The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Unconventional Secretory Routes: Direct Protein Export Across the Plasma Membrane of Mammalian Cells
Abstract
The vast majority of extracellular proteins are exported from mammalian cells by the endoplasmic reticulum/Golgi‐dependent secretory pathway. For poorly understood reasons, however, a heterogenous group of extracellular proteins has been discovered that does not make use of signal peptide‐dependent secretory transport. Both the release mechanisms and the molecular identity of the secretory machines involved have remained elusive. Recent studies now have established a subgroup of unconventional secretory proteins capable of translocating from the cytoplasm directly across the plasma membrane to get access to the exterior of eukaryotic cells. This review aims to focus on a detailed comparison of the subcellular site of membrane translocation of various unconventional secretory proteins such as the proangiogenic molecule fibroblast growth factor‐2 (FGF‐2) and Leishmania hydrophilic acylated surface protein B (HASP B). A potential link between membrane translocation and quality control as an integral part of unconventional secretory processes is discussed.
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Cites
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Active Caspase-1 Is a Regulator of Unconventional Protein Secretion
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Metadata
- Authors
- Nickel, W.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2005-05-20
- Volume
- 6
- Issue
- 8
- Pages
- 607-614
- ISSN
- 1398-9219 (ISSN-L)
- 1600-0854
- OpenAlex
- W2165623503
- Cited by
- 331
- References
- 55
- FWCI
- 10.76
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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