| Tartalom: |
http://dx.doi.org/10.1083/jcb.201409127 |
| Archívum: |
MTA Könyvtár |
| Gyűjtemény: |
Status = Published
Type = Article
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| Cím: |
Diffusion and retention are major determinants of protein targeting to the inner nuclear membrane
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| Létrehozó: |
Ungricht, Rosemarie
Klann, Michael
Horváth, Péter
Kutay, Ulrike
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| Dátum: |
2015
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| Téma: |
QH3011 Biochemistry / biokémia
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| Tartalmi leírás: |
Newly synthesized membrane proteins are constantly sorted from the endoplasmic reticulum (ER) to various membranous compartments. How proteins specifically enrich at the inner nuclear membrane (INM) is not well understood. We have established a visual in vitro assay to measure kinetics and investigate requirements of protein targeting to the INM. Using human LBR, SUN2, and LAP2 beta as model substrates, we show that INM targeting is energy-dependent but distinct from import of soluble cargo. Accumulation of proteins at the INM relies on both a highly interconnected ER network, which is affected by energy depletion, and an efficient immobilization step at the INM. Nucleoporin depletions suggest that translocation through nuclear pore complexes (NPCs) is rate-limiting and restricted by the central NPC scaffold. Our experimental data combined with mathematical modeling support a diffusion-retention-based mechanism of INM targeting. We experimentally confirmed the sufficiency of diffusion and retention using an artificial reporter lacking natural sorting signals that recapitulates the energy dependence of the process in vivo.
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| Típus: |
Article
PeerReviewed
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| Formátum: |
text
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| Azonosító: |
Ungricht, Rosemarie and Klann, Michael and Horváth, Péter and Kutay, Ulrike (2015) Diffusion and retention are major determinants of protein targeting to the inner nuclear membrane. Journal of Cell Biology, 209 (5). pp. 687-703. ISSN 0021-9525
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