2 then mediates physical capture of endosomes on the outer surface of the nucleus; a process involving interaction between the nuclear import machinery and a nuclear localisation sequence in EphA2’s cytodomain. Nuclear capture of EphA2 promotes RhoG-dependent phosphorylation of the actin-binding protein, cofilin to oppose nuclear import of G-actin. The resulting depletion of nuclear G-actin drives transcription of Myocardin-related transcription factor (MRTF)/serum-response factor (SRF)-target genes to implement cell scattering and the invasive behaviour of cancer cells.

Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus

FEBS Letters ◽  
1996 ◽  
Vol 382 (3) ◽  
pp. 330-334 ◽  
Author(s):  
S. Kügler ◽  
A. Grünweller ◽  
C. Probst ◽  
M. Klinger ◽  
P.K. Müller ◽  
...  
Keyword(s):  
Nuclear Localisation ◽  
Nuclear Localisation Sequence

scholarly journals Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Hyeon Gyu Seo ◽  
Han Byeol Kim ◽  
Min Jueng Kang ◽  
Joo Hwan Ryum ◽  
Eugene C. Yi ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Nuclear Localisation Signal ◽  
Nuclear Localisation ◽  
Glcnac Transferase

Dynamic changes in nuclear import of a nuclear localisation signal-bearing substrate in 8-cell stage porcine embryos

2015 ◽  
Vol 27 (2) ◽  
pp. 385 ◽  
Author(s):  
Yanfang Li ◽  
Ki-Eun Park ◽  
Ryan A. Cabot
Keyword(s):  
Nuclear Import ◽  
In Vitro Assays ◽  
Cell Stage ◽  
Nuclear Trafficking ◽  
Nuclear Localisation ◽  
Cellular Events ◽  
Stage Of Development ◽  
Importin Α

Coordinated intracellular trafficking is critically important for proper timing of major cellular events during embryogenesis. Nuclear import mediated by the karyopherin α/β (importin α/β) heterodimer is perhaps the best characterised nuclear trafficking system in eukaryotic cells. Seven karyopherin α subtypes have been identified in the domestic pig, and although each karyopherin α subtype transports proteins bearing classical nuclear localisation signals (NLSs), individual karyopherin α subtypes have been shown to preferentially transport specific cargoes. The aim of the present study was to determine the mechanism by which BRN2, a transcription factor previously reported to be transported by the karyopherin α/β heterodimer, gains access to the nucleus in porcine oocytes and embryos. Using a combination of in vivo and in vitro assays, we tested the hypothesis that discrete karyopherin α subtypes transport BRN2 into the nuclei of porcine oocytes and cleavage stage embryos. Our results show that ectopically expressed BRN2 adopts a nuclear localisation in all nuclei through the 4-cell stage of development, whereas only a subset of blastomeres in 8-cell stage embryos possess nuclear BRN2. This pattern is unique to BRN2 because another ectopically expressed NLS-containing protein is able to adopt a nuclear localisation in all blastomeres of 8-cell stage embryos.

scholarly journals CRISPR/Cas9 mediated mutation of mouse IL-1α nuclear localisation sequence abolishes expression

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Michael J. D. Daniels ◽  
Antony D. Adamson ◽  
Neil Humphreys ◽  
David Brough
Keyword(s):  
Nuclear Localisation ◽  
Nuclear Localisation Sequence
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