Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution (Q27640483)

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18 December 2019

title

Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution (English)

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18 December 2019

1

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18 December 2019

author name string

David Neuhaus

series ordinal

2

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18 December 2019

Murray Stewart

series ordinal

3

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18 December 2019

language of work or name

English

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publication date

1 February 2003

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Journal of Molecular Biology

18 December 2019

published in

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18 December 2019

volume

326

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18 December 2019

issue

3

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18 December 2019

page(s)

849-858

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Protein and RNA export from the nucleus

18 December 2019

cites work

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Nuclear export of mRNA by TAP/NXF1 requires two nucleoporin-binding sites but not p15.

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Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores

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The mRNA export in Caenorhabditis elegans is mediated by Ce-NXF-1, an ortholog of human TAP/NXF and Saccharomyces cerevisiae Mex67p

7 January 2021

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The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences

7 January 2021

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The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain

7 January 2021

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The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor

7 January 2021

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Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor

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In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap

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Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1

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The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates

7 January 2021

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Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins

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Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex

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The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm

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Kinetic analysis of translocation through nuclear pore complexes

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Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import.

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Proteomic analysis of nucleoporin interacting proteins

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Comparative Spatial Localization of Protein-A-Tagged and Authentic Yeast Nuclear Pore Complex Proteins by Immunogold Electron Microscopy

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Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication

7 January 2021

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7 January 2021

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The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex

7 January 2021

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Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta

7 January 2021

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7 January 2021

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7 January 2021

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10.1016/S0022-2836(02)01474-2

7 January 2021

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12581645%20AND%20SRC:MED&resulttype=core&format=json

18 December 2019

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