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 (658 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
The cap-like structure covering the anterior portion of sperm head. Acrosome, derived from lysosomes, is a membrane-bound organelle that contains the required hydrolytic and proteolytic enzymes necessary for sperm penetration of the egg in fertilization.
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: Acrosomes.
Where it fits in the MeSH classification
- Broader topics
- Sperm Head; Lysosomes
- See also
- Acrosome Reaction
Related concepts
- Sperm Head
- Lysosomes
- Fertilization
Research landscape
PubMed indexes 4,531 records tagged with the MeSH heading “Acrosome” (counts retrieved 2026-10-31). 406 of them (9.0%) were published from 2020 onward, and the busiest period so far is through 1999 with 2,373 records.
Reviews account for 249 records (5.5%) and meta-analyses for 1. Randomized controlled trials number 11 (0.2%) 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 | 2,373 |
| 2000-2009 | 860 |
| 2010-2019 | 892 |
| 2020 onward | 406 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 249 | 5.5% |
| Meta-analyses | 1 | 0.0% |
| Randomized controlled trials | 11 | 0.2% |
Method: PubMed query "Acrosome"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in anatomy and physiology
Anatomy describes how body structures are built and physiology describes how they normally work, so most findings here are descriptive or mechanistic rather than evidence about treatment. Much of what is known comes from dissection, imaging, tissue studies and experiments in animals, and measurements in healthy volunteers can differ from those in people with disease or at different ages. Normal ranges vary between individuals and populations. Check whether a result was measured in people or in another species, the age and health of the participants, and the method used.
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 |
|---|---|---|---|---|
| Globozoospermia and lack of acrosome formation in GM130-deficient mice | 2017 | Research article Design not recorded in structured metadata | 72 | cc by PMID 28055014 · DOI · PMC5386352 |
| FAM71F1 binds to RAB2A and RAB2B and is essential for acrosome formation and male fertility in mice | 2021 | Research article Design not recorded in structured metadata | 33 | cc by PMID 34714330 · DOI · PMC8602946 |
| FAM209 associates with DPY19L2, and is required for sperm acrosome biogenesis and fertility in mice | 2021 | Research article Design not recorded in structured metadata | 28 | cc by PMID 34471926 · DOI · PMC8627553 |
| The intrinsically disordered protein SPE-56 is required for acrosomal-like exocytosis and fertility in Caenorhabditis elegans | 2026 | Research article Design not recorded in structured metadata | 0 | cc by PMID 41965464 · DOI · PMC13070043 |
Globozoospermia and lack of acrosome formation in GM130-deficient mice [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Globozoospermia is a common reproductive disorder that causes male infertility in humans, and the malformation or loss of acrosomes is the prominent feature of this disease.
- Closing excerpt
- Thus, the GM130-deficient mouse provides a valuable model for investigating the etiology of human globozoospermia.
- 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 (177 words)
Globozoospermia is a common reproductive disorder that causes male infertility in humans, and the malformation or loss of acrosomes is the prominent feature of this disease. Although the acrosome is thought to be derived from the Golgi apparatus, the detailed molecular mechanisms remain unclear. GM130 is a cis-side localized Golgi matrix protein,whereas the physiological functions of this protein remain elusive. Here we showed that inactivation of GM130-caused male infertility in mouse model. The primary defects were the absence of acrosomes, round sperm heads, and aberrant assembly of the mitochondrial sheath, which comprise the characteristic features of human globozoospermia. Further investigation indicated that loss of GM130 did not affect the secretion of pro-acrosomic vesicles, whereas the vesicles failed to fuse into a single large acrosome vesicle. Co-localization of the adaptor protein complex AP1 and trans-Golgi network (TGN) protein TGN46 was disrupted, suggesting that the malformation of acrosomes is most likely due to the defect in the sorting and coating of Golgi-derived pro-acrosomic vesicles. Thus, the GM130-deficient mouse provides a valuable model for investigating the etiology of human globozoospermia.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 28055014 · DOI · PMC5386352
FAM71F1 binds to RAB2A and RAB2B and is essential for acrosome formation and male fertility in mice [2]
Abstract reading summary — source excerpts
- Opening excerpt
- The acrosome is a cap-shaped, Golgi-derived membranous organelle that is located over the anterior of the sperm nucleus and highly conserved throughout evolution.
- Closing excerpt
- These results indicate that a complex of FAM71F1 and active RAB2A/B suppresses excessive vesicle trafficking during acrosome formation.
- 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 (164 words)
The acrosome is a cap-shaped, Golgi-derived membranous organelle that is located over the anterior of the sperm nucleus and highly conserved throughout evolution. Although morphological changes during acrosome biogenesis in spermatogenesis have been well described, the molecular mechanism underlying this process is still largely unknown. Family with sequence similarity 71, member F1 and F2 (FAM71F1 and FAM71F2) are testis-enriched proteins that contain a RAB2B-binding domain, a small GTPase involved in vesicle transport and membrane trafficking. Here, by generating mutant mice for each gene, we found that Fam71f1 is essential for male fertility. In Fam71f1-mutant mice, the acrosome was abnormally expanded at the round spermatid stage, likely because of enhanced vesicle trafficking. Mass spectrometry analysis after immunoprecipitation indicated that, in testes, FAM71F1 binds not only RAB2B, but also RAB2A. Further study suggested that FAM71F1 binds to the GTP-bound active form of RAB2A/B, but not the inactive form. These results indicate that a complex of FAM71F1 and active RAB2A/B suppresses excessive vesicle trafficking during acrosome formation.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34714330 · DOI · PMC8602946
FAM209 associates with DPY19L2, and is required for sperm acrosome biogenesis and fertility in mice [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Infertility afflicts up to 15% of couples globally each year with men a contributing factor in 50% of these cases.
- Closing excerpt
- Here, we identified FAM209 as the first interacting partner of DPY19L2, and the second protein that is essential for acrosome biogenesis that localizes to the inner nuclear membrane.
- 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 (175 words)
Infertility afflicts up to 15% of couples globally each year with men a contributing factor in 50% of these cases. Globozoospermia is a rare condition found in infertile men, which is characterized by defective acrosome biogenesis leading to the production of round-headed sperm. Here, we report that family with sequence similarity 209 (Fam209) is required for acrosome biogenesis in mouse sperm. FAM209 is a small transmembrane protein conserved among mammals. Loss of Fam209 results in fertility defects that are secondary to abnormalities in acrosome biogenesis during spermiogenesis, reminiscent of globozoospermia. Analysis of the FAM209 proteome identified DPY19L2, whose human orthologue is involved in the majority of globozoospermia cases. Although mutations in human and mouse Dpy19l2 have been shown to cause globozoospermia, no in vivo interacting partners of DPY19L2 have been identified until now. FAM209 colocalizes with DPY19L2 at the inner nuclear membrane to maintain the developing acrosome. Here, we identified FAM209 as the first interacting partner of DPY19L2, and the second protein that is essential for acrosome biogenesis that localizes to the inner nuclear membrane.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34471926 · DOI · PMC8627553
The intrinsically disordered protein SPE-56 is required for acrosomal-like exocytosis and fertility in Caenorhabditis elegans [4]
Abstract reading summary — source excerpts
- Opening excerpt
- In sexually reproducing organisms, activation of fertilization-competent sperm requires acrosomal vesicle exocytosis.
- Closing excerpt
- Overall, IDR-mediated structural flexibility may represent a conserved mechanism for maintaining sperm function across variable temperatures.
- 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 (142 words)
In sexually reproducing organisms, activation of fertilization-competent sperm requires acrosomal vesicle exocytosis. We characterized the C. elegans gene spe-56, which encodes a single-pass transmembrane protein containing a C-terminal intrinsically disordered region (IDR). SPE-56 localizes to acrosomal-like membranous organelles (MOs) in the sperm, and loss of spe-56 causes sterility due to defective MO-plasma membrane fusion during sperm activation. Genetic epistasis places SPE-56 downstream of the canonical SPE-8/SPE-6 sperm activation pathway, which comprises a membrane receptor and a kinase. Strains with partial deletions of the IDR are fertile at low temperatures but sterile at elevated temperatures. Larger deletions of the IDR are infertile at low and high temperatures. These data indicate that SPE-56 promotes acrosomal-like exocytosis and that its IDR contributes to the thermal robustness of sperm activation. Overall, IDR-mediated structural flexibility may represent a conserved mechanism for maintaining sperm function across variable temperatures.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41965464 · DOI · PMC13070043
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 The acrosome-acroplaxome-manchette complex and the shaping of the spermatid head [5]
- Research article Mammalian sperm acrosome: formation, contents, and function [6]
- Research article Early events in mammalian fertilization [7]
- Research article Molecular events mediating sperm activation [8]
- Research article Methods for evaluating the acrosomal status of mammalian sperm [9]
- Research article The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization [10]
References
- Han F, Liu C, Zhang L, Chen M, Zhou Y, Qin Y, et al.. Globozoospermia and lack of acrosome formation in GM130-deficient mice. . 2017. PMID 28055014 · DOI · PMC5386352
- Morohoshi A, Miyata H, Oyama Y, Oura S, Noda T, Ikawa M. FAM71F1 binds to RAB2A and RAB2B and is essential for acrosome formation and male fertility in mice. . 2021. PMID 34714330 · DOI · PMC8602946
- Castaneda JM, Shimada K, Satouh Y, Yu Z, Devlin DJ, Ikawa M, et al.. FAM209 associates with DPY19L2, and is required for sperm acrosome biogenesis and fertility in mice. . 2021. PMID 34471926 · DOI · PMC8627553
- Gottschling DC, Eiser S, Döring F. The intrinsically disordered protein SPE-56 is required for acrosomal-like exocytosis and fertility in Caenorhabditis elegans. . 2026. PMID 41965464 · DOI · PMC13070043
- Kierszenbaum AL, Tres LL. The acrosome-acroplaxome-manchette complex and the shaping of the spermatid head. Arch Histol Cytol. 2004. PMID 15700535 · DOI
- Abou-Haila A, Tulsiani DR. Mammalian sperm acrosome: formation, contents, and function. Arch Biochem Biophys. 2000. PMID 10898932 · DOI
- Wassarman PM. Early events in mammalian fertilization. Annu Rev Cell Biol. 1987. PMID 3318876 · DOI
- Ward CR, Kopf GS. Molecular events mediating sperm activation. Dev Biol. 1993. PMID 8392473 · DOI
- Cross NL, Meizel S. Methods for evaluating the acrosomal status of mammalian sperm. Biol Reprod. 1989. PMID 2695176 · DOI
- Tulsiani DR, Abou-Haila A, Loeser CR, Pereira BM. The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp Cell Res. 1998. PMID 9596988 · 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 2026-10-31.
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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.