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The transport of integral membrane proteins across the nuclear pore complex
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Volume 3, Issue 4 July/August 2012
Pages 322 - 329
http://dx.doi.org/10.4161/nucl.20439
Keywords: inner nuclear membrane, intrinsically disordered, membrane protein, nuclear envelope, nuclear pore complex
Authors: Anne C. Meinema, Bert Poolman and Liesbeth M. Veenhoff
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- Anne C. Meinema
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Department of Biochemistry; Groningen Biomolecular Sciences and Biotechnology Institute; Netherlands Proteomics Centre; Zernike Institute for Advanced Materials; University of Groningen; Groningen, The Netherlands
- Bert Poolman
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Department of Biochemistry; Groningen Biomolecular Sciences and Biotechnology Institute; Netherlands Proteomics Centre; Zernike Institute for Advanced Materials; University of Groningen; Groningen, The Netherlands
- Liesbeth M. Veenhoff
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Corresponding author: l.m.veenhoff@rug.nl
Department of Neuroscience; University Medical Centre Groningen; University of Groningen; European Research Institute for the Biology of Ageing; Netherlands Proteomics Centre; The Netherlands
Abstract:
The nuclear envelope protects and organizes the genome. The nuclear pore complexes embedded in the nuclear envelope allow selective transport of macromolecules between the cytosol and nucleoplasm, and as such help to control the flow of information from DNA to RNA to proteins. A growing list of integral membrane proteins of the nuclear envelope are described to function in the organization of the genome, as well as the assembly of the NPCs. Here, we discuss how the nuclear pore complex may sort these proteins to obtain a specific protein composition of the inner membrane.
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AC Meinema, JK Laba, RA Hapsari, R Otten, FA Mulder, A Kralt, den Bogaart G van, CP Lusk, B Poolman, LM Veenhoff. Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science 2011; 333: 90-3
PMID: 21659568 DOI: 10.1126/science.1205741
Received: April 5, 2012; Accepted: April 19, 2012; Published Online: May 22, 2012
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