Mechanisms of ER protein import:
Protein import into the endoplasmic reticulum (ER) is the first step in the biogenesis of approximately 10,000 different soluble and membrane proteins of human cells, which amounts to about 30% of the proteome. Most of these proteins fulfill their functions either in the membrane or lumen of the ER...
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| Sprache: | English |
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[2022]
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| Zusammenfassung: | Protein import into the endoplasmic reticulum (ER) is the first step in the biogenesis of approximately 10,000 different soluble and membrane proteins of human cells, which amounts to about 30% of the proteome. Most of these proteins fulfill their functions either in the membrane or lumen of the ER plus the nuclear envelope, in one of the organelles of the pathways for endo- and exocytosis (ERGIC, Golgi apparatus, endosome, lysosome, and trafficking vesicles), or at the cell surface as plasma membrane or secreted proteins. An increasing number of membrane proteins destined to lipid droplets, peroxisomes or mitochondria are first targeted to and inserted into the ER membrane prior to their integration into budding lipid droplets or peroxisomes or prior to their delivery to mitochondria via the ER-SURF pathway. ER protein import involves two stages, ER targeting, which guarantees membrane specificity, and the insertion of nascent membrane proteins into or translocation of soluble precursor polypeptides across the ER membrane. In most cases, both processes depend on amino-terminal signal peptides or transmembrane helices, which serve as signal peptide equivalents. However, the targeting reaction can also involve the ER targeting of specific mRNAs or ribosome–nascent chain complexes. Both processes may occur co- or post-translationally and are facilitated by various sophisticated machineries, which reside in the cytosol and the ER membrane, respectively. Except for resident ER and mitochondrial membrane proteins, the mature proteins are delivered to their functional locations by vesicular transport. |
| Beschreibung: | Titelrückseite: This is a reprint of articles from the Special Issue published online in the open access journal International Journal of Molecular Sciences (ISSN 1422-0067) (available at: www.mdpi.com/journal/ ijms/special_issues/mechanisms_ER_protein_import). |
| Beschreibung: | 1 Online-Ressource (ix, 246 Seiten) |
| ISBN: | 9783036540931 |
| DOI: | 10.3390/books978-3-0365-4093-1 |
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| 520 | 3 | |a Protein import into the endoplasmic reticulum (ER) is the first step in the biogenesis of approximately 10,000 different soluble and membrane proteins of human cells, which amounts to about 30% of the proteome. Most of these proteins fulfill their functions either in the membrane or lumen of the ER plus the nuclear envelope, in one of the organelles of the pathways for endo- and exocytosis (ERGIC, Golgi apparatus, endosome, lysosome, and trafficking vesicles), or at the cell surface as plasma membrane or secreted proteins. An increasing number of membrane proteins destined to lipid droplets, peroxisomes or mitochondria are first targeted to and inserted into the ER membrane prior to their integration into budding lipid droplets or peroxisomes or prior to their delivery to mitochondria via the ER-SURF pathway. ER protein import involves two stages, ER targeting, which guarantees membrane specificity, and the insertion of nascent membrane proteins into or translocation of soluble precursor polypeptides across the ER membrane. In most cases, both processes depend on amino-terminal signal peptides or transmembrane helices, which serve as signal peptide equivalents. However, the targeting reaction can also involve the ER targeting of specific mRNAs or ribosome–nascent chain complexes. Both processes may occur co- or post-translationally and are facilitated by various sophisticated machineries, which reside in the cytosol and the ER membrane, respectively. Except for resident ER and mitochondrial membrane proteins, the mature proteins are delivered to their functional locations by vesicular transport. | |
| 650 | 0 | 7 | |a Endoplasmatisches Retikulum |0 (DE-588)4152184-5 |2 gnd |9 rswk-swf |
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| 653 | |a chaperones | ||
| 653 | |a contact sites | ||
| 653 | |a endoplasmic reticulum | ||
| 653 | |a ER-SURF | ||
| 653 | |a membrane extraction | ||
| 653 | |a mitochondria | ||
| 653 | |a protein targeting | ||
| 653 | |a bimolecular luminescence complementation | ||
| 653 | |a competition | ||
| 653 | |a split luciferase | ||
| 653 | |a membrane proteins | ||
| 653 | |a protein–protein interactions | ||
| 653 | |a Sec61 complex | ||
| 653 | |a Sec63 | ||
| 653 | |a synthetic peptide complementation | ||
| 653 | |a TRAP complex | ||
| 653 | |a ER protein translocase | ||
| 653 | |a signal peptide | ||
| 653 | |a protein translocation | ||
| 653 | |a nascent peptide chain | ||
| 653 | |a membrane insertion | ||
| 653 | |a molecular modelling | ||
| 653 | |a molecular dynamics simulations | ||
| 653 | |a molecular docking | ||
| 653 | |a signal peptidase | ||
| 653 | |a ER translocon | ||
| 653 | |a signal recognition particle dependent protein targeting | ||
| 653 | |a Sec61 dependent translocation | ||
| 653 | |a co-translational translocation | ||
| 653 | |a inhibitor | ||
| 653 | |a high throughput screening | ||
| 653 | |a Sec61 | ||
| 653 | |a Sec62 | ||
| 653 | |a folding | ||
| 653 | |a insertion | ||
| 653 | |a membrane protein | ||
| 653 | |a translocon | ||
| 653 | |a ribosome | ||
| 653 | |a transmembrane segment | ||
| 653 | |a lipid droplets | ||
| 653 | |a peroxisomes | ||
| 653 | |a PEX3 | ||
| 653 | |a membrane protein insertion | ||
| 653 | |a label-free quantitative mass spectrometry | ||
| 653 | |a differential protein abundance analysis | ||
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Datensatz im Suchindex
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| author2 | Zimmermann, Richard 1951- Lang, Sven 1982- |
| author2_role | edt edt |
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| author_GND | (DE-588)1080008659 (DE-588)1147159580 |
| author_facet | Zimmermann, Richard 1951- Lang, Sven 1982- |
| building | Verbundindex |
| bvnumber | BV048447782 |
| classification_rvk | WE 2401 WE 3150 |
| collection | ZDB-94-OAB |
| ctrlnum | (OCoLC)1344242544 (DE-599)HEB497484277 |
| discipline | Biologie |
| discipline_str_mv | Biologie |
| doi_str_mv | 10.3390/books978-3-0365-4093-1 |
| format | Electronic eBook |
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| indexdate | 2025-01-23T09:01:00Z |
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| isbn | 9783036540931 |
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| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | marc |
| spelling | Mechanisms of ER protein import editors Richard Zimmermann, Sven Lang Basel MDPI - Multidisciplinary Digital Publishing Institute [2022] The Hague OAPEN FOUNDATION © 2022 1 Online-Ressource (ix, 246 Seiten) txt rdacontent c rdamedia cr rdacarrier Titelrückseite: This is a reprint of articles from the Special Issue published online in the open access journal International Journal of Molecular Sciences (ISSN 1422-0067) (available at: www.mdpi.com/journal/ ijms/special_issues/mechanisms_ER_protein_import). Protein import into the endoplasmic reticulum (ER) is the first step in the biogenesis of approximately 10,000 different soluble and membrane proteins of human cells, which amounts to about 30% of the proteome. Most of these proteins fulfill their functions either in the membrane or lumen of the ER plus the nuclear envelope, in one of the organelles of the pathways for endo- and exocytosis (ERGIC, Golgi apparatus, endosome, lysosome, and trafficking vesicles), or at the cell surface as plasma membrane or secreted proteins. An increasing number of membrane proteins destined to lipid droplets, peroxisomes or mitochondria are first targeted to and inserted into the ER membrane prior to their integration into budding lipid droplets or peroxisomes or prior to their delivery to mitochondria via the ER-SURF pathway. ER protein import involves two stages, ER targeting, which guarantees membrane specificity, and the insertion of nascent membrane proteins into or translocation of soluble precursor polypeptides across the ER membrane. In most cases, both processes depend on amino-terminal signal peptides or transmembrane helices, which serve as signal peptide equivalents. However, the targeting reaction can also involve the ER targeting of specific mRNAs or ribosome–nascent chain complexes. Both processes may occur co- or post-translationally and are facilitated by various sophisticated machineries, which reside in the cytosol and the ER membrane, respectively. Except for resident ER and mitochondrial membrane proteins, the mature proteins are delivered to their functional locations by vesicular transport. Endoplasmatisches Retikulum (DE-588)4152184-5 gnd rswk-swf Proteintransport (DE-588)4273577-4 gnd rswk-swf chaperones contact sites endoplasmic reticulum ER-SURF membrane extraction mitochondria protein targeting bimolecular luminescence complementation competition split luciferase membrane proteins protein–protein interactions Sec61 complex Sec63 synthetic peptide complementation TRAP complex ER protein translocase signal peptide protein translocation nascent peptide chain membrane insertion molecular modelling molecular dynamics simulations molecular docking signal peptidase ER translocon signal recognition particle dependent protein targeting Sec61 dependent translocation co-translational translocation inhibitor high throughput screening Sec61 Sec62 folding insertion membrane protein translocon ribosome transmembrane segment lipid droplets peroxisomes PEX3 membrane protein insertion label-free quantitative mass spectrometry differential protein abundance analysis (DE-588)4143413-4 Aufsatzsammlung gnd-content Endoplasmatisches Retikulum (DE-588)4152184-5 s Proteintransport (DE-588)4273577-4 s DE-604 Zimmermann, Richard 1951- (DE-588)1080008659 edt Lang, Sven 1982- (DE-588)1147159580 edt Erscheint auch als Druck-Ausgabe, Hardcover 978-3-0365-4094-8 https://directory.doabooks.org/handle/20.500.12854/84433 Verlag kostenfrei Volltext https://doi.org/10.3390/books978-3-0365-4093-1 Verlag kostenfrei Volltext |
| spellingShingle | Mechanisms of ER protein import Endoplasmatisches Retikulum (DE-588)4152184-5 gnd Proteintransport (DE-588)4273577-4 gnd |
| subject_GND | (DE-588)4152184-5 (DE-588)4273577-4 (DE-588)4143413-4 |
| title | Mechanisms of ER protein import |
| title_auth | Mechanisms of ER protein import |
| title_exact_search | Mechanisms of ER protein import |
| title_exact_search_txtP | Mechanisms of ER protein import |
| title_full | Mechanisms of ER protein import editors Richard Zimmermann, Sven Lang |
| title_fullStr | Mechanisms of ER protein import editors Richard Zimmermann, Sven Lang |
| title_full_unstemmed | Mechanisms of ER protein import editors Richard Zimmermann, Sven Lang |
| title_short | Mechanisms of ER protein import |
| title_sort | mechanisms of er protein import |
| topic | Endoplasmatisches Retikulum (DE-588)4152184-5 gnd Proteintransport (DE-588)4273577-4 gnd |
| topic_facet | Endoplasmatisches Retikulum Proteintransport Aufsatzsammlung |
| url | https://directory.doabooks.org/handle/20.500.12854/84433 https://doi.org/10.3390/books978-3-0365-4093-1 |
| work_keys_str_mv | AT zimmermannrichard mechanismsoferproteinimport AT langsven mechanismsoferproteinimport |