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Mechanisms of ER Protein Import
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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.
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Keywords
- bimolecular luminescence complementation
- Biology, Life Sciences
- chaperones
- co-translational translocation
- Competition
- contact sites
- cyclotriazadisulfonamide
- differential protein abundance analysis
- DNAJC3
- EMC
- Endoplasmic Reticulum
- ER protein translocase
- ER quality control
- ER translocon
- ER-SURF
- fidelity
- folding
- GET
- high throughput screening
- hydrophobicity
- inhibitor
- insertion
- label-free quantitative mass spectrometry
- lipid droplets
- Mathematics & science
- membrane extraction
- membrane insertion
- membrane protein
- membrane protein insertion
- membrane proteins
- Mitochondria
- molecular docking
- molecular dynamics simulations
- molecular modelling
- n/a
- NAC
- nascent peptide chain
- nascent polypeptide-associated complex
- Peroxisomes
- PEX3
- positive-inside rule
- preprotein
- protein targeting
- protein translocation
- protein transport
- protein–protein interactions
- Reference, information & interdisciplinary subjects
- Research & information: general
- ribosome
- ribosome stalling
- Sec61
- Sec61 complex
- Sec61 dependent translocation
- Sec61 translocase
- Sec61 translocon
- Sec62
- Sec63
- signal peptidase
- signal peptide
- signal recognition particle
- signal recognition particle dependent protein targeting
- signal sequence
- SND
- split luciferase
- SRP
- synthetic peptide complementation
- translocon
- transmembrane helix
- transmembrane segment
- TRAP complex
- Zellweger syndrome
Links
DOI: 10.3390/books978-3-0365-4093-1Editions