Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13

Fulvia Bono; Atlanta G Cook; Marlene Grünwald; Judith Ebert; Elena Conti

doi:10.1016/j.molcel.2010.01.007

Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13

Fulvia Bono, Atlanta G Cook, Marlene Grünwald, Judith Ebert, Elena Conti

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.

Original language	English
Pages (from-to)	211-22
Number of pages	12
Journal	Molecular Cell
Volume	37
Issue number	2
Early online date	28 Jan 2010
DOIs	https://doi.org/10.1016/j.molcel.2010.01.007
Publication status	Published - 29 Jan 2010

Keywords / Materials (for Non-textual outputs)

Active Transport, Cell Nucleus
Amino Acid Sequence
Animals
Binding Sites
Crystallography, X-Ray
Drosophila
Drosophila Proteins
Humans
Karyopherins
Molecular Sequence Data
Nuclear Proteins
Protein Structure, Tertiary
RNA, Messenger
RNA-Binding Proteins
Sequence Alignment
ran GTP-Binding Protein

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title = "Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13",

abstract = "Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.",

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doi = "10.1016/j.molcel.2010.01.007",

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AU - Grünwald, Marlene

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AU - Conti, Elena

PY - 2010/1/29

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N2 - Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.

AB - Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.

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KW - Protein Structure, Tertiary

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JO - Molecular Cell

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Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13

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