TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD

Kuniaki Saito, Toshinobu Fujiwara, Jun Katahira, Kunio Inoue, Hiroshi Sakamoto

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Hu proteins are RNA-binding proteins that are implicated in the control of stabilization, nuclear export, and/or translation of specific mRNAs with AU-rich elements (AREs) in the 3′-untranslated region. Three neuron-specific Hu proteins (HuD, HuB, and HuC), but not a ubiquitously expressed Hu protein HuR, have an activity to induce neurite outgrowth when they are overexpressed in a rat neuronal cell line PC12. Here we show that TAP/NXF1, the primary export receptor for the bulk mRNA, is a specific binding partner for HuD. In vitro binding experiments using recombinant proteins revealed that the interaction between TAP and HuD is direct and that HuD can form a ternary complex together with both TAP and RNA. Interestingly, HuR does not interact with TAP. These results suggest that HuD acts as a novel adaptor protein to recruit TAP for efficient export of ARE-containing mRNAs in neuronal cells.

Original languageEnglish
Pages (from-to)291-297
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume321
Issue number2
DOIs
Publication statusPublished - 2004 Aug 20
Externally publishedYes

Fingerprint

AU Rich Elements
RNA-Binding Proteins
Messenger RNA
Cell Nucleus Active Transport
Protein Biosynthesis
3' Untranslated Regions
Recombinant Proteins
Proteins
RNA
Neurons
Cell Line
Rats
Stabilization
Cells
Experiments

Keywords

  • AU-rich element
  • HuD
  • mRNA export
  • Neuron
  • TAP

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD. / Saito, Kuniaki; Fujiwara, Toshinobu; Katahira, Jun; Inoue, Kunio; Sakamoto, Hiroshi.

In: Biochemical and Biophysical Research Communications, Vol. 321, No. 2, 20.08.2004, p. 291-297.

Research output: Contribution to journalArticle

Saito, Kuniaki ; Fujiwara, Toshinobu ; Katahira, Jun ; Inoue, Kunio ; Sakamoto, Hiroshi. / TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD. In: Biochemical and Biophysical Research Communications. 2004 ; Vol. 321, No. 2. pp. 291-297.
@article{c2043db4b23d4aadac5651729f408249,
title = "TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD",
abstract = "Hu proteins are RNA-binding proteins that are implicated in the control of stabilization, nuclear export, and/or translation of specific mRNAs with AU-rich elements (AREs) in the 3′-untranslated region. Three neuron-specific Hu proteins (HuD, HuB, and HuC), but not a ubiquitously expressed Hu protein HuR, have an activity to induce neurite outgrowth when they are overexpressed in a rat neuronal cell line PC12. Here we show that TAP/NXF1, the primary export receptor for the bulk mRNA, is a specific binding partner for HuD. In vitro binding experiments using recombinant proteins revealed that the interaction between TAP and HuD is direct and that HuD can form a ternary complex together with both TAP and RNA. Interestingly, HuR does not interact with TAP. These results suggest that HuD acts as a novel adaptor protein to recruit TAP for efficient export of ARE-containing mRNAs in neuronal cells.",
keywords = "AU-rich element, HuD, mRNA export, Neuron, TAP",
author = "Kuniaki Saito and Toshinobu Fujiwara and Jun Katahira and Kunio Inoue and Hiroshi Sakamoto",
year = "2004",
month = "8",
day = "20",
doi = "10.1016/j.bbrc.2004.06.140",
language = "English",
volume = "321",
pages = "291--297",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD

AU - Saito, Kuniaki

AU - Fujiwara, Toshinobu

AU - Katahira, Jun

AU - Inoue, Kunio

AU - Sakamoto, Hiroshi

PY - 2004/8/20

Y1 - 2004/8/20

N2 - Hu proteins are RNA-binding proteins that are implicated in the control of stabilization, nuclear export, and/or translation of specific mRNAs with AU-rich elements (AREs) in the 3′-untranslated region. Three neuron-specific Hu proteins (HuD, HuB, and HuC), but not a ubiquitously expressed Hu protein HuR, have an activity to induce neurite outgrowth when they are overexpressed in a rat neuronal cell line PC12. Here we show that TAP/NXF1, the primary export receptor for the bulk mRNA, is a specific binding partner for HuD. In vitro binding experiments using recombinant proteins revealed that the interaction between TAP and HuD is direct and that HuD can form a ternary complex together with both TAP and RNA. Interestingly, HuR does not interact with TAP. These results suggest that HuD acts as a novel adaptor protein to recruit TAP for efficient export of ARE-containing mRNAs in neuronal cells.

AB - Hu proteins are RNA-binding proteins that are implicated in the control of stabilization, nuclear export, and/or translation of specific mRNAs with AU-rich elements (AREs) in the 3′-untranslated region. Three neuron-specific Hu proteins (HuD, HuB, and HuC), but not a ubiquitously expressed Hu protein HuR, have an activity to induce neurite outgrowth when they are overexpressed in a rat neuronal cell line PC12. Here we show that TAP/NXF1, the primary export receptor for the bulk mRNA, is a specific binding partner for HuD. In vitro binding experiments using recombinant proteins revealed that the interaction between TAP and HuD is direct and that HuD can form a ternary complex together with both TAP and RNA. Interestingly, HuR does not interact with TAP. These results suggest that HuD acts as a novel adaptor protein to recruit TAP for efficient export of ARE-containing mRNAs in neuronal cells.

KW - AU-rich element

KW - HuD

KW - mRNA export

KW - Neuron

KW - TAP

UR - http://www.scopus.com/inward/record.url?scp=3242808974&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=3242808974&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2004.06.140

DO - 10.1016/j.bbrc.2004.06.140

M3 - Article

C2 - 15358174

AN - SCOPUS:3242808974

VL - 321

SP - 291

EP - 297

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -