A comprehensive review of signal peptides: Structure, roles, and applications
Abstract
Signal peptides (SP) are short peptides located in the N-terminal of proteins, carrying information for protein secretion. They are ubiquitous to all prokaryotes and eukaryotes. SPs have been of special interest in several scientific and industrial fields, including recombinant protein production, disease diagnosis, immunization, and laboratory techniques. Recently, the role of SPs in recombinant protein production has gained too much attention. Herein, several studies have been reviewed to elucidate the precise structure and function of SPs, particularly the optimized ones for recombinant protein production. However, some features of SPs still have remained obscure. In this review, some approaches concerning elucidation and optimization of SPs are discussed, and pragmatic conclusions and suggestions for future studies are also proposed. Moreover, a summary of secretory pathways, evolutionary changes, functions, applications, and different types of SPs is mentioned. At last, current limitations and prospects are discussed.
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The choice of signal peptide sequence and co-expression with chaperones can affect secretion and folding.
“Additionally, the choice of the signal peptide sequence [146,147,148,149] and the co-expression with chaperons can affect the secretion and folding (see Figure 1).”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [149]
Cites
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Chimeric antigen receptor natural killer (CAR-NK) cell design and engineering for cancer therapy
Gong, Y., Klein Wolterink, R. G. J., Wang, J., Bos, G. M. J., & Germeraad, W. T. V. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01083-5 · Cited by 379 · see citing works
Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
Understanding the mammalian TRAP complex function(s)
Russo, A. (2020) · Open Biology · doi:10.1098/rsob.190244 · Cited by 28 · see citing works
Identifying carbohydrate-active enzymes of Cutaneotrichosporon oleaginosus using systems biology
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- Authors
- Owji, H., Nezafat, N., Negahdaripour, M., Hajiebrahimi, A., & Ghasemi, Y.
- Affiliations
- Shiraz University of Medical Sciences (IR)
- Corresponding author
- Ghasemi, Younes
- Venue
- European Journal of Cell Biology
- Publisher
- Elsevier BV
- Published
- 2018-08
- Volume
- 97
- Issue
- 6
- Pages
- 422-441
- ISSN
- 0171-9335 (ISSN-L)
- OpenAlex
- W2809247618
- Cited by
- 523
- References
- 2
- Citations by year
- 2026: 58 · 2025: 114 · 2024: 108 · 2023: 67 · 2022: 75 · 2021: 60 · 2020: 27 · 2019: 11 · 2018: 3
- FWCI
- 3.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Shiraz University of Medical Sciences
- Shiraz Transplant Research Center, Shiraz University of Medical Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- signal peptide, protein secretion, secretory pathway, recombinant protein expression, disease diagnosis, immunization
- MeSH terms
- Animals, Humans, Protein Conformation, Protein Sorting Signals
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