Literature DB >> 22708492

The biology of the RNA binding protein guanine-rich sequence binding factor 1.

Christoph Ufer1.   

Abstract

The mechanisms that drive the expression of a gene into its final protein product can be sub-divided into three levels: transcriptional, post-transcriptional and post-translational events. To facilitate the development and maintenance of a multi-cellular organism precise regulatory circuits are needed to ensure the survival of the organism and its ability to respond to changes in its environment. The key element of post-transcriptional regulation is RNA. Within the cell RNA exists in the form of ribonucleoproteins (RNPs), which are characterised by the underlying RNA and the proteins that are associated to it. The eukaryotic cell contains a vast plethora of RNA-binding proteins (RBPs) that control the complex fate of cellular RNAs. One of such RBPs is Guanine-rich sequence binding factor 1 (Grsf1). Grsf1 belongs to a group of heterogeneous nuclear RNPs that are characterised by the presence of an RNA binding domain designated RNA recognition motif (RRM). Grsf1 is present in most eukaryotic cells and is located in the nucleus as well as in the cytoplasm. Thus, its activity has been related to nuclear processes (RNA splicing) as well as cytoplasmic events (translation initiation). However, its full functional significance is not yet understood. Grsf1 has been implicated in the influenza viral life cycle, embryonic brain development and the regulation of apoptosis. Moreover, Grsf1 is a functional component of several cellular signalling pathways as well as of the regulation of the cellular redox homeostasis. This review summarises the present knowledge of Grsf1 biology to bring the scattered reports of Grsf1 function into a proper context.

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Year:  2012        PMID: 22708492     DOI: 10.2174/138920312801619457

Source DB:  PubMed          Journal:  Curr Protein Pept Sci        ISSN: 1389-2037            Impact factor:   3.272


  13 in total

1.  GRSF1-mediated MIR-G-1 promotes malignant behavior and nuclear autophagy by directly upregulating TMED5 and LMNB1 in cervical cancer cells.

Authors:  Zhen Yang; Qi Sun; Junfei Guo; Shixing Wang; Ge Song; Weiying Liu; Min Liu; Hua Tang
Journal:  Autophagy       Date:  2018-11-05       Impact factor: 16.016

Review 2.  Regnase-1, a rapid response ribonuclease regulating inflammation and stress responses.

Authors:  Renfang Mao; Riyun Yang; Xia Chen; Edward W Harhaj; Xiaoying Wang; Yihui Fan
Journal:  Cell Mol Immunol       Date:  2017-02-13       Impact factor: 11.530

3.  hnRNP A2/B1 interacts with influenza A viral protein NS1 and inhibits virus replication potentially through suppressing NS1 RNA/protein levels and NS1 mRNA nuclear export.

Authors:  Yimeng Wang; Jianhong Zhou; Yuchun Du
Journal:  Virology       Date:  2013-11-26       Impact factor: 3.616

4.  Grsf1-induced translation of the SNARE protein Use1 is required for expansion of the erythroid compartment.

Authors:  Andrzej Nieradka; Christoph Ufer; Klaske Thiadens; Godfrey Grech; Rastislav Horos; Marleen van Coevorden-Hameete; Emile van den Akker; Sajad Sofi; Hartmut Kuhn; Marieke von Lindern
Journal:  PLoS One       Date:  2014-09-03       Impact factor: 3.240

Review 5.  Long noncoding RNAs coordinate functions between mitochondria and the nucleus.

Authors:  Yaru Dong; Takeshi Yoshitomi; Ji-Fan Hu; Jizhe Cui
Journal:  Epigenetics Chromatin       Date:  2017-08-23       Impact factor: 4.954

6.  GRSF1 deficiency in skeletal muscle reduces endurance in aged mice.

Authors:  Riley K Driscoll; Linda K Krasniewski; Samuel G Cockey; Jen-Hao Yang; Yulan Piao; Elin Lehrmann; Yongqing Zhang; Marc Michel; Ji Heon Noh; Chang-Yi Cui; Myriam Gorospe
Journal:  Aging (Albany NY)       Date:  2021-06-02       Impact factor: 5.682

7.  GRSF1 regulates RNA processing in mitochondrial RNA granules.

Authors:  Alexis A Jourdain; Mirko Koppen; Mateusz Wydro; Chris D Rodley; Robert N Lightowlers; Zofia M Chrzanowska-Lightowlers; Jean-Claude Martinou
Journal:  Cell Metab       Date:  2013-03-05       Impact factor: 31.373

8.  HuR and GRSF1 modulate the nuclear export and mitochondrial localization of the lncRNA RMRP.

Authors:  Ji Heon Noh; Kyoung Mi Kim; Kotb Abdelmohsen; Je-Hyun Yoon; Amaresh C Panda; Rachel Munk; Jiyoung Kim; Jessica Curtis; Christopher A Moad; Christina M Wohler; Fred E Indig; Wilson de Paula; Dawood B Dudekula; Supriyo De; Yulan Piao; Xiaoling Yang; Jennifer L Martindale; Rafael de Cabo; Myriam Gorospe
Journal:  Genes Dev       Date:  2016-05-19       Impact factor: 11.361

9.  miR-346 and miR-138 competitively regulate hTERT in GRSF1- and AGO2-dependent manners, respectively.

Authors:  Ge Song; Renjie Wang; Junfei Guo; Xuyuan Liu; Fang Wang; Ying Qi; Haiying Wan; Min Liu; Xin Li; Hua Tang
Journal:  Sci Rep       Date:  2015-10-28       Impact factor: 4.379

Review 10.  RNA Binding Proteins and Regulation of mRNA Translation in Erythropoiesis.

Authors:  Kat S Moore; Marieke von Lindern
Journal:  Front Physiol       Date:  2018-07-24       Impact factor: 4.566

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