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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The requested identity is verified. Caenorhabditis elegans unc-11—the locus historically assigned to ORF C32E8.10 and protein Q9XZI6—encodes the worm ortholog of neuronal AP180, a member of the PICALM/SNAP91 clathrin-adaptor family. Genetic rescue with an 8.8-kb genomic fragment and identification of five independent unc-11 mutations in its sole predicted ORF established the locus experimentally. UNC-11 shares 44.7% sequence identity with mouse AP180 and 41.4% with human CALM/PICALM, with strongest conservation in its N-terminal region. Thus, this report concerns the correct worm gene rather than a similarly named gene from another organism. (nonet1999unc11acaenorhabditis pages 3-6)
UNC-11 is not an enzyme or transporter. It is a predominantly neuronal, membrane-associated assembly adaptor/scaffold that operates at presynaptic membrane-retrieval sites. Its central functions are to organize clathrin-associated synaptic-vesicle formation, recruit selected cargo—most clearly synaptobrevin/VAMP—couple PI(4,5)P₂-rich membranes to actin, and constrain the diameter and molecular composition of recycled vesicles. Loss of UNC-11 does not abolish membrane endocytosis, but it produces abnormally large, compositionally altered vesicles and profoundly inefficient neurotransmission. (nonet1999unc11acaenorhabditis pages 12-14, nonet1999unc11acaenorhabditis pages 1-2, wang2026endocyticproteinap180 pages 12-15)
| Question/feature | Best-supported annotation | Direct evidence and key quantitative result | Evidence status | Principal source/year |
|---|---|---|---|---|
| Identity | unc-11/C32E8.10 encodes the C. elegans AP180-like clathrin adaptor corresponding to UniProt Q9XZI6. | An 8.8-kb genomic fragment rescued the mutant phenotype; five independent unc-11 alleles mapped within the single ORF. UNC-11 is 44.7% identical to mouse AP180 and 41.4% identical to human CALM/PICALM. (nonet1999unc11acaenorhabditis pages 3-6) | Direct worm genetics and sequence comparison | Nonet et al., 1999 |
| Architecture and isoforms | UNC-11 has a conserved N-terminal ANTH domain and a variable, intrinsically disordered C-terminal assembly domain; alternative splicing produces isoforms A–F. | The locus has nine coding exons and six transcript classes. Modern mapping places the ANTH domain at residues 1–304 and the assembly domain at residues 305–546; immunoblots detected approximately 60-, 65-, and 75-kDa products. (nonet1999unc11acaenorhabditis pages 6-8, wang2026endocyticproteinap180 pages 2-4) | Direct worm molecular evidence; disorder supported by worm-protein biochemistry | Nonet et al., 1999; Wang et al., 2026 |
| Cellular and tissue localization | UNC-11 is predominantly neuronal and enriched at presynaptic regions, with additional signal in neuronal somata and lower expression outside the nervous system. | Antibody staining was punctate in the nerve ring and dorsal and ventral nerve cords, overlapping synaptotagmin-positive synaptic regions but appearing more diffuse; null-like alleles eliminated this staining. (nonet1999unc11acaenorhabditis pages 6-8, nonet1999unc11acaenorhabditis pages 1-2) | Direct worm immunolocalization | Nonet et al., 1999 |
| Clathrin-associated assembly | UNC-11 functions as a monomeric clathrin-associated assembly adaptor during synaptic membrane retrieval. | The UNC-11 C-terminal region promoted clathrin assembly in vitro. Endocytosis still occurred in null mutants, indicating that UNC-11 controls coat geometry and cargo composition rather than being absolutely required for membrane internalization. (nonet1999unc11acaenorhabditis pages 6-8, nonet1999unc11acaenorhabditis pages 12-14) | Biochemical assay with worm protein plus direct worm ultrastructure | Nonet et al., 1999 |
| Membrane and lipid recognition | The ANTH domain is expected to recruit UNC-11 to PI(4,5)P₂-rich membranes; full-length UNC-11 can couple such membranes to actin. | Full-length protein associated with 50-nm liposomes containing 2% PIP₂ and bridged them to F-actin, whereas phosphatidylcholine-only liposomes showed minimal association. Assignment of the canonical ANTH lipid-binding mechanism is also supported by AP180-family conservation. (wang2026endocyticproteinap180 pages 12-15) | Biochemical evidence with worm protein; detailed binding mode partly family inference | Wang et al., 2026 |
| Synaptobrevin sorting | UNC-11 promotes incorporation and retention of synaptobrevin/VAMP on synaptic vesicles. | Null mutants had reduced vesicular synaptobrevin and diffuse or plasma-membrane-associated GFP–synaptobrevin, whereas localization of other tested vesicle proteins was comparatively preserved. (nonet1999unc11acaenorhabditis pages 12-14, nonet1999unc11acaenorhabditis pages 1-2) | Direct worm genetics, imaging, and vesicle analysis | Nonet et al., 1999 |
| Synaptic-vesicle size control | UNC-11 constrains vesicle diameter during recycling; it is not itself an enzyme or transporter. | Wild-type vesicles averaged 29.5 ± 5.4 nm, versus 39.1 ± 7.3 nm in e47 and 40.4 ± 8.0 nm in q358—about 33% greater diameter and 77% greater membrane area. A later study measured 32.1 ± 0.2 nm in wild type and 40.2 ± 0.2 nm in null mutants. (nonet1999unc11acaenorhabditis pages 12-14, wang2026endocyticproteinap180 pages 7-10) | Direct worm electron microscopy | Nonet et al., 1999; Wang et al., 2026 |
| Actin coupling and condensates | The disordered assembly domain concentrates actin monomers, promotes filament formation, and couples cortical actin to PIP₂-rich membranes; this activity helps set vesicle size. | Full-length UNC-11 and its isolated assembly domain formed salt-sensitive, fusing, FRAP-recovering condensates that recruited G-actin and generated F-actin within minutes. Replacing the domain with Lifeact restored vesicle diameter to 35.0 ± 0.3 nm, miniature-event frequency to 37 ± 5 Hz, and amplitude to 26 ± 2 pA. (wang2026endocyticproteinap180 pages 12-15, wang2026endocyticproteinap180 pages 10-12) | Biochemical evidence with worm protein plus direct worm domain-rescue experiments | Wang et al., 2026 |
| Neurotransmission | UNC-11 is required for efficient evoked and spontaneous synaptic transmission; enlarged vesicles increase quantal amplitude even as null mutants release far less frequently. | Null alleles produced evoked EPSCs of 0.19–0.20 nA versus 3.24 ± 0.20 nA in wild type and miniature frequencies of 6–11 Hz versus 53 ± 3 Hz, while amplitudes rose to 30–31 pA from 22 ± 2 pA. Full-length neuronal UNC-11 rescued these defects. (wang2026endocyticproteinap180 pages 2-4) | Direct worm electrophysiology and rescue | Wang et al., 2026 |
| Complexin relationship | UNC-11-dependent vesicle geometry enables curvature-sensitive complexin clamping of spontaneous fusion; complexin remains necessary for evoked release. | Removing complexin increased spontaneous frequency in wild type but not at UNC-11ΔAD synapses. Vesicle-tethered CPX-1::RAB-3 restored inhibition to 24 ± 6 Hz, whereas untethered CPX-1 or a tether lacking its SNARE-binding helix did not. (wang2026endocyticproteinap180 pages 7-10) | Direct worm genetics, electrophysiology, and engineered rescue | Wang et al., 2026 |
| ATG-9 sorting and presynaptic autophagy extension | UNC-11/AP180 also participates in sorting the autophagy membrane protein ATG-9 at synapses, linking endocytic organization to activity-dependent presynaptic autophagy. | unc-11(e47) caused abnormal subsynaptic ATG-9 foci that phenocopied cla-1 defects; genetic interactions support an AP180/AP-2-dependent step in budding ATG-9 carriers from endocytic intermediates. Direct UNC-11 localization to a periactive zone or a direct autophagic-flux measurement in unc-11 mutants was not established. (xuan2023theactivezone pages 11-13, xuan2023theactivezone pages 10-11, xuan2023theactivezone pages 17-18) | Direct worm genetic and imaging evidence for ATG-9 sorting; pathway model partly inferential | Xuan et al., 2023 |
Table: Evidence-weighted annotation of C. elegans UNC-11/Q9XZI6, separating direct worm findings and worm-protein biochemistry from AP180-family inference. Quantitative results define its principal role in presynaptic cargo sorting, actin-coupled vesicle-size control, and neurotransmission.
The locus contains nine coding exons and generates six reported splice classes, UNC-11A–F. All share the conserved N-terminal region encoded by exons 1–4, while alternative use of downstream exons changes the C-terminal region and the number of NPF motifs. At least three products of approximately 60, 65, and 75 kDa were detected by immunoblotting. The largest originally predicted isoform was 588 amino acids. (nonet1999unc11acaenorhabditis pages 6-8, nonet1999unc11acaenorhabditis pages 3-6)
Modern functional mapping divides the experimentally studied protein into an N-terminal ANTH domain, residues 1–304, and a largely intrinsically disordered assembly domain (AD), residues 305–546. This agrees with the supplied InterPro assignments—ANTH, ENTH/VHS superfamily, and AP180-like—and with membership in the AP180/PICALM/SNAP91 family. The older sequence analysis identified a strongly conserved approximately 290-residue N-terminal region, 62.8% identical to mouse AP180, and a more divergent C terminus, 27.1% identical. (nonet1999unc11acaenorhabditis pages 3-6, wang2026endocyticproteinap180 pages 2-4)
The ANTH/ENTH terminology requires care: UNC-11 is functionally and evolutionarily an AP180-type ANTH-domain protein. Broader InterPro ENTH/VHS labels describe structural-superfamily relationships and should not be interpreted as evidence that UNC-11 is a canonical epsin.
UNC-11’s C-terminal region promotes clathrin assembly in vitro, directly supporting its classification as a clathrin assembly adaptor. Ultrastructurally, however, null mutants still contain synaptic vesicles and recognizable neuromuscular synapses. UNC-11 is therefore not absolutely required to internalize membrane; instead, it governs the geometry and cargo composition of vesicles generated during recycling. Alternative or partially redundant internalization routes likely remain active in the null background. (nonet1999unc11acaenorhabditis pages 6-8, nonet1999unc11acaenorhabditis pages 12-14)
The best-supported mechanistic model is that UNC-11 is recruited to phosphoinositide-rich presynaptic membrane through its ANTH domain, while its disordered assembly region organizes coat and cytoskeletal components. Direct biochemical work with worm protein showed that full-length UNC-11 associated with 50-nm liposomes containing 2% PI(4,5)P₂, 25% phosphatidylserine, and 71% phosphatidylcholine, whereas phosphatidylcholine-only liposomes showed little association. The canonical atomic details of ANTH–PI(4,5)P₂ recognition derive partly from AP180-family conservation, but membrane selectivity and membrane-to-actin bridging have now been demonstrated with UNC-11 itself. (wang2026endocyticproteinap180 pages 12-15)
The strongest cargo-specific evidence concerns synaptobrevin, the vesicular R-SNARE. In unc-11 mutants, synaptobrevin was depleted from isolated synaptic vesicles and GFP–synaptobrevin became diffuse or plasma-membrane-associated instead of remaining concentrated in synaptic vesicles. Other vesicle proteins tested in the foundational study were much less affected. UNC-11 therefore performs selective cargo capture or retention, rather than indiscriminately controlling all vesicular proteins. (nonet1999unc11acaenorhabditis pages 12-14, nonet1999unc11acaenorhabditis pages 1-2)
Although AP180-family ANTH domains are broadly understood to interact with VAMP/synaptobrevin, the most secure worm-specific annotation is phenotypic and cell biological: UNC-11 is required for efficient synaptobrevin incorporation into recycled vesicles. A direct binding constant for purified UNC-11 and worm synaptobrevin was not established in the evidence reviewed here.
Electron microscopy originally showed average synaptic-vesicle diameters of 29.5 ± 5.4 nm in wild type, compared with 39.1 ± 7.3 nm in unc-11(e47) and 40.4 ± 8.0 nm in unc-11(q358). This is approximately a 33% increase in diameter and 77% increase in membrane area. The N-terminal in-frame-deletion allele n2954 produced both normal-sized and enlarged populations, consistent with partial domain function. (nonet1999unc11acaenorhabditis pages 12-14)
A recent mechanistic study independently measured 32.1 ± 0.2 nm in wild type and 40.2 ± 0.2 nm in null mutants; deletion of the assembly domain yielded 40.4 ± 0.2 nm vesicles. The difference in absolute wild-type values likely reflects experimental or analytical differences, while both studies agree on a robust enlargement phenotype. (wang2026endocyticproteinap180 pages 7-10)
The newer work identifies actin coupling as a major mechanism. Full-length UNC-11 and its isolated assembly domain formed salt-sensitive, fusing, FRAP-recovering condensates in vitro. These condensates enriched G-actin, supported appearance of F-actin within minutes, and associated with assembled filaments. Full-length UNC-11 additionally bridged F-actin to PI(4,5)P₂-containing liposomes. (wang2026endocyticproteinap180 pages 12-15, wang2026endocyticproteinap180 pages 10-12)
Domain replacement experiments provide causal support rather than merely correlation. Substitution with the actin-interacting HIPR-1 or epsin C-terminal regions reduced vesicle diameters to 35.6 ± 0.5 nm and 34.7 ± 0.4 nm, respectively. Removing HIPR-1’s THATCH actin-binding module impaired rescue, producing 39.8 ± 0.3 nm vesicles. Addition of the 17-residue Lifeact motif to UNC-11ΔAD restored diameter to 35.0 ± 0.3 nm and improved miniature-event frequency and amplitude to 37 ± 5 Hz and 26 ± 2 pA. These experiments indicate that actin interaction is a central and partly substitutable activity of the assembly domain. (wang2026endocyticproteinap180 pages 10-12)
UNC-11 is expressed most strongly in the nervous system, with lower expression outside it. Antibody staining showed punctate enrichment in the nerve ring and dorsal and ventral nerve cords, overlapping synaptotagmin-positive synaptic regions, although UNC-11 staining was more diffuse. Protein was also observed in neuronal cell bodies. Severe alleles eliminated or markedly reduced this staining, supporting antibody specificity. (nonet1999unc11acaenorhabditis pages 6-8, nonet1999unc11acaenorhabditis pages 1-2)
The functional site is therefore the cytoplasmic face of presynaptic membranes and associated endocytic/recycling structures, rather than the extracellular space or vesicle lumen. The available evidence supports presynaptic enrichment, but does not justify labeling UNC-11 as an exclusive active-zone protein. Recent work sometimes uses UNC-11 as an endocytic-zone reference, yet the 2023 ATG-9 study did not itself directly prove a precise periactive-zone localization for UNC-11. (xuan2023theactivezone pages 15-17, xuan2023theactivezone pages 8-10)
UNC-11 acts after exocytosis during clathrin-associated membrane and cargo retrieval, helping to regenerate correctly sized, fusion-competent vesicles. Null mutants remain viable but display coiling, backward jerking, and uncoordinated locomotion, consistent with broad defects in neuronal transmission. Multiple neurotransmitter systems are impaired, although this is best interpreted as a consequence of defective vesicle recycling rather than direct action in transmitter synthesis. (nonet1999unc11acaenorhabditis pages 2-3)
Electrophysiology quantifies the severity. Two null alleles produced evoked EPSCs of only 0.20 ± 0.04 nA and 0.19 ± 0.04 nA, versus 3.24 ± 0.20 nA in wild type. Spontaneous frequencies fell to 6 ± 1 and 11 ± 3 Hz, versus 53 ± 3 Hz. In contrast, spontaneous amplitudes increased from 22 ± 2 pA to 31 ± 2 and 30 ± 2 pA, consistent with enlarged vesicles carrying larger quanta. Pan-neuronal full-length UNC-11 restored evoked current to 3.1 ± 0.2 nA, frequency to 51 ± 6 Hz, and amplitude to 23 ± 1 pA. (wang2026endocyticproteinap180 pages 2-4)
Assembly-domain deletion separated recycling efficiency from size control. UNC-11ΔAD increased evoked current to 4.3 ± 0.2 nA and spontaneous frequency to 75 ± 5 Hz, yet failed to normalize quantal amplitude (37 ± 2 pA) or vesicle diameter. Thus, the ANTH-containing fragment can support substantial release, whereas the assembly domain is specifically required to impose normal vesicle morphology and release regulation. (wang2026endocyticproteinap180 pages 2-4)
The latest mechanistic interpretation connects UNC-11-dependent vesicle size to complexin-mediated fusion clamping. Complexin loss increased spontaneous release in wild type but had little additional effect at UNC-11ΔAD synapses, under either 1 or 0.25 mM extracellular Ca²⁺, while evoked responses still required complexin. Tethering CPX-1 directly to vesicles through RAB-3 restored spontaneous inhibition to 24 ± 6 Hz; untethered CPX-1 and a tether lacking the SNARE-binding helix did not. The authors infer that low curvature on enlarged vesicles reduces normal complexin recruitment or clamping, linking endocytic morphology to subsequent exocytic behavior. (wang2026endocyticproteinap180 pages 7-10)
This is an important conceptual advance: UNC-11 does not merely replenish vesicles. By setting their curvature, it determines how effectively curvature-sensitive release regulators control those vesicles in the next cycle.
A 2023 study broadened UNC-11’s cargo repertoire. unc-11(e47) animals developed abnormal subsynaptic ATG-9::GFP foci resembling those in cla-1 mutants, and genetic interactions placed AP180/UNC-11 and AP-2 in synaptic ATG-9 sorting. The proposed pathway has adaptor complexes helping bud ATG-9 carriers from endocytic intermediates near synapses. Because ATG-9 delivery supports activity-dependent presynaptic autophagosome formation, UNC-11-mediated sorting may couple endocytic organization to presynaptic proteostasis. (xuan2023theactivezone pages 11-13, xuan2023theactivezone pages 10-11, xuan2023theactivezone pages 17-18)
This extension should be stated conservatively. The study directly established an UNC-11-dependent ATG-9 localization phenotype, but did not directly quantify autophagic flux in unc-11 mutants or demonstrate that UNC-11 itself occupies a sharply defined periactive zone. CLA-1L’s role in activity-induced autophagy is stronger than the direct evidence for UNC-11 in that downstream process. (xuan2023theactivezone pages 15-17, xuan2023theactivezone pages 1-2)
UNC-11 is used primarily as an in vivo mechanistic model, not as a clinical target or industrial protein. Its principal applications are:
The functional annotation is unusually strong for a worm adaptor because it combines classical genetics, rescue, immunolocalization, ultrastructure, electrophysiology, and purified-protein reconstitution. The highest-confidence annotation is:
UNC-11 is a presynaptic AP180-family adaptor that organizes clathrin-associated recycling, sorts synaptobrevin and selected additional membrane cargo, and uses its ANTH and disordered assembly domains to couple phosphoinositide-rich membrane, coat assembly, and actin so that recycled synaptic vesicles acquire the correct size and release properties.
Several qualifications remain important. First, clathrin and AP-2 association is strongly supported by family biology and clathrin-assembly assays, but a complete quantitative interactome for native worm UNC-11 is unavailable. Second, altered cargo composition could contribute to the enlarged-vesicle and release phenotypes; the recent study explicitly notes that morphology-specific causality cannot be fully isolated without biochemical purification or proteomics of distinct vesicle populations. Third, condensate formation and actin nucleation were observed in reconstituted systems; their precise material state and concentration dependence in living presynaptic terminals remain to be established. (wang2026endocyticproteinap180 pages 12-15)
The targeted 2023–2024 literature is limited: UNC-11 was not the principal subject of a major dedicated paper in that interval. The most informative 2023 result extended UNC-11 function to synaptic ATG-9 sorting. The most detailed modern mechanistic study is instead the February 2026 PLOS Biology paper, which supplies direct evidence for assembly-domain condensates, actin recruitment, domain-swap rescue, and the curvature–complexin relationship. These newer findings refine rather than overturn the foundational 1999 model. (wang2026endocyticproteinap180 pages 12-15, wang2026endocyticproteinap180 pages 1-2, xuan2023theactivezone pages 1-2)
Overall, the experimental literature supports annotating Q9XZI6/UNC-11 primarily as a presynaptic phosphoinositide-binding, clathrin-associated, actin-coupling cargo adaptor and vesicle-size determinant, with additional participation in ATG-9 sorting. There is no evidence that it catalyzes a chemical reaction or transports a soluble substrate across a membrane.
References
(nonet1999unc11acaenorhabditis pages 3-6): Michael L. Nonet, Andrea M. Holgado, Faraha Brewer, Craig J. Serpe, Betty A. Norbeck, Julianne Holleran, Liping Wei, Erika Hartwieg, Erik M. Jorgensen, and Aixa Alfonso. Unc-11, a caenorhabditis elegans ap180 homologue, regulates the size and protein composition of synaptic vesicles. Molecular biology of the cell, 10 7:2343-60, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2343, doi:10.1091/mbc.10.7.2343. This article has 336 citations and is from a domain leading peer-reviewed journal.
(nonet1999unc11acaenorhabditis pages 12-14): Michael L. Nonet, Andrea M. Holgado, Faraha Brewer, Craig J. Serpe, Betty A. Norbeck, Julianne Holleran, Liping Wei, Erika Hartwieg, Erik M. Jorgensen, and Aixa Alfonso. Unc-11, a caenorhabditis elegans ap180 homologue, regulates the size and protein composition of synaptic vesicles. Molecular biology of the cell, 10 7:2343-60, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2343, doi:10.1091/mbc.10.7.2343. This article has 336 citations and is from a domain leading peer-reviewed journal.
(nonet1999unc11acaenorhabditis pages 1-2): Michael L. Nonet, Andrea M. Holgado, Faraha Brewer, Craig J. Serpe, Betty A. Norbeck, Julianne Holleran, Liping Wei, Erika Hartwieg, Erik M. Jorgensen, and Aixa Alfonso. Unc-11, a caenorhabditis elegans ap180 homologue, regulates the size and protein composition of synaptic vesicles. Molecular biology of the cell, 10 7:2343-60, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2343, doi:10.1091/mbc.10.7.2343. This article has 336 citations and is from a domain leading peer-reviewed journal.
(wang2026endocyticproteinap180 pages 12-15): Yu Wang, Lanxi Wu, Lin Zhang, Yongming Dong, Aaradhya Pant, Yan Liu, and Jihong Bai. Endocytic protein ap180 assembly domain regulates synaptic vesicle size and release in caenorhabditis elegans. PLOS Biology, 24:e3003643, Feb 2026. URL: https://doi.org/10.1371/journal.pbio.3003643, doi:10.1371/journal.pbio.3003643. This article has 0 citations and is from a highest quality peer-reviewed journal.
(nonet1999unc11acaenorhabditis pages 6-8): Michael L. Nonet, Andrea M. Holgado, Faraha Brewer, Craig J. Serpe, Betty A. Norbeck, Julianne Holleran, Liping Wei, Erika Hartwieg, Erik M. Jorgensen, and Aixa Alfonso. Unc-11, a caenorhabditis elegans ap180 homologue, regulates the size and protein composition of synaptic vesicles. Molecular biology of the cell, 10 7:2343-60, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2343, doi:10.1091/mbc.10.7.2343. This article has 336 citations and is from a domain leading peer-reviewed journal.
(wang2026endocyticproteinap180 pages 2-4): Yu Wang, Lanxi Wu, Lin Zhang, Yongming Dong, Aaradhya Pant, Yan Liu, and Jihong Bai. Endocytic protein ap180 assembly domain regulates synaptic vesicle size and release in caenorhabditis elegans. PLOS Biology, 24:e3003643, Feb 2026. URL: https://doi.org/10.1371/journal.pbio.3003643, doi:10.1371/journal.pbio.3003643. This article has 0 citations and is from a highest quality peer-reviewed journal.
(wang2026endocyticproteinap180 pages 7-10): Yu Wang, Lanxi Wu, Lin Zhang, Yongming Dong, Aaradhya Pant, Yan Liu, and Jihong Bai. Endocytic protein ap180 assembly domain regulates synaptic vesicle size and release in caenorhabditis elegans. PLOS Biology, 24:e3003643, Feb 2026. URL: https://doi.org/10.1371/journal.pbio.3003643, doi:10.1371/journal.pbio.3003643. This article has 0 citations and is from a highest quality peer-reviewed journal.
(wang2026endocyticproteinap180 pages 10-12): Yu Wang, Lanxi Wu, Lin Zhang, Yongming Dong, Aaradhya Pant, Yan Liu, and Jihong Bai. Endocytic protein ap180 assembly domain regulates synaptic vesicle size and release in caenorhabditis elegans. PLOS Biology, 24:e3003643, Feb 2026. URL: https://doi.org/10.1371/journal.pbio.3003643, doi:10.1371/journal.pbio.3003643. This article has 0 citations and is from a highest quality peer-reviewed journal.
(xuan2023theactivezone pages 11-13): Zhao Xuan, Sisi Yang, Benjamin Clark, Sarah E. Hill, Laura Manning, and Daniel A. Colón-Ramos. The active zone protein clarinet regulates synaptic sorting of atg-9 and presynaptic autophagy. PLOS Biology, 21:e3002030, Apr 2023. URL: https://doi.org/10.1371/journal.pbio.3002030, doi:10.1371/journal.pbio.3002030. This article has 29 citations and is from a highest quality peer-reviewed journal.
(xuan2023theactivezone pages 10-11): Zhao Xuan, Sisi Yang, Benjamin Clark, Sarah E. Hill, Laura Manning, and Daniel A. Colón-Ramos. The active zone protein clarinet regulates synaptic sorting of atg-9 and presynaptic autophagy. PLOS Biology, 21:e3002030, Apr 2023. URL: https://doi.org/10.1371/journal.pbio.3002030, doi:10.1371/journal.pbio.3002030. This article has 29 citations and is from a highest quality peer-reviewed journal.
(xuan2023theactivezone pages 17-18): Zhao Xuan, Sisi Yang, Benjamin Clark, Sarah E. Hill, Laura Manning, and Daniel A. Colón-Ramos. The active zone protein clarinet regulates synaptic sorting of atg-9 and presynaptic autophagy. PLOS Biology, 21:e3002030, Apr 2023. URL: https://doi.org/10.1371/journal.pbio.3002030, doi:10.1371/journal.pbio.3002030. This article has 29 citations and is from a highest quality peer-reviewed journal.
(xuan2023theactivezone pages 15-17): Zhao Xuan, Sisi Yang, Benjamin Clark, Sarah E. Hill, Laura Manning, and Daniel A. Colón-Ramos. The active zone protein clarinet regulates synaptic sorting of atg-9 and presynaptic autophagy. PLOS Biology, 21:e3002030, Apr 2023. URL: https://doi.org/10.1371/journal.pbio.3002030, doi:10.1371/journal.pbio.3002030. This article has 29 citations and is from a highest quality peer-reviewed journal.
(xuan2023theactivezone pages 8-10): Zhao Xuan, Sisi Yang, Benjamin Clark, Sarah E. Hill, Laura Manning, and Daniel A. Colón-Ramos. The active zone protein clarinet regulates synaptic sorting of atg-9 and presynaptic autophagy. PLOS Biology, 21:e3002030, Apr 2023. URL: https://doi.org/10.1371/journal.pbio.3002030, doi:10.1371/journal.pbio.3002030. This article has 29 citations and is from a highest quality peer-reviewed journal.
(nonet1999unc11acaenorhabditis pages 2-3): Michael L. Nonet, Andrea M. Holgado, Faraha Brewer, Craig J. Serpe, Betty A. Norbeck, Julianne Holleran, Liping Wei, Erika Hartwieg, Erik M. Jorgensen, and Aixa Alfonso. Unc-11, a caenorhabditis elegans ap180 homologue, regulates the size and protein composition of synaptic vesicles. Molecular biology of the cell, 10 7:2343-60, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2343, doi:10.1091/mbc.10.7.2343. This article has 336 citations and is from a domain leading peer-reviewed journal.
(xuan2023theactivezone pages 1-2): Zhao Xuan, Sisi Yang, Benjamin Clark, Sarah E. Hill, Laura Manning, and Daniel A. Colón-Ramos. The active zone protein clarinet regulates synaptic sorting of atg-9 and presynaptic autophagy. PLOS Biology, 21:e3002030, Apr 2023. URL: https://doi.org/10.1371/journal.pbio.3002030, doi:10.1371/journal.pbio.3002030. This article has 29 citations and is from a highest quality peer-reviewed journal.
(wang2026endocyticproteinap180 pages 1-2): Yu Wang, Lanxi Wu, Lin Zhang, Yongming Dong, Aaradhya Pant, Yan Liu, and Jihong Bai. Endocytic protein ap180 assembly domain regulates synaptic vesicle size and release in caenorhabditis elegans. PLOS Biology, 24:e3003643, Feb 2026. URL: https://doi.org/10.1371/journal.pbio.3003643, doi:10.1371/journal.pbio.3003643. This article has 0 citations and is from a highest quality peer-reviewed journal.