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Hel-N1/Hel-N2 proteins are bound to poly(A)+ mRNA in granular RNP structures and are implicated in neuronal differentiation.

Publication ,  Journal Article
Gao, FB; Keene, JD
Published in: J Cell Sci
March 1996

Human proteins Hel-N1 and Hel-N2 contain three RNA recognition motifs (RRMs), and are members of a family of proteins highly homologous to Drosophila ELAV, which is essential for neuronal differentiation. Both proteins bind to A+U-rich 3' untranslated regions of a variety of growth-related mRNAs in vitro. Here we demonstrate that in medulloblastoma cells derived from childhood brain tumors, Hel-N1 and Hel-N2 are mainly expressed in the cytoplasm, but are detectable in the nucleus. Both proteins are associated with polysomes and can be UV-crosslinked to poly(A)+ mRNA in cell extracts. In the cytoplasm the Hel-N1 protein family resides in granular structures that may contain multiple protein molecules bound to each mRNA. Evidence supporting this multimeric ribonucleoprotein (RNP) model includes in vitro reconstitution and competition experiments in which addition of a single RRM (RRM3) can alter complex formation. As in medulloblastoma cells, the Hel-N1 protein family is present in granular particles in the soma and the proximal regions of dendrites of cultured neurons, and colocalizes with ribosomes. In addition, we demonstrate that expression of the Hel-N1 protein family is up-regulated during neuronal differentiation of embryonic carcinoma P19 cells. Our data suggest that the Hel-N1 protein family is associated with the translational apparatus and implicated in both mRNA metabolism and neuronal differentiation. Furthermore, our findings open the possibility that these proteins participate in mRNA homeostasis in the dendrites and soma of mature neurons.

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Published In

J Cell Sci

DOI

ISSN

0021-9533

Publication Date

March 1996

Volume

109 ( Pt 3)

Start / End Page

579 / 589

Location

England

Related Subject Headings

  • Up-Regulation
  • Tumor Cells, Cultured
  • Ribonucleoproteins
  • Rats
  • RNA, Messenger
  • Protein Biosynthesis
  • Phenotype
  • Neurons
  • Nerve Tissue Proteins
  • Molecular Sequence Data
 

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Gao, F. B., & Keene, J. D. (1996). Hel-N1/Hel-N2 proteins are bound to poly(A)+ mRNA in granular RNP structures and are implicated in neuronal differentiation. J Cell Sci, 109 ( Pt 3), 579–589. https://doi.org/10.1242/jcs.109.3.579
Gao, F. B., and J. D. Keene. “Hel-N1/Hel-N2 proteins are bound to poly(A)+ mRNA in granular RNP structures and are implicated in neuronal differentiation.J Cell Sci 109 ( Pt 3) (March 1996): 579–89. https://doi.org/10.1242/jcs.109.3.579.
Gao, F. B., and J. D. Keene. “Hel-N1/Hel-N2 proteins are bound to poly(A)+ mRNA in granular RNP structures and are implicated in neuronal differentiation.J Cell Sci, vol. 109 ( Pt 3), Mar. 1996, pp. 579–89. Pubmed, doi:10.1242/jcs.109.3.579.
Journal cover image

Published In

J Cell Sci

DOI

ISSN

0021-9533

Publication Date

March 1996

Volume

109 ( Pt 3)

Start / End Page

579 / 589

Location

England

Related Subject Headings

  • Up-Regulation
  • Tumor Cells, Cultured
  • Ribonucleoproteins
  • Rats
  • RNA, Messenger
  • Protein Biosynthesis
  • Phenotype
  • Neurons
  • Nerve Tissue Proteins
  • Molecular Sequence Data