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...
Saved in:
HerausgeberIn: | |
---|---|
Sonstige: | |
Year of Publication: | 2022 |
Language: | English |
Physical Description: | 1 electronic resource (258 p.) |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
id |
993544642504498 |
---|---|
ctrlnum |
(CKB)5720000000008312 (oapen)https://directory.doabooks.org/handle/20.500.12854/84433 (EXLCZ)995720000000008312 |
collection |
bib_alma |
record_format |
marc |
spelling |
Zimmermann, Richard edt Mechanisms of ER Protein Import Basel MDPI - Multidisciplinary Digital Publishing Institute 2022 1 electronic resource (258 p.) text txt rdacontent computer c rdamedia online resource cr rdacarrier 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. English Research & information: general bicssc Biology, life sciences bicssc 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 3-0365-4094-6 3-0365-4093-8 Lang, Sven edt Zimmermann, Richard oth Lang, Sven oth |
language |
English |
format |
eBook |
author2 |
Lang, Sven Zimmermann, Richard Lang, Sven |
author_facet |
Lang, Sven Zimmermann, Richard Lang, Sven |
author2_variant |
r z rz s l sl |
author2_role |
HerausgeberIn Sonstige Sonstige |
title |
Mechanisms of ER Protein Import |
spellingShingle |
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_auth |
Mechanisms of ER Protein Import |
title_new |
Mechanisms of ER Protein Import |
title_sort |
mechanisms of er protein import |
publisher |
MDPI - Multidisciplinary Digital Publishing Institute |
publishDate |
2022 |
physical |
1 electronic resource (258 p.) |
isbn |
3-0365-4094-6 3-0365-4093-8 |
illustrated |
Not Illustrated |
work_keys_str_mv |
AT zimmermannrichard mechanismsoferproteinimport AT langsven mechanismsoferproteinimport |
status_str |
n |
ids_txt_mv |
(CKB)5720000000008312 (oapen)https://directory.doabooks.org/handle/20.500.12854/84433 (EXLCZ)995720000000008312 |
carrierType_str_mv |
cr |
is_hierarchy_title |
Mechanisms of ER Protein Import |
author2_original_writing_str_mv |
noLinkedField noLinkedField noLinkedField |
_version_ |
1796651434656137217 |
fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>04887nam-a2201117z--4500</leader><controlfield tag="001">993544642504498</controlfield><controlfield tag="005">20231214133054.0</controlfield><controlfield tag="006">m o d </controlfield><controlfield tag="007">cr|mn|---annan</controlfield><controlfield tag="008">202206s2022 xx |||||o ||| 0|eng d</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(CKB)5720000000008312</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(oapen)https://directory.doabooks.org/handle/20.500.12854/84433</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(EXLCZ)995720000000008312</subfield></datafield><datafield tag="041" ind1="0" ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Zimmermann, Richard</subfield><subfield code="4">edt</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Mechanisms of ER Protein Import</subfield></datafield><datafield tag="260" ind1=" " ind2=" "><subfield code="a">Basel</subfield><subfield code="b">MDPI - Multidisciplinary Digital Publishing Institute</subfield><subfield code="c">2022</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">1 electronic resource (258 p.)</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">computer</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">online resource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="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.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">English</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Research & information: general</subfield><subfield code="2">bicssc</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Biology, life sciences</subfield><subfield code="2">bicssc</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">chaperones</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">contact sites</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">endoplasmic reticulum</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">ER-SURF</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">membrane extraction</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">mitochondria</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">protein targeting</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">bimolecular luminescence complementation</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">competition</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">split luciferase</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">membrane proteins</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">protein-protein interactions</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec61 complex</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec63</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">synthetic peptide complementation</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">TRAP complex</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">ER protein translocase</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">signal peptide</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">protein translocation</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">nascent peptide chain</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">membrane insertion</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">molecular modelling</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">molecular dynamics simulations</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">molecular docking</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">signal peptidase</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">ER translocon</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">signal recognition particle dependent protein targeting</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec61 dependent translocation</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">co-translational translocation</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">inhibitor</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">high throughput screening</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec61</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec62</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">folding</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">insertion</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">membrane protein</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">translocon</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">ribosome</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">transmembrane segment</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">lipid droplets</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">peroxisomes</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">PEX3</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">membrane protein insertion</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">label-free quantitative mass spectrometry</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">differential protein abundance analysis</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Zellweger syndrome</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">GET</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">protein transport</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">SND</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">SRP</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">EMC</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">positive-inside rule</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">hydrophobicity</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">transmembrane helix</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">signal recognition particle</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">nascent polypeptide-associated complex</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">fidelity</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">cyclotriazadisulfonamide</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">ER quality control</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">DNAJC3</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">preprotein</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec61 translocon</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">ribosome stalling</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">signal sequence</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Sec61 translocase</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">NAC</subfield></datafield><datafield tag="776" ind1=" " ind2=" "><subfield code="z">3-0365-4094-6</subfield></datafield><datafield tag="776" ind1=" " ind2=" "><subfield code="z">3-0365-4093-8</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lang, Sven</subfield><subfield code="4">edt</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zimmermann, Richard</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lang, Sven</subfield><subfield code="4">oth</subfield></datafield><datafield tag="906" ind1=" " ind2=" "><subfield code="a">BOOK</subfield></datafield><datafield tag="ADM" ind1=" " ind2=" "><subfield code="b">2023-12-15 05:41:51 Europe/Vienna</subfield><subfield code="f">system</subfield><subfield code="c">marc21</subfield><subfield code="a">2022-07-02 22:45:44 Europe/Vienna</subfield><subfield code="g">false</subfield></datafield><datafield tag="AVE" ind1=" " ind2=" "><subfield code="i">DOAB Directory of Open Access Books</subfield><subfield code="P">DOAB Directory of Open Access Books</subfield><subfield code="x">https://eu02.alma.exlibrisgroup.com/view/uresolver/43ACC_OEAW/openurl?u.ignore_date_coverage=true&portfolio_pid=5337735330004498&Force_direct=true</subfield><subfield code="Z">5337735330004498</subfield><subfield code="b">Available</subfield><subfield code="8">5337735330004498</subfield></datafield></record></collection> |