Transportin

Nuclear transport receptor of a novel nuclear protein import pathway

Sara Nakielny, Mikiko C. Siomi, Haruhiko Siomi, W. Matthew Michael, Victoria Pollard, Gideon Dreyfuss

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

Many nuclear proteins are imported into the cell nucleus by the 'classical' nuclear localization signal (NLS)-mediated import pathway. In this pathway, a sequence rich in basic residues in the protein interacts with a heterodimeric complex termed importin and this, along with the GTPase Ran, mediates nuclear import of the NLS-bearing protein. The heterogeneous nuclear ribonucleoprotein (hnRNP) A1 protein contains a novel nuclear localization sequence, termed M9, that does not contain any clusters of basic residues. Very recently, we showed that M9 directs import into the nucleus by a novel protein import pathway distinct from the classical NLS pathway. A 90- kilodalton protein termed transportin was identified as a protein that specifically interacts with wild-type M9 but not transport-defective M9 mutants. Transportin and an ATP-regenerating system were found to be necessary and sufficient for import of M9-containing proteins in an in vitro import assay. In this report, we provide additional evidence that transportin can interact directly with M9-containing proteins and also show that it can mediate import of full-length hnRNP A1. In addition, Ran, or a Ran-binding protein, is identified as a second protein component of this novel nuclear import pathway. Transportin relatives from Saccharomyces cerevisiae which likely serve as additional nuclear transport receptors are described.

Original languageEnglish
Pages (from-to)261-266
Number of pages6
JournalExperimental Cell Research
Volume229
Issue number2
DOIs
Publication statusPublished - 1996 Dec 15
Externally publishedYes

Fingerprint

Karyopherins
Cell Nucleus Active Transport
Cytoplasmic and Nuclear Receptors
Nuclear Proteins
Nuclear Localization Signals
Proteins
Heterogeneous-Nuclear Ribonucleoproteins
ran GTP-Binding Protein
GTP Phosphohydrolases
Cell Nucleus
Saccharomyces cerevisiae
Signal Transduction
Carrier Proteins
Adenosine Triphosphate

ASJC Scopus subject areas

  • Cell Biology

Cite this

Transportin : Nuclear transport receptor of a novel nuclear protein import pathway. / Nakielny, Sara; Siomi, Mikiko C.; Siomi, Haruhiko; Michael, W. Matthew; Pollard, Victoria; Dreyfuss, Gideon.

In: Experimental Cell Research, Vol. 229, No. 2, 15.12.1996, p. 261-266.

Research output: Contribution to journalArticle

Nakielny, S, Siomi, MC, Siomi, H, Michael, WM, Pollard, V & Dreyfuss, G 1996, 'Transportin: Nuclear transport receptor of a novel nuclear protein import pathway', Experimental Cell Research, vol. 229, no. 2, pp. 261-266. https://doi.org/10.1006/excr.1996.0369
Nakielny, Sara ; Siomi, Mikiko C. ; Siomi, Haruhiko ; Michael, W. Matthew ; Pollard, Victoria ; Dreyfuss, Gideon. / Transportin : Nuclear transport receptor of a novel nuclear protein import pathway. In: Experimental Cell Research. 1996 ; Vol. 229, No. 2. pp. 261-266.
@article{4ad987bc375e4dcd9ce4943736443262,
title = "Transportin: Nuclear transport receptor of a novel nuclear protein import pathway",
abstract = "Many nuclear proteins are imported into the cell nucleus by the 'classical' nuclear localization signal (NLS)-mediated import pathway. In this pathway, a sequence rich in basic residues in the protein interacts with a heterodimeric complex termed importin and this, along with the GTPase Ran, mediates nuclear import of the NLS-bearing protein. The heterogeneous nuclear ribonucleoprotein (hnRNP) A1 protein contains a novel nuclear localization sequence, termed M9, that does not contain any clusters of basic residues. Very recently, we showed that M9 directs import into the nucleus by a novel protein import pathway distinct from the classical NLS pathway. A 90- kilodalton protein termed transportin was identified as a protein that specifically interacts with wild-type M9 but not transport-defective M9 mutants. Transportin and an ATP-regenerating system were found to be necessary and sufficient for import of M9-containing proteins in an in vitro import assay. In this report, we provide additional evidence that transportin can interact directly with M9-containing proteins and also show that it can mediate import of full-length hnRNP A1. In addition, Ran, or a Ran-binding protein, is identified as a second protein component of this novel nuclear import pathway. Transportin relatives from Saccharomyces cerevisiae which likely serve as additional nuclear transport receptors are described.",
author = "Sara Nakielny and Siomi, {Mikiko C.} and Haruhiko Siomi and Michael, {W. Matthew} and Victoria Pollard and Gideon Dreyfuss",
year = "1996",
month = "12",
day = "15",
doi = "10.1006/excr.1996.0369",
language = "English",
volume = "229",
pages = "261--266",
journal = "Experimental Cell Research",
issn = "0014-4827",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Transportin

T2 - Nuclear transport receptor of a novel nuclear protein import pathway

AU - Nakielny, Sara

AU - Siomi, Mikiko C.

AU - Siomi, Haruhiko

AU - Michael, W. Matthew

AU - Pollard, Victoria

AU - Dreyfuss, Gideon

PY - 1996/12/15

Y1 - 1996/12/15

N2 - Many nuclear proteins are imported into the cell nucleus by the 'classical' nuclear localization signal (NLS)-mediated import pathway. In this pathway, a sequence rich in basic residues in the protein interacts with a heterodimeric complex termed importin and this, along with the GTPase Ran, mediates nuclear import of the NLS-bearing protein. The heterogeneous nuclear ribonucleoprotein (hnRNP) A1 protein contains a novel nuclear localization sequence, termed M9, that does not contain any clusters of basic residues. Very recently, we showed that M9 directs import into the nucleus by a novel protein import pathway distinct from the classical NLS pathway. A 90- kilodalton protein termed transportin was identified as a protein that specifically interacts with wild-type M9 but not transport-defective M9 mutants. Transportin and an ATP-regenerating system were found to be necessary and sufficient for import of M9-containing proteins in an in vitro import assay. In this report, we provide additional evidence that transportin can interact directly with M9-containing proteins and also show that it can mediate import of full-length hnRNP A1. In addition, Ran, or a Ran-binding protein, is identified as a second protein component of this novel nuclear import pathway. Transportin relatives from Saccharomyces cerevisiae which likely serve as additional nuclear transport receptors are described.

AB - Many nuclear proteins are imported into the cell nucleus by the 'classical' nuclear localization signal (NLS)-mediated import pathway. In this pathway, a sequence rich in basic residues in the protein interacts with a heterodimeric complex termed importin and this, along with the GTPase Ran, mediates nuclear import of the NLS-bearing protein. The heterogeneous nuclear ribonucleoprotein (hnRNP) A1 protein contains a novel nuclear localization sequence, termed M9, that does not contain any clusters of basic residues. Very recently, we showed that M9 directs import into the nucleus by a novel protein import pathway distinct from the classical NLS pathway. A 90- kilodalton protein termed transportin was identified as a protein that specifically interacts with wild-type M9 but not transport-defective M9 mutants. Transportin and an ATP-regenerating system were found to be necessary and sufficient for import of M9-containing proteins in an in vitro import assay. In this report, we provide additional evidence that transportin can interact directly with M9-containing proteins and also show that it can mediate import of full-length hnRNP A1. In addition, Ran, or a Ran-binding protein, is identified as a second protein component of this novel nuclear import pathway. Transportin relatives from Saccharomyces cerevisiae which likely serve as additional nuclear transport receptors are described.

UR - http://www.scopus.com/inward/record.url?scp=0030589598&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030589598&partnerID=8YFLogxK

U2 - 10.1006/excr.1996.0369

DO - 10.1006/excr.1996.0369

M3 - Article

VL - 229

SP - 261

EP - 266

JO - Experimental Cell Research

JF - Experimental Cell Research

SN - 0014-4827

IS - 2

ER -