The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.
Protein Translocation Across Biological Membranes
Abstract
Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts. How do proteins get where they need to go? The first steps are targeting to an organelle and efficient translocation across its limiting membrane. Given that most transport systems are exquisitely substrate specific, how are diverse protein sequences recognized for translocation? Are they translocated as linear polypeptide chains or after folding? During translocation, how are diverse amino acyl side chains accommodated? What are the proteins and the lipid environment that catalyze transport and couple it to energy? How is translocation coordinated with protein synthesis and folding, and how are partially translocated transmembrane proteins released into the lipid bilayer? We review here the marked progress of the past 35 years and salient questions for future work. Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts. How do proteins get where they need to go? The first steps are targeting to an organelle and efficient translocation across its limiting membrane. Given that most transport systems are exquisitely substrate specific, how are diverse protein sequences recognized for translocation? Are they translocated as linear polypeptide chains or after folding? During translocation, how are diverse amino acyl side chains accommodated? What are the proteins and the lipid environment that catalyze transport and couple it to energy? How is translocation coordinated with protein synthesis and folding, and how are partially translocated transmembrane proteins released into the lipid bilayer? We review here the marked progress of the past 35 years and salient questions for future work.
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“Cargo protein with a classic NLS requires a direct interaction with importin-α to be transported through the nuclear pore complex [31], [40], [45], [46], [47]”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [45]
In the citing paper
“Transportation of cargo protein in importin-α/−β protein complexes through the NPC requires energy derived from the activities of GTPases [40], [45] (Figure 2A).”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [45]
Citations
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Enzyme–MOF (metal–organic framework) composites
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ER stress: Autophagy induction, inhibition and selection
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Metadata
- Authors
- Wickner, W., & Schekman, R.
- Affiliations
- Dartmouth College (US)
- Corresponding author
- Wickner, William
- Schekman, Randy
- Venue
- Science
- Published
- 2005-12-02
- Volume
- 310
- Issue
- 5753
- Pages
- 1452-1456
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2021288400
- Cited by
- 458
- References
- 96
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 10 · 2023: 13 · 2022: 20 · 2021: 20 · 2020: 25 · 2019: 13 · 2018: 13 · 2017: 16 · 2016: 18 · 2015: 18 · 2014: 35 · 2013: 19 · 2012: 28
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- protein translocation, biological membranes, organelle targeting, mitochondrial protein import, chloroplast protein import, substrate specificity, membrane lipid environment, energy coupling, subcellular compartmentalization
- MeSH terms
- Carrier Proteins, Endoplasmic Reticulum, Intracellular Membranes, Mitochondria, Protein Biosynthesis, Protein Folding, Peroxisomes, Protein Transport
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