The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Identity verification passed. The target is the D. melanogaster gene Mst27D, also known as CG31907, encoding Male-specific transcript 27D. The exact gene studied by Li, Messina and Lehner in 2023 is a testis-specialized, EB1-related protein with an N-terminal calponin-homology (CH) region. This agrees with the supplied UniProt Q8IPI4 annotations—InterPro CH domain IPR001715/IPR036872, MAPRE-related IPR027328, and Pfam CH PF00307. No literature concerning a similarly named gene in another organism was used. Sequence similarity to EB1 is concentrated mainly in the CH region, so the MAPRE annotation denotes evolutionary/structural relatedness rather than canonical EB1 activity. (li2023nuclearelongationduring pages 16-18, li2023nuclearelongationduring pages 2-4)
The best-supported primary function is not enzymatic, transport, or conventional signaling activity. Mst27D is a structural cytoskeletal adaptor that links Nup358-containing nuclear pore complexes (NPCs) in the spermatid nuclear envelope to bundled microtubules of the dense complex. Its N-terminal region supports microtubule binding, whereas its C-terminal region mediates self-association and association with Nup358. This linkage organizes a stiff longitudinal microtubule bundle that directs the normally straight transformation of round spermatid nuclei into elongated, needle-shaped sperm nuclei. (li2023nuclearelongationduring pages 1-2, li2023nuclearelongationduring pages 22-24, li2023nuclearelongationduring pages 8-10, li2023nuclearelongationduring pages 10-12)
| Annotation question | Best-supported conclusion | Key direct evidence | Evidence level | Important caveat |
|---|---|---|---|---|
| Identity and domains | Target is Drosophila melanogaster Mst27D/CG31907, UniProt Q8IPI4. It is an EB1-related protein with an N-terminal calponin-homology microtubule-binding region and a distinct C-terminal region, consistent with the supplied CH/MAPRE annotations. | The exact Mst27D gene was analyzed genetically and molecularly; similarity to canonical EB1 proteins is concentrated in the CH domain. (li2023nuclearelongationduring pages 16-18, li2023nuclearelongationduring pages 2-4) | High | MAPRE/CH annotations indicate structural relationship, not canonical EB1 activity or functional interchangeability. |
| Primary molecular function | Mst27D is a non-enzymatic structural adaptor linking nuclear pore complexes to dense-complex microtubules; it likely also cross-links microtubules to support straight spermatid-nuclear elongation. | The N-terminal region mediates microtubule association, while the C-terminal region self-associates and recruits Nup358. Full-length Mst27D decorates microtubule lattices, and high expression induces microtubule cables. (li2023nuclearelongationduring pages 1-2, li2023nuclearelongationduring pages 8-10, li2023nuclearelongationduring pages 24-25) | High for NPC–microtubule linkage; moderate for MT–MT bundling | Bundling is supported mainly by cellular, genetic, co-immunoprecipitation, and imaging evidence rather than purified-protein biochemistry. |
| Relationship to EB1 | Mst27D differs functionally from canonical EB1 because it distributes along microtubules instead of forming moving plus-end comets. | Full-length Mst27D and a CH–EB1-C-terminal chimera associated along microtubules; Mst27D did not show canonical EB1-like comet behavior. (li2023nuclearelongationduring pages 8-10, li2023nuclearelongationduring pages 19-21) | Moderate–high | EB1-related sequence and CH-domain annotations alone do not justify assigning plus-end-tracking activity. |
| Nup358 interaction | Mst27D binds the cytoplasmic NPC component Nup358 through its C-terminal region, and Nup358 is required for Mst27D enrichment at the nuclear envelope. | Nup358 was the most specific protein recovered by Mst27D-EGFP affinity purification and mass spectrometry. Full-length Mst27D recruited Nup358 to induced cables, whereas a construct lacking the Mst27D C terminus did not; Nup358 depletion abolished nuclear-envelope enrichment of Mst27D. (li2023nuclearelongationduring pages 4-6, li2023nuclearelongationduring pages 12-13, li2023nuclearelongationduring pages 10-12) | High | RanGAP also co-purified, probably through its established association with Nup358; this does not establish a separate direct Mst27D–RanGAP interaction. |
| Localization during spermiogenesis | After meiosis, Mst27D becomes asymmetrically enriched with Nup358 at the NPC-bearing nuclear envelope and adjacent dense-complex microtubules. A hemispherical cap becomes a longitudinal stripe along the nuclear groove, followed by removal during NPC/NE shedding. | Endogenously driven fluorescent fusions co-localized with Nup358 throughout nuclear elongation. Shedding occurred after protamine accumulation over approximately one hour; Mst27D initially accompanied the shed vesicle and then disappeared. (li2023nuclearelongationduring pages 12-13) | High | Mst27D-mCherry also showed meiotic spindle enrichment, but the demonstrated fertility mechanism concerns its post-meiotic NPC–microtubule localization. |
| Biological process and pathway | Mst27D acts in late spermiogenesis during a second symmetry-breaking event that converts a hemispherical NPC distribution into a linear arrangement and organizes a longitudinal microtubule bundle defining the nuclear-elongation axis. | Early nuclear-envelope and cyst polarization occurred without Mst27D. Defects appeared during later NPC redistribution, dense-complex bundling, and nuclear elongation; progressive bundling normally lasts roughly 10–12 hours. (li2023nuclearelongationduring pages 24-25, li2023nuclearelongationduring pages 22-24) | High | This is a cytoskeletal and nuclear-envelope remodeling mechanism, not a conventional signaling or metabolic pathway. |
| Loss-of-function nuclear phenotype | Mst27D loss severely disrupts canoe- and needle-shaped nuclear elongation, producing bent axes, variable diameters, patchy NPC distribution, and failure to form a prominent adjacent microtubule bundle. | Irregular non-canoe nuclei occurred in 98% of mutant versus 1.4% of control Tpl94D-positive cysts, based on 197 versus 191 cysts, and in 95% versus 1.4% of ProtB-positive cysts, based on 159 versus 141 cysts. Two independent loss-of-function alleles were studied. (li2023nuclearelongationduring pages 16-18, li2023nuclearelongationduring pages 18-19, li2023nuclearelongationduring pages 21-22) | High | Mutant nuclei retain some elongation; Mst27D is required for normal geometry and efficiency rather than every residual extension event. |
| Male fertility | Mst27D is required for normal male fertility but not viability or female fertility. | Hemizygous mutant males produced approximately 20% as many progeny as controls. Homozygotes reached adulthood without obvious abnormalities; Mst27Dcc homozygotes constituted 34% of eclosing progeny, and female fertility was unaffected. (li2023nuclearelongationduring pages 16-18) | High | Mst27D lies within an intron of Mnn1, but rescue by an Mst27D genomic transgene supports attribution of the fertility phenotype to Mst27D loss. |
| Genetic rescue and domain sufficiency | Both the CH-containing N terminus and C-terminal region must be present in the same full-length protein for normal biological function. | Full-length genomic Mst27D-EGFP or Mst27D-mCherry rescued fertility and nuclear elongation, whereas isolated CH or C-terminal fragments failed to rescue and localized abnormally. (li2023nuclearelongationduring pages 16-18, li2023nuclearelongationduring pages 18-19) | High | Fragment failure establishes non-sufficiency but does not exclude additional regulatory motifs or post-translational controls. |
| Histone-to-protamine transition | Mst27D controls nuclear mechanics largely independently of the gross timing and progression of histone replacement and protamine incorporation. | Tpl94D-positive cysts numbered 19.1 ± 3.6 in mutants versus 19.7 ± 3.2 in controls; ProtB-positive cysts numbered 23.5 ± 4.6 versus 26.5 ± 4.8, with preserved spatial order despite major shape defects. (li2023nuclearelongationduring pages 18-19) | High for gross marker progression | Marker counts do not exclude subtle defects in chromatin composition, compaction, or biochemistry. |
| Actin cones and individualization | Mst27D loss does not prevent actin-cone assembly, although abnormal nuclear geometry and NPC/NE shedding are associated with partial downstream individualization defects. | Investment cones formed in Mst27D mutants, while substantial Nup58-EGFP remained on the nuclear envelope and individualization was abnormal. (kawadkar2025nup43positivelyregulates pages 16-20, li2023nuclearelongationduring pages 21-22) | Moderate–high | Actin-cone failure in Nup43 mutants is a Nup43 phenotype, not an Mst27D phenotype; Mst27D-mCherry served only as a marker in that experiment. (kawadkar2025nup43positivelyregulates pages 11-16) |
| Evolution | Mst27D is proposed to be a rapidly diverged, testis-specialized derivative generated by retroposition from the testis-expressed EB1-family gene CG15306. | Sequence and genomic analysis supported retroposition and retention of an EB1-related CH region. (li2023nuclearelongationduring pages 24-25) | Moderate | Evolutionary origin does not imply preservation of canonical EB1 localization, partners, or plus-end tracking. |
| Research application and recent evidence | Mst27D is useful as a Drosophila model and fluorescent marker for spermatid nuclear shaping, NPC–cytoskeleton coupling, dense-complex organization, and male-fertility mechanisms. | The 2023 study established the mechanism. A 2025 Nup43 preprint used Mst27D-mCherry to test whether Nup43 loss altered its localization and found comparable asymmetric localization without directly perturbing Mst27D. (li2023nuclearelongationduring pages 1-2, kawadkar2025nup43positivelyregulates pages 11-16) | High for basic-research utility; low for translation | No substantive Mst27D-specific 2024 study or clinical or industrial implementation was identified; evidence remains dominated by the detailed 2023 primary study. |
Table: This table separates experimentally established Mst27D functions from mechanistic inference and contextual reuse. It summarizes identity, molecular role, localization, quantitative phenotypes, fertility, evolution, and research utility.
Affinity purification of Mst27D-EGFP from testes followed by mass spectrometry identified Nup358 as its most efficiently and specifically co-purified protein; RanGAP, an established Nup358-associated protein, was also recovered. This provided unbiased interaction evidence connecting Mst27D to the cytoplasmic face of nuclear pores. (li2023nuclearelongationduring pages 4-6)
Interaction and localization experiments support a modular mechanism:
Co-immunoprecipitation showed that Mst27D-mCherry recovered full-length Mst27D-EGFP and its C-terminal region, but not the isolated CH region or canonical EB1. Together with cable formation after elevated expression in S2R+ cells, this supports C-terminally mediated dimerization or oligomerization and a plausible secondary role as a microtubule–microtubule cross-linker/bundler. That bundling interpretation is compelling but somewhat less direct than the NPC–microtubule-linker assignment because it has not been fully reconstructed with purified proteins. (li2023nuclearelongationduring pages 8-10, li2023nuclearelongationduring pages 24-25)
Canonical EB1 proteins form moving “comets” at growing microtubule plus ends. Mst27D instead distributes along microtubules, and elevated expression generates microtubule cables. Thus, assigning “microtubule plus-end tracking” solely from its CH/MAPRE annotations would be inappropriate. Mst27D appears to have evolved a specialized lattice-binding, bundling, and nuclear-pore-coupling function in spermatids. (li2023nuclearelongationduring pages 8-10, li2023nuclearelongationduring pages 19-21)
Mst27D localization is strongly stage-dependent. It is enriched on meiotic spindles during meiosis, but its demonstrated fertility function occurs after meiosis. In early round spermatids, Mst27D and Nup358 become asymmetrically enriched in the same polarized nuclear-envelope territory. At the onset of elongation they occupy a hemispherical NPC-bearing nuclear-envelope cap and adjacent perinuclear dense-complex microtubules. During elongation, this cap is remodeled into a longitudinal stripe in a groove along the extending nucleus. (li2023nuclearelongationduring pages 22-24, li2023nuclearelongationduring pages 12-13)
Mst27D therefore carries out its principal function on the cytoplasmic side of the spermatid nuclear envelope, at the interface between Nup358-bearing NPCs and dense-complex microtubules. The proposed geometry places the relevant Nup358 region roughly 60 nm from the nuclear envelope, where Mst27D can bridge the NPC cytoplasmic filaments and nearby microtubules. (li2023nuclearelongationduring pages 24-25, li2023nuclearelongationduring pages 19-21)
After elongation and the onset of protamine accumulation, the NPC-bearing nuclear-envelope region is shed. This removal is completed in approximately one hour. Mst27D initially remains associated with the shed vesicle but disappears rapidly afterward rather than remaining with material transported to the sperm-tail waste bag. (li2023nuclearelongationduring pages 12-13)
Mst27D acts in the late spermiogenesis nuclear-shaping pathway, specifically during a second symmetry-breaking event:
The dense-complex bundle is interpreted as a stiff guiding rod. Without Mst27D, a normal bundle fails to form adjacent to the nucleus, the axoneme can pass beside rather than remain properly aligned with the nucleus, and residual nuclear extension follows bent or irregular trajectories. Mst27D thus couples cytoskeletal organization to nuclear-envelope remodeling rather than transmitting a conventional soluble signaling cascade. (li2023nuclearelongationduring pages 1-2, li2023nuclearelongationduring pages 21-22)
Mst27D and the SUN-domain protein Spag4 have separable roles. Mst27D links NPC-bearing nuclear envelope to dense-complex microtubules during shaping, whereas Spag4 maintains the later nucleus–basal-body/axoneme connection. Mutation of either protein did not abolish the characteristic localization of the other, arguing against their being components of a single obligate complex. (li2023nuclearelongationduring pages 21-22)
Li et al. analyzed two loss-of-function alleles: Mst27D^LL, containing a piggyBac insertion in the coding region, and Mst27D^cc, an intragenic deletion removing the start codon and most of the coding sequence. Homozygous animals survived to adulthood without conspicuous general morphological defects; Mst27D^cc homozygotes represented 34% of eclosing progeny. Female fertility was unaffected, whereas hemizygous mutant males produced only approximately 20% of control progeny, establishing a relatively specific requirement in male reproduction. (li2023nuclearelongationduring pages 16-18)
The nuclear-shaping phenotype was highly penetrant:
The locus lies within an intron of Mnn1, creating a potential attribution concern. However, genomic transgenes encoding full-length Mst27D-EGFP or Mst27D-mCherry rescued male fertility and nuclear elongation. Constructs encoding only the CH-containing or C-terminal portions failed to rescue and localized abnormally. These results strongly assign the phenotype to Mst27D and show that its microtubule- and NPC-interacting functions must be integrated within the full-length protein. (li2023nuclearelongationduring pages 16-18, li2023nuclearelongationduring pages 18-19)
Mst27D loss does not grossly block the histone-to-transition-protein/protamine program. Mutant and control testes contained comparable numbers of Tpl94D-positive cysts—19.1 ± 3.6 versus 19.7 ± 3.2 per testis tube—and ProtB-positive cysts—23.5 ± 4.6 versus 26.5 ± 4.8—with preserved spatial ordering. The severe shape defect therefore reflects impaired nuclear-envelope/cytoskeletal mechanics rather than wholesale failure to initiate protamine incorporation. Subtle chromatin-composition defects were not excluded by these marker measurements. (li2023nuclearelongationduring pages 18-19)
Actin investment cones can assemble in Mst27D mutants, distinguishing Mst27D from factors directly required for actin-cone biogenesis. Nevertheless, abnormal nuclear geometry, persistence of Nup58-EGFP on the nuclear envelope, defective NPC-envelope shedding, and partial individualization abnormalities connect the primary shaping defect to later sperm maturation. (kawadkar2025nup43positivelyregulates pages 16-20, li2023nuclearelongationduring pages 21-22)
Mst27D was proposed to have arisen by retroposition from CG15306, a testis-expressed EB1-family gene. It has retained an EB1-related CH region but diverged in its C-terminal architecture and cellular behavior. The most plausible evolutionary interpretation is neofunctionalization: an ancestral microtubule-binding module was adapted to bind Nup358, oligomerize, and organize the specialized dense complex of Drosophila spermatids. This origin is supported by comparative sequence/genomic analysis, whereas the precise evolutionary steps and species range of the mechanism remain less firmly established than the cell-biological function in D. melanogaster. (li2023nuclearelongationduring pages 24-25, li2023nuclearelongationduring pages 2-4)
The major recent advance is the peer-reviewed article by Li, Messina and Lehner, published in July 2023 in PLoS Genetics: “Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by Drosophila Mst27D,” volume 19, e1010837. URL: https://doi.org/10.1371/journal.pgen.1010837. It integrated live imaging, loss-of-function genetics, genomic rescue, affinity-purification mass spectrometry, domain/chimera experiments, RNAi/degradation, and quantitative morphology to establish the current mechanistic model. (li2023nuclearelongationduring pages 1-2, li2023nuclearelongationduring pages 16-18, li2023nuclearelongationduring pages 18-19, li2023nuclearelongationduring pages 4-6)
No substantive Mst27D-specific 2024 publication was identified in the searches. A September/October 2025 bioRxiv preprint on Nup43 used Mst27D-mCherry as a localization marker in a Nup43-knockout background. Mst27D abundance and asymmetric chromatin-associated localization appeared comparable to controls even though Nup43-deficient spermatids remained disorganized and failed individualization. This result argues that Mst27D mislocalization is not the explanation for the Nup43 phenotype, but it is not an independent Mst27D perturbation study. URL: https://doi.org/10.1101/2025.09.29.679220. (kawadkar2025nup43positivelyregulates pages 11-16)
Current real-world use is therefore principally as a basic-research model and experimental marker for:
No clinical, diagnostic, agricultural, or industrial implementation was identified, and no human ortholog with an established equivalent function can be inferred merely from the conserved CH domain.
The strongest functional annotation is:
Spermatid-specific microtubule-associated structural adaptor that couples Nup358-containing nuclear pore complexes to dense-complex microtubule bundles, promoting microtubule bundling, linear nuclear-envelope remodeling, and straight nuclear elongation during spermiogenesis.
Recommended process annotations include spermatid development, sperm-nucleus morphogenesis, microtubule-bundle organization, nuclear-envelope organization/remodeling, nuclear-pore organization, and male fertility. Recommended localization terms include spermatid nuclear envelope/nuclear pore complex cytoplasmic face, perinuclear dense complex, and associated microtubule bundles. An EB1-like “microtubule plus-end tracking” annotation should be avoided unless future experiments demonstrate it directly. (li2023nuclearelongationduring pages 22-24, li2023nuclearelongationduring pages 12-13, li2023nuclearelongationduring pages 8-10, li2023nuclearelongationduring pages 19-21)
The overall evidence for the primary function is high, because two independent loss-of-function alleles, full-length genomic rescue, domain dissection, interaction proteomics, partner-dependence tests, and live-cell localization all converge on the same mechanism. The main limitations are that the detailed mechanism rests predominantly on one comprehensive 2023 study, direct purified-protein reconstitution of NPC–Mst27D–microtubule coupling is lacking, and literature through 2024 is sparse.
References
(li2023nuclearelongationduring pages 16-18): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 2-4): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 1-2): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 22-24): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 8-10): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 10-12): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 24-25): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 19-21): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 4-6): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 12-13): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 18-19): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(li2023nuclearelongationduring pages 21-22): Pengfei Li, Giovanni Messina, and Christian F. Lehner. Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by drosophila mst27d. Jul 2023. URL: https://doi.org/10.1371/journal.pgen.1010837, doi:10.1371/journal.pgen.1010837. This article has 12 citations and is from a domain leading peer-reviewed journal.
(kawadkar2025nup43positivelyregulates pages 16-20): Jyotsna Kawadkar, Ashley Suraj Hermon, Rohit Kumar, and Ram Kumar Mishra. Nup43 positively regulates drosophila fertility and myosin vi-dependent actin cone assembly during spermiogenesis. bioRxiv, Oct 2025. URL: https://doi.org/10.1101/2025.09.29.679220, doi:10.1101/2025.09.29.679220. This article has 0 citations.
(kawadkar2025nup43positivelyregulates pages 11-16): Jyotsna Kawadkar, Ashley Suraj Hermon, Rohit Kumar, and Ram Kumar Mishra. Nup43 positively regulates drosophila fertility and myosin vi-dependent actin cone assembly during spermiogenesis. bioRxiv, Oct 2025. URL: https://doi.org/10.1101/2025.09.29.679220, doi:10.1101/2025.09.29.679220. This article has 0 citations.