Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (631 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
A series of sequential intracellular steps involved in the transport of proteins (such as hormones and enzymes) from the site of synthesis to outside the cell. The pathway involves membrane-bound compartments through which the newly synthesized proteins undergo post-translational modifications, packaging, storage, or transportation to the plasma membrane for secretion.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Secretory Pathways; Secretory Process; Secretory Processes; Secretion Pathway; Secretion Pathways; Secretion Process; Secretion Processes.
Where it fits in the MeSH classification
- Broader topics
- Biological Transport; Exocytosis
Related concepts
- Post-Translational Modifications
- Plasma Membrane
Research landscape
PubMed indexes 1,711 records tagged with the MeSH heading “Secretory Pathway” (counts retrieved 2026-10-29). 463 of them (27.1%) were published from 2020 onward, and the busiest period so far is 2010-2019 with 1,079 records.
Reviews account for 366 records (21.4%) and meta-analyses for 0. Randomized controlled trials number 7 (0.4%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 0 |
| 2000-2009 | 175 |
| 2010-2019 | 1,079 |
| 2020 onward | 463 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 366 | 21.4% |
| Meta-analyses | 0 | 0.0% |
| Randomized controlled trials | 7 | 0.4% |
Method: PubMed query "Secretory Pathway"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-29.
Reading the evidence in molecular biology
Molecular biology establishes mechanisms through controlled experiments, often in simplified systems such as purified proteins, cultured cells or model organisms. Such work can show what is possible in a defined system, but whether a pathway matters in a whole organism or in human disease needs further evidence. Check the experimental system, whether findings were reproduced by independent groups, and whether the authors tested the mechanism directly or inferred it from correlation.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Understanding the mechanism of IL-1β secretion | 2011 | Review article Design not recorded in structured metadata | 1,215 | cc by PMID 22019906 · DOI · PMC3714593 |
| A proteomic atlas of senescence-associated secretomes for aging biomarker development | 2020 | Research article Design not recorded in structured metadata | 1,213 | cc0 PMID 31945054 · DOI · PMC6964821 |
| Molecular Mechanisms Responsible for Therapeutic Potential of Mesenchymal Stem Cell-Derived Secretome | 2019 | Review article Design not recorded in structured metadata | 378 | cc by PMID 31100966 · DOI · PMC6562906 |
| Structural basis of regulated N-glycosylation at the secretory translocon | 2026 | Research article Design not recorded in structured metadata | 3 | cc by PMID 41261126 · DOI · PMC12804085 |
Understanding the mechanism of IL-1β secretion [1]
Abstract reading summary — source excerpts
- Opening excerpt
- The cytokine interleukin-1β (IL-1β) is a key mediator of the inflammatory response.
- Closing excerpt
- Here we summarise these observations and propose that secretion of IL-1β occurs on a continuum, dependent upon stimulus strength and the extracellular IL-1β requirement.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (119 words)
The cytokine interleukin-1β (IL-1β) is a key mediator of the inflammatory response. Essential for the host-response and resistance to pathogens, it also exacerbates damage during chronic disease and acute tissue injury. It is not surprising therefore that there is a huge level of interest in how this protein is produced and exported from cells. However, the mechanism of IL-1β release has proven to be elusive. It does not follow the conventional ER-Golgi route of secretion. A literature full of disparate observations arising from numerous experimental systems, has contributed to a complicated mix of diverse proposals. Here we summarise these observations and propose that secretion of IL-1β occurs on a continuum, dependent upon stimulus strength and the extracellular IL-1β requirement.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 22019906 · DOI · PMC3714593
A proteomic atlas of senescence-associated secretomes for aging biomarker development [2]
Abstract reading summary — source excerpts
- Opening excerpt
- The senescence-associated secretory phenotype (SASP) has recently emerged as a driver of and promising therapeutic target for multiple age-related conditions, ranging from neurodegeneration to cancer.
- Closing excerpt
- Our findings will facilitate the identification of proteins characteristic of senescence-associated phenotypes and catalog potential senescence biomarkers to assess the burden, originating stimulus, and tissue of origin of senescent cells in vivo.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (183 words)
The senescence-associated secretory phenotype (SASP) has recently emerged as a driver of and promising therapeutic target for multiple age-related conditions, ranging from neurodegeneration to cancer. The complexity of the SASP, typically assessed by a few dozen secreted proteins, has been greatly underestimated, and a small set of factors cannot explain the diverse phenotypes it produces in vivo. Here, we present the "SASP Atlas," a comprehensive proteomic database of soluble proteins and exosomal cargo SASP factors originating from multiple senescence inducers and cell types. Each profile consists of hundreds of largely distinct proteins but also includes a subset of proteins elevated in all SASPs. Our analyses identify several candidate biomarkers of cellular senescence that overlap with aging markers in human plasma, including Growth/differentiation factor 15 (GDF15), stanniocalcin 1 (STC1), and serine protease inhibitors (SERPINs), which significantly correlated with age in plasma from a human cohort, the Baltimore Longitudinal Study of Aging (BLSA). Our findings will facilitate the identification of proteins characteristic of senescence-associated phenotypes and catalog potential senescence biomarkers to assess the burden, originating stimulus, and tissue of origin of senescent cells in vivo.
Abstract reproduced from the open-access article under the recorded cc0 licence; © the authors. PMID 31945054 · DOI · PMC6964821
Molecular Mechanisms Responsible for Therapeutic Potential of Mesenchymal Stem Cell-Derived Secretome [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Mesenchymal stem cell (MSC)-sourced secretome, defined as the set of MSC-derived bioactive factors (soluble proteins, nucleic acids, lipids and extracellular vesicles), showed therapeutic effects similar to those observed after transplantation of MSCs.
- Closing excerpt
- Therapeutic effects of MSC-sourced secretomes relied on their capacity to deliver genetic material, growth and immunomodulatory factors to the target cells enabling activation of anti-apoptotic and pro-survival pathways that resulted in tissue repair and regeneration.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (199 words)
Mesenchymal stem cell (MSC)-sourced secretome, defined as the set of MSC-derived bioactive factors (soluble proteins, nucleic acids, lipids and extracellular vesicles), showed therapeutic effects similar to those observed after transplantation of MSCs. MSC-derived secretome may bypass many side effects of MSC-based therapy, including unwanted differentiation of engrafted MSCs. In contrast to MSCs which had to be expanded in culture to reach optimal cell number for transplantation, MSC-sourced secretome is immediately available for treatment of acute conditions, including fulminant hepatitis, cerebral ischemia and myocardial infarction. Additionally, MSC-derived secretome could be massively produced from commercially available cell lines avoiding invasive cell collection procedure. In this review article we emphasized molecular and cellular mechanisms that were responsible for beneficial effects of MSC-derived secretomes in the treatment of degenerative and inflammatory diseases of hepatobiliary, respiratory, musculoskeletal, gastrointestinal, cardiovascular and nervous system. Results obtained in a large number of studies suggested that administration of MSC-derived secretomes represents a new, cell-free therapeutic approach for attenuation of inflammatory and degenerative diseases. Therapeutic effects of MSC-sourced secretomes relied on their capacity to deliver genetic material, growth and immunomodulatory factors to the target cells enabling activation of anti-apoptotic and pro-survival pathways that resulted in tissue repair and regeneration.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 31100966 · DOI · PMC6562906
Structural basis of regulated N-glycosylation at the secretory translocon [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Most human secretory pathway proteins are N-glycosylated by oligosaccharyltransferase (OST) complexes as they enter the endoplasmic reticulum (ER)1-3.
- Closing excerpt
- Our results define a mechanism of regulated N-glycosylation and illustrate how the nascent chain remodels the translocon to facilitate its own biogenesis.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (130 words)
Most human secretory pathway proteins are N-glycosylated by oligosaccharyltransferase (OST) complexes as they enter the endoplasmic reticulum (ER)1-3. Recent work revealed a substrate-assisted mechanism by which N-glycosylation of the chaperone glucose-regulated protein 94 (GRP94) is regulated to control cell surface receptor signalling4. Here we report the structure of a natively isolated GRP94 folding intermediate tethered to a specialized CCDC134-bound translocon. Together with functional analysis, the data reveal how a conserved N-terminal extension in GRP94 inhibits OST-A and how structural rearrangements within the translocon shield the tethered nascent chain from inappropriate OST-B glycosylation. These interactions depend on a hydrophobic CCDC134 groove, which recognizes a non-native conformation of nascent GRP94. Our results define a mechanism of regulated N-glycosylation and illustrate how the nascent chain remodels the translocon to facilitate its own biogenesis.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41261126 · DOI · PMC12804085
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Mechanisms of regulated unconventional protein secretion [5]
- Research article Biological diversity of prokaryotic type IV secretion systems [6]
- Research article Pathways of Unconventional Protein Secretion [7]
- Research article Protein quality control in the secretory pathway [8]
- Research article Astrocytes as secretory cells of the central nervous system: idiosyncrasies of vesicular secretion [9]
- Research article COPII and the regulation of protein sorting in mammals [10]
References
- Lopez-Castejon G, Brough D. Understanding the mechanism of IL-1β secretion. . 2011. PMID 22019906 · DOI · PMC3714593
- Basisty N, Kale A, Jeon OH, Kuehnemann C, Payne T, Rao C, et al.. A proteomic atlas of senescence-associated secretomes for aging biomarker development. . 2020. PMID 31945054 · DOI · PMC6964821
- Harrell CR, Fellabaum C, Jovicic N, Djonov V, Arsenijevic N, Volarevic V. Molecular Mechanisms Responsible for Therapeutic Potential of Mesenchymal Stem Cell-Derived Secretome. . 2019. PMID 31100966 · DOI · PMC6562906
- Yamsek M, Ma M, Jha R, Wan Y, Li Q, Zhong F, et al.. Structural basis of regulated N-glycosylation at the secretory translocon. . 2026. PMID 41261126 · DOI · PMC12804085
- Nickel W, Rabouille C. Mechanisms of regulated unconventional protein secretion. Nat Rev Mol Cell Biol. 2009. PMID 19122676 · DOI
- Alvarez-Martinez CE, Christie PJ. Biological diversity of prokaryotic type IV secretion systems. Microbiol Mol Biol Rev. 2009. PMID 19946141 · DOI · PMC2786583
- Rabouille C. Pathways of Unconventional Protein Secretion. Trends Cell Biol. 2017. PMID 27989656 · DOI
- Sun Z, Brodsky JL. Protein quality control in the secretory pathway. J Cell Biol. 2019. PMID 31537714 · DOI · PMC6781448
- Verkhratsky A, Matteoli M, Parpura V, Mothet JP, Zorec R. Astrocytes as secretory cells of the central nervous system: idiosyncrasies of vesicular secretion. EMBO J. 2016. PMID 26758544 · DOI · PMC4741299
- Zanetti G, Pahuja KB, Studer S, Shim S, Schekman R. COPII and the regulation of protein sorting in mammals. Nat Cell Biol. 2011. PMID 22193160 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-29.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.