Extensive association of HuR with hnRNP proteins within immunoselected hnRNP and mRNP complexes
- Resource Type
- Authors
- Apostolia Guialis; Christina Papadopoulou; Meropi Patrinou-Georgoula
- Source
- Subject
- Heterogeneous nuclear ribonucleoprotein
genetic processes
RNA, Messenger/metabolism
RNA-binding protein
environment and public health
Biochemistry
Heterogeneous-Nuclear Ribonucleoproteins
ELAV-Like Protein 1
Analytical Chemistry
Mice
Heterogeneous-Nuclear Ribonucleoprotein Group A-B/chemistry/genetics/metabolism
RNA-Protein Interaction
Heterogeneous-Nuclear Ribonucleoprotein Group A-B
Ribonucleoproteins/chemistry/*metabolism
RNA Processing, Post-Transcriptional
Ribonucleoprotein
Microscopy, Confocal
Heterogeneous-Nuclear Ribonucleoproteins/chemistry/*metabolism
RNA-Binding Proteins
Antibodies, Monoclonal
Translation (biology)
RNA-Binding Proteins/chemistry/*metabolism
Cell biology
ELAV Proteins
Ribonucleoproteins
Antigens, Surface
Recombinant Fusion Proteins
RNA Splicing
Biophysics
Context (language use)
Biology
Polyadenylation
Cell Line
Animals
Humans
Immunoprecipitation
snRNP
RNA, Messenger
Molecular Biology
Cell Nucleus
Binding Sites
Recombinant Fusion Proteins/chemistry/genetics/metabolism
Molecular biology
KH domain
Antigens, Surface/chemistry/*metabolism
Protein Structure, Tertiary
Multiprotein Complexes
Cell Nucleus/metabolism
health occupations
Heat-Shock Response
- Language
- English
Regulated gene expression at the post-transcriptional level in higher eukaryotes is based on a network of interactions among RNA-binding proteins (RBPs) operating within multifactorial ribonucleoprotein (RNP) complexes, notably heterogeneous nuclear ribonucleoprotein (hnRNP) and mRNP complexes. We are interested in interactions involving hnRNP proteins participating in several steps of mRNA processing (mainly pre-mRNA splicing) and HuR with an established role in stability/translation of associated mRNAs. hnRNP and HuR proteins have a major nucleoplasmic localization and ability to shuttle between nucleus and cytoplasm. We report here on interactions between hnRNP and HuR proteins that were identified in the context of isolated hnRNP and mRNP complexes. This was done by the application of immunoprecipitation and pull-down assays on different sub-cellular fractions prepared from cells of human and mouse origin, as well as in vivo localization studies. A range of specific associations of HuR with the shuttling hnRNP A1 and A3 and the non-shuttling hnRNP C1/C2 was identified and ascribed discrete properties with respect to stability to RNase A and increasing salt, as well as to cellular distribution. The likelihood of a biological relevance of these associations was tested under heat shock conditions in growing cells, which appeared to affect both the sub-nuclear distribution and interaction of HuR with hnRNPs. The establishment of an extensive association of HuR with hnRNP components of nuclear hnRNP/mRNP and cytoplasmic mRNP complexes supports its broader participation in mRNA processing events than initially anticipated. Biochim Biophys Acta