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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MDPI - Multidisciplinary Digital Publishing Institute
2022
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| Mynediad Ar-lein: | ONIX_20220621_9783036540948_11 |
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| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-84433 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2022 |
| publishDateRange | 2022 |
| publishDateSort | 2022 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-844332024-03-28T03:33:56Z Mechanisms of ER Protein Import Zimmermann, Richard Lang, Sven 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 Zellweger syndrome GET protein transport SND SRP EMC positive-inside rule hydrophobicity transmembrane helix signal recognition particle nascent polypeptide-associated complex fidelity cyclotriazadisulfonamide ER quality control DNAJC3 preprotein Sec61 translocon ribosome stalling signal sequence Sec61 translocase NAC n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences 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. 2022-06-21T08:35:37Z 2022-06-21T08:35:37Z 2022 book ONIX_20220621_9783036540948_11 9783036540948 9783036540931 https://directory.doabooks.org/handle/20.500.12854/84433 eng application/octet-stream Attribution 4.0 International https://mdpi.com/books/pdfview/book/5416 https://mdpi.com/books/pdfview/book/5416 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-4093-1 10.3390/books978-3-0365-4093-1 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036540948 9783036540931 258 Basel open access |
| spellingShingle | 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 Zellweger syndrome GET protein transport SND SRP EMC positive-inside rule hydrophobicity transmembrane helix signal recognition particle nascent polypeptide-associated complex fidelity cyclotriazadisulfonamide ER quality control DNAJC3 preprotein Sec61 translocon ribosome stalling signal sequence Sec61 translocase NAC n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences Mechanisms of ER Protein Import |
| title | Mechanisms of ER Protein Import |
| title_full | Mechanisms of ER Protein Import |
| title_fullStr | Mechanisms of ER Protein Import |
| title_full_unstemmed | Mechanisms of ER Protein Import |
| title_short | Mechanisms of ER Protein Import |
| title_sort | mechanisms of er protein import |
| topic | 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 Zellweger syndrome GET protein transport SND SRP EMC positive-inside rule hydrophobicity transmembrane helix signal recognition particle nascent polypeptide-associated complex fidelity cyclotriazadisulfonamide ER quality control DNAJC3 preprotein Sec61 translocon ribosome stalling signal sequence Sec61 translocase NAC n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| topic_facet | 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 Zellweger syndrome GET protein transport SND SRP EMC positive-inside rule hydrophobicity transmembrane helix signal recognition particle nascent polypeptide-associated complex fidelity cyclotriazadisulfonamide ER quality control DNAJC3 preprotein Sec61 translocon ribosome stalling signal sequence Sec61 translocase NAC n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| url | ONIX_20220621_9783036540948_11 |