Efficient protein targeting to the inner nuclear membrane requires atlastin-dependent maintenance of ER topology
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| 005 | 20190908091346.0 | ||
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| 008 | 180924e201708 xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.3929/ethz-b-000180500 |2 doi |
| 024 | 7 | 0 | |a 10.7554/elife.28202 |2 doi |
| 035 | |a (ETHRESEARCH)oai:www.research-collecti.ethz.ch:20.500.11850/180500 | ||
| 245 | 0 | 0 | |a Efficient protein targeting to the inner nuclear membrane requires atlastin-dependent maintenance of ER topology |h [Elektronische Daten] |c [Sumit Pawar, Rosemarie Ungricht, Peter Tiefenboeck, Jean-Christophe Leroux, Ulrike Kutay] |
| 506 | |a Open access |2 ethresearch | ||
| 520 | 3 | |a Newly synthesized membrane proteins are targeted to the inner nuclear membrane (INM) by diffusion within the membrane system of the endoplasmic reticulum (ER), translocation through nuclear pore complexes (NPCs) and retention on nuclear partners. Using a visual in vitro assay we previously showed that efficient protein targeting to the INM depends on nucleotide hydrolysis. We now reveal that INM targeting is GTP-dependent. Exploiting in vitro reconstitution and in vivo analysis of INM targeting, we establish that Atlastins, membrane-bound GTPases of the ER, sustain the efficient targeting of proteins to the INM by their continued activity in preserving ER topology. When ER topology is altered, the long-range diffusional exchange of proteins in the ER network and targeting efficiency to the INM are diminished. Highlighting the general importance of proper ER topology, we show that Atlastins also influence NPC biogenesis and timely exit of secretory cargo from the ER. | |
| 540 | |a Creative Commons Attribution 4.0 International |u http://creativecommons.org/licenses/by/4.0 |2 ethresearch | ||
| 700 | 1 | |a Pawar |D Sumit |e joint author | |
| 700 | 1 | |a Ungricht |D Rosemarie |e joint author | |
| 700 | 1 | |a Tiefenboeck |D Peter |e joint author | |
| 700 | 1 | |a Leroux |D Jean-Christophe |e joint author | |
| 700 | 1 | |a Kutay |D Ulrike |e joint author | |
| 773 | 0 | |t eLife |d Cambridge : eLife Sciences Publications |g 6, p. e28202 |x 2050-084X | |
| 856 | 4 | 0 | |u http://hdl.handle.net/20.500.11850/180500 |q text/html |z WWW-Backlink auf das Repository (Open access) |
| 908 | |D 1 |a Journal Article |2 ethresearch | ||
| 950 | |B ETHRESEARCH |P 856 |E 40 |u http://hdl.handle.net/20.500.11850/180500 |q text/html |z WWW-Backlink auf das Repository (Open access) | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Pawar |D Sumit |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Ungricht |D Rosemarie |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Tiefenboeck |D Peter |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Leroux |D Jean-Christophe |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Kutay |D Ulrike |e joint author | ||
| 950 | |B ETHRESEARCH |P 773 |E 0- |t eLife |d Cambridge : eLife Sciences Publications |g 6, p. e28202 |x 2050-084X | ||
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B ETHRESEARCH |F ETHRESEARCH |b ETHRESEARCH |j Journal Article |c Open access | ||