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dc.contributor.editorZimmermann, Richard
dc.contributor.editorLang, Sven
dc.date.accessioned2022-06-21T08:35:37Z
dc.date.available2022-06-21T08:35:37Z
dc.date.issued2022
dc.identifierONIX_20220621_9783036540948_11
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/84433
dc.description.abstractProtein 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.
dc.languageEnglish
dc.subject.classificationbic Book Industry Communication::G Reference, information & interdisciplinary subjects::GP Research & information: general
dc.subject.classificationbic Book Industry Communication::P Mathematics & science::PS Biology, life sciences
dc.subject.otherchaperones
dc.subject.othercontact sites
dc.subject.otherendoplasmic reticulum
dc.subject.otherER-SURF
dc.subject.othermembrane extraction
dc.subject.othermitochondria
dc.subject.otherprotein targeting
dc.subject.otherbimolecular luminescence complementation
dc.subject.othercompetition
dc.subject.othersplit luciferase
dc.subject.othermembrane proteins
dc.subject.otherprotein–protein interactions
dc.subject.otherSec61 complex
dc.subject.otherSec63
dc.subject.othersynthetic peptide complementation
dc.subject.otherTRAP complex
dc.subject.otherER protein translocase
dc.subject.othersignal peptide
dc.subject.otherprotein translocation
dc.subject.othernascent peptide chain
dc.subject.othermembrane insertion
dc.subject.othermolecular modelling
dc.subject.othermolecular dynamics simulations
dc.subject.othermolecular docking
dc.subject.othersignal peptidase
dc.subject.otherER translocon
dc.subject.othersignal recognition particle dependent protein targeting
dc.subject.otherSec61 dependent translocation
dc.subject.otherco-translational translocation
dc.subject.otherinhibitor
dc.subject.otherhigh throughput screening
dc.subject.otherSec61
dc.subject.otherSec62
dc.subject.otherfolding
dc.subject.otherinsertion
dc.subject.othermembrane protein
dc.subject.othertranslocon
dc.subject.otherribosome
dc.subject.othertransmembrane segment
dc.subject.otherlipid droplets
dc.subject.otherperoxisomes
dc.subject.otherPEX3
dc.subject.othermembrane protein insertion
dc.subject.otherlabel-free quantitative mass spectrometry
dc.subject.otherdifferential protein abundance analysis
dc.subject.otherZellweger syndrome
dc.subject.otherGET
dc.subject.otherprotein transport
dc.subject.otherSND
dc.subject.otherSRP
dc.subject.otherEMC
dc.subject.otherpositive-inside rule
dc.subject.otherhydrophobicity
dc.subject.othertransmembrane helix
dc.subject.othersignal recognition particle
dc.subject.othernascent polypeptide-associated complex
dc.subject.otherfidelity
dc.subject.othercyclotriazadisulfonamide
dc.subject.otherER quality control
dc.subject.otherDNAJC3
dc.subject.otherpreprotein
dc.subject.otherSec61 translocon
dc.subject.otherribosome stalling
dc.subject.othersignal sequence
dc.subject.otherSec61 translocase
dc.subject.otherNAC
dc.subject.othern/a
dc.titleMechanisms of ER Protein Import
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-4093-1
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036540948
oapen.relation.isbn9783036540931
oapen.pages258
oapen.place.publicationBasel


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