Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope.

Saksena S; Summers MD; Burks JK; Johnson AE; Braunagel SC

doi:10.1038/nsmb1098

Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope.

Affiliations

1. Department of Biochemistry and Biophysics, Texas A&M University, USA.
Authors
Saksena S¹
(1 author)

Nature Structural & Molecular Biology, 21 May 2006, 13(6):500-508
https://doi.org/10.1038/nsmb1098 PMID: 16715095

A comment on this article appears in "A sorting importin on Sec61." Nat Struct Mol Biol. 2006 Jun;13(6):476-8.

Abstract

A viral inner nuclear membrane-sorting motif sequence (INM-SM) was used to identify proteins that recognize integral membrane proteins destined for the INM. Herein we describe importin-alpha-16, a membrane-associated isoform of Spodoptera frugiperda importin-alpha that contains the C-terminal amino acid residues comprising armadillo helical-repeat domains 7-10. In the endoplasmic reticulum (ER) membrane, importin-alpha-16 is adjacent to the translocon protein Sec61alpha. Importin-alpha-16 cross-links to the INM-SM sequence as it emerges from the ribosomal tunnel and remains adjacent to the INM-SM after INM-SM integration into the ER membrane and release from the translocon. Cross-linking results suggest that importin-alpha-16 discriminates between INM- and non-INM-directed proteins. Thus, it seems that during and after cotranslational membrane integration, importin-alpha-16 is involved in the trafficking of integral membrane proteins to the INM.

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Read article at publisher's site: https://doi.org/10.1038/nsmb1098

References

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Funding

Funders who supported this work.

NIGMS NIH HHS (1)

Grant ID: R01 GM26494
9 publications

Search life-sciences literature (45,104,206 articles, preprints and more)

Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope.

Affiliations

Authors

Abstract

Full text links

References

Pushing the envelope: structure, function, and dynamics of the nuclear periphery.

Cotranslational integration and initial sorting at the endoplasmic reticulum translocon of proteins destined for the inner nuclear membrane.

Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: facilitated trafficking to the inner nuclear membrane.

Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore.

N-terminal sequences from Autographa californica nuclear polyhedrosis virus envelope proteins ODV-E66 and ODV-E25 are sufficient to direct reporter proteins to the nuclear envelope, intranuclear microvesicles and the envelope of occlusion derived virus.

Effects of deletion and overexpression of the Autographa californica nuclear polyhedrosis virus FP25K gene on synthesis of two occlusion-derived virus envelope proteins and their transport into virus-induced intranuclear membranes.

Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore.

The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation.

Molecular cloning and characterization of the translationally controlled tumor protein gene in Bombyx mori.

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.

Citations & impact

Impact metrics

Citations of article over time

Alternative metrics

Smart citations by scite.ai
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1038/nsmb1098

Article citations

Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.

Lamin is essential for nuclear localization of the GPI synthesis enzyme PIG-B and GPI-anchored protein production in Drosophila.

A nuclear localization signal targets tail-anchored membrane proteins to the inner nuclear envelope in plants.

Myosin-1C uses a novel phosphoinositide-dependent pathway for nuclear localization.

Per os infectivity factors: a complicated and evolutionarily conserved entry machinery of baculovirus.

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Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope.

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