The effect of O-GlcNAcylation on hnRNP A1 translocation and interaction with transportin1

The heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a major pre-mRNA binding protein involved in transcription and translation. Although predominantly nuclear, hnRNP A1 shuttles rapidly between the nucleus and the cytosol, delivering its anchored pre-mRNA for further processing. Translocati...

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Published in:Experimental cell research 2017-01, Vol.350 (1), p.210-217
Main Authors: Roth, Shira, Khalaila, Isam
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
Acetylation
AGGLUTININS
beta Karyopherins - metabolism
Binding sites
Cell Nucleus - metabolism
Cells, Cultured
Cytoplasm - metabolism
Heterogeneous Nuclear Ribonucleoprotein A1
Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism
hnRNP A1
Humans
INTERACTIONS
MESSENGER-RNA
NEOPLASMS
NUCLEI
O-GlcNAcylation
PHOSPHORYLATION
PROCESSING
Protein Transport
Protein-protein interaction
RABBIT TUBES
RESIDUES
RNA Precursors - metabolism
RNA-protein interactions
SERINE
THREONINE
TRANSCRIPTION
TRANSFERASES
TRANSLOCATION
Trn1
WHEAT
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Summary:The heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a major pre-mRNA binding protein involved in transcription and translation. Although predominantly nuclear, hnRNP A1 shuttles rapidly between the nucleus and the cytosol, delivering its anchored pre-mRNA for further processing. Translocation is important for hnRNP A1 to accomplish its transcriptional and translational roles. Transportin1 (Trn1), a translocation protein, facilitates the translocation of hnRNP A1 back to the nucleus. Moreover, phosphorylation of serine residues at hnRNP A1 C-terminal domain affects its translocation. In this study, we found that phosphorylation is not the only modification that hnRNP A1 undergoes, but also O-linked N-acetylglucosaminylation (O-GlcNAcylation) could occur. Several putative novel O-GlcNAcylation and phosphorylation sites in hnRNP A1 were mapped. Whereas enhanced O-GlcNAcylation increased hnRNP A1 interaction with Trn1, enhanced phosphorylation reduced the interaction between the proteins. In addition, elevated O-GlcNAcylation resulted in hnRNP A1 seclusion in the nucleus, whereas elevated phosphorylation resulted in its accumulation in the cytosol. These findings suggest that a new player, i.e., O-GlcNAcylation, regulates hnRNP A1 translocation and interaction with Trn1, possibly affecting its function. There is a need for further study, to elucidate the role of O-GlcNAcylation in the regulation of the specific activities of hnRNP A1 in transcription and translation. •O-GlcNAcylation regulates hnRNP A1 translocation and interaction with Trn1.•Reciprocity between phosphorylation and O-GlcNAcylation in hnRNP A1 is proposed.•Novel O-GlcNAcylation and phosphorylation sites on hnRNPA1 were identified.
ISSN:0014-4827
1090-2422
DOI:10.1016/j.yexcr.2016.11.023