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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target identity is verified. Caenorhabditis elegans dpy-23 is the same locus as apm-2 and encodes the worm’s sole μ2 medium subunit of the heterotetrameric AP-2 clathrin-adaptor complex. Genomic rescue, mutant mapping, and molecular characterization—not merely sequence similarity—established this assignment. This matches UniProt P35603 and the supplied names AP50/μ2-adaptin; no literature concerning a similarly named protein in another organism was used. (gu2008μ2adaptinfacilitates pages 2-3)
DPY-23 is not an enzyme or transporter. Its primary function is structural and selective: as the μ2 cargo-recognition subunit of AP-2, it helps couple plasma-membrane cargo and phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to the clathrin-coated-pit machinery. Its best-supported worm-specific roles are in clathrin organization and synaptic-vesicle recycling, MIG-14/Wntless internalization, glutamate-receptor trafficking, and membrane/protein organization at sensory-cilium bases. Some signaling and developmental phenotypes are therefore downstream consequences of altered membrane trafficking rather than evidence that DPY-23 is itself a canonical signaling protein. (gu2008μ2adaptinfacilitates pages 1-2, gu2008μ2adaptinfacilitates pages 1-1, pan2008c.elegansap2 pages 4-5, ditirro2019thecaenorhabditiselegans pages 16-17)
The names dpy-23, apm-2, and protein APM-2/DPY-23 refer to the same C. elegans locus and product. The locus was initially defined by dumpy mutants; RNA interference phenocopied the morphology, overlapping genomic clones rescued it, and a 12-kb genomic fragment containing apm-2 fully rescued dumpy, uncoordinated, and egg-laying defects. The study explicitly identified APM-2 as the only AP-2 μ2 subunit in the worm. (gu2008μ2adaptinfacilitates pages 2-3)
AP-2 comprises α and β2 large subunits, the μ2 medium subunit DPY-23, and a σ2 small subunit. The supplied InterPro assignments—Adaptor complex medium-subunit family, AP2_Mu_N, AP2_Mu_C superfamily, AP_mu_sigma, and clathrin-adaptor μ domains—are therefore internally consistent with the experimentally established identity. The characteristic architecture supports an N-terminal complex-assembly region and a C-terminal cargo-recognition region, although a purified DPY-23 domain structure was not identified in the retrieved worm literature. (garafalo2015theap2clathrin pages 1-4)
The mechanistic model is strongly conserved: μ2 recognizes cytoplasmic tyrosine-based YxxΦ sorting motifs, while μ2/AP-2 contacts PI(4,5)P2 and AP-2 recruits clathrin at plasma-membrane endocytic sites. These molecular interactions are established AP-2/μ2 principles cited by the worm studies, but should be distinguished from direct biochemical measurements using purified DPY-23. (gu2008μ2adaptinfacilitates pages 1-2, gu2008μ2adaptinfacilitates pages 1-1)
DPY-23 performs three closely connected functions:
DPY-23 also stabilizes the AP-2 complex. In apm-2(e840) and apm-2(gm17) mutants, α-adaptin abundance fell to approximately 60% and 12% of wild type, respectively. Residual α-adaptin nevertheless remained detectable at synapses and coelomocyte plasma membranes. Thus, DPY-23 is important for complex integrity, but some partial AP-2 assemblies or alternative interactions persist in its absence. This residual activity is an important qualification when interpreting viable mutants and incomplete endocytic phenotypes. (gu2008μ2adaptinfacilitates pages 6-7, gu2008μ2adaptinfacilitates pages 8-8)
DPY-23 is highly expressed in the nervous system and localizes to synapses, consistent with a local role in synaptic-vesicle membrane retrieval. Neuron-specific restoration of APM-2 rescued synaptic-vesicle abundance, directly supporting a neuronal, presynaptic function. (gu2008μ2adaptinfacilitates pages 1-1, gu2008μ2adaptinfacilitates pages 5-6)
Its localization is not exclusively neuronal. Tissue-specific rescue places a critical pool in Wnt-producing hypodermal cells, where DPY-23 mediates MIG-14/Wntless internalization. At AWB olfactory sensory endings, DPY-23::GFP is concentrated at the ciliary base/periciliary membrane compartment, a specialized membrane-trafficking zone. Residual AP-2 components also occur at coelomocyte plasma membranes. Collectively, the protein acts principally on the cytoplasmic face of the plasma membrane and at specialized endocytic membrane domains, rather than extracellularly or as a stable resident of the ciliary axoneme. (gu2008μ2adaptinfacilitates pages 6-7, pan2008c.elegansap2 pages 4-5, ditirro2019thecaenorhabditiselegans pages 16-17)
Loss of μ2 mislocalized synaptic clathrin and reduced synaptic-vesicle abundance to roughly 60% of control. Miniature-event frequency was 60% of wild type and evoked amplitude 82%; corresponding vesicle levels were 55% at GABAergic and 69% at cholinergic synapses. In broader summary measurements, evoked responses were approximately 65% of control. Neuronal rescue restored vesicle number. (gu2008μ2adaptinfacilitates pages 1-1, gu2008μ2adaptinfacilitates pages 5-6)
The defect was substantially milder than in synaptojanin or endophilin mutants, which retained only about 38% and 30% of normal vesicle numbers in one comparison, or approximately 35% in a broader comparison. Mutant animals retained neurotransmission, and synaptic-vesicle proteins remained localized. The correct annotation is therefore that DPY-23 facilitates but is not absolutely essential for synaptic-vesicle recycling. Residual AP-2 and AP-2-independent retrieval routes remain plausible explanations. (gu2008μ2adaptinfacilitates pages 5-6, gu2008μ2adaptinfacilitates pages 6-7, gu2008μ2adaptinfacilitates pages 8-8)
This is the clearest cargo-specific developmental mechanism. In dpy-23 mutants, MIG-14/Wntless::GFP accumulated close to the plasma membrane and in large membrane-associated vesicles, consistent with impaired internalization. By contrast, loss of retromer caused intracellular accumulation and reduced MIG-14 abundance, consistent with failure to retrieve internalized Wntless from a degradative route. (pan2008c.elegansap2 pages 4-5)
DPY-23 functions in Wnt-producing cells: hypodermal DPY-23::GFP completely rescued Q-cell migration defects and partly rescued HSN defects, whereas neuronal expression did not. Expression driven by the egl-20/Wnt promoter partly rescued both phenotypes. Extra MIG-14 rescued dpy-23 defects, but extra DPY-23 did not bypass mig-14. The resulting mechanistic model is sequential: AP-2/DPY-23 first internalizes surface MIG-14; retromer then retrieves it for recycling, sustaining repeated Wnt secretion and long-range developmental signaling. (pan2008c.elegansap2 pages 4-5)
Two independent apm-2 alleles reduced GLR-1::GFP fluorescence in ventral-nerve-cord puncta by 26% and 30%, respectively, both with p<0.001. Rescue and temporal experiments placed the requirement in mature GLR-1-expressing interneurons. Rather than simply accumulating at the surface as expected from a pure endocytosis block, GLR-1 accumulated in neuronal cell bodies and Syntaxin-13- and RAB-14-positive intracellular compartments. (garafalo2015theap2clathrin pages 1-4)
This indicates that AP-2/DPY-23 also supports an early secretory or endosomal trafficking step needed to maintain receptor abundance in neurites. It is an important warning against annotating every DPY-23 phenotype as reduced plasma-membrane uptake alone. (garafalo2015theap2clathrin pages 1-4)
DPY-23 localizes to the AWB periciliary membrane compartment. dpy-23 loss expands AWB ciliary membrane morphology, while loss of the Tubby-family protein TUB-1 completely suppresses this expansion; tub-1; dpy-23 cilia resemble tub-1 single mutants. DPY-23::GFP localization/intensity and PI(4,5)P2-reporter distribution were assessed directly by fluorescence imaging. (ditirro2019thecaenorhabditiselegans pages 16-17)
The favored model is that TUB-1 acts partly through DPY-23 to position PPK-1/PIP5 kinase and thereby regulate PI(4,5)P2 distribution, ciliary membrane shape, and ciliary signaling-protein traffic. The morphology, localization, and epistasis are direct observations; the precise linear TUB-1→DPY-23→PPK-1 mechanism remains an inference from those data. (ditirro2019thecaenorhabditiselegans pages 16-17)
In dpy-23(e840), GFP::DBL-1 abundance was 39.87 ± 14.82 relative units versus 100 ± 15.57 in controls (p=0.0005), whereas the spp-9p::GFP pathway reporter rose to 120.47 ± 13.55 (p=0.0015). These results establish that DPY-23 loss changes DBL-1 abundance and BMP-associated transcriptional output. They do not by themselves demonstrate that DPY-23 directly binds or transports DBL-1 or its receptor; models involving ligand trafficking, receptor trafficking, or indirect extracellular-matrix feedback remain to be resolved. (lakdawala2022identifyingandcharacterizing pages 33-39)
A forward suppressor study linked AP-2 activity to the NIMA-related kinases NEKL-2 and NEKL-3. The DPY-23 S434T allele fd155 allowed 98% of otherwise severely affected nekl-2; nekl-3 animals to reach adulthood, versus only 1–2% of the parental kinase-deficient animals. An independent Y275D allele, a predicted-null allele, and RNAi also suppressed, showing that the interaction was not unique to S434T. (joseph2020controlofclathrinmediated pages 3-5)
This is strong genetic evidence that lowering AP-2/DPY-23 activity counterbalances the NEKL-deficient state. It is not direct proof that NEKL proteins phosphorylate DPY-23; the mechanistic conclusion is pathway-level antagonism within clathrin-mediated endocytosis. (joseph2020controlofclathrinmediated pages 3-5)
The most directly relevant 2024 study examined SEL-5, the worm orthologue of AP2-associated kinase AAK1. Phospho-specific immunoblotting showed that SEL-5 loss reduced phosphorylation of DPY-23 at T160, corresponding to mammalian AP2M1 T156, but did not eliminate it. This implies at least one additional DPY-23 kinase. (knop2024caenorhabditiseleganssel5aak1 pages 6-7, knop2024caenorhabditiseleganssel5aak1 pages 7-8)
Crucially, animals expressing nonphosphorylatable DPY-23 did not reproduce the Wnt-dependent QL-descendant migration or excretory-canal shortening seen in sel-5; vps-29 animals, and kinase-inactive SEL-5 rescued those defects. MIG-14 abundance and localization were also not significantly altered in sel-5; vps-29. The authors therefore concluded that SEL-5’s roles in these developmental processes are kinase-independent and are not explained by failure to phosphorylate DPY-23 or by a simple MIG-14-internalization defect. The paper was published 19 July 2024 in eLife, DOI 10.7554/eLife.91054. (knop2024caenorhabditiseleganssel5aak1 pages 15-16, knop2024caenorhabditiseleganssel5aak1 pages 1-2, knop2024caenorhabditiseleganssel5aak1 pages 7-8)
No comparably substantial 2023 DPY-23-specific primary study was identified in the retrieved literature. Thus, the mechanistic foundation remains dominated by older, precise worm genetics and cell biology, with the 2024 work refining rather than replacing that model.
The following table separates direct measurements from pathway-level interpretation.
| Biological context | Direct finding | Evidence type / quantitative result | Interpretation | Key source / date / DOI URL |
|---|---|---|---|---|
| Protein identity | Direct: dpy-23 is apm-2 and encodes the sole C. elegans AP-2 μ2 medium subunit. |
Mutant mapping, RNAi phenocopy, and complete rescue of dumpy, uncoordinated, and egg-laying defects with a 12-kb genomic fragment. | Confirms that the target is AP-2 μ2—not an unrelated similarly named protein—and agrees with UniProt P35603 and the adaptor-complex medium-subunit family. | Gu et al.; Dec. 2008; 10.1083/jcb.200806088 (gu2008μ2adaptinfacilitates pages 2-3) |
| Synaptic-vesicle recycling | Direct: APM-2 is enriched in the nervous system and at synapses; its loss mislocalizes synaptic clathrin but does not abolish neurotransmission. | Mutant imaging, EM, rescue, and electrophysiology: vesicle abundance ≈60% of control; overall evoked responses ≈65%; miniature-event frequency 60%; evoked amplitude 82%; vesicle levels 55% at GABA and 69% at acetylcholine synapses. Neuronal expression rescued vesicle number. | DPY-23/AP-2 facilitates clathrin-dependent synaptic-vesicle recycling but is not absolutely essential; residual AP-2 or alternative recycling routes likely remain. | Gu et al.; Dec. 2008; 10.1083/jcb.200806088 (gu2008μ2adaptinfacilitates pages 1-1, gu2008μ2adaptinfacilitates pages 5-6, gu2008μ2adaptinfacilitates pages 6-7) |
| AP-2-complex stability | Direct: Loss of μ2 destabilizes AP-2 while leaving some correctly localized α-adaptin. | Quantitative immunoblotting: α-adaptin was 60% of wild type in apm-2(e840) and 12% in apm-2(gm17); residual α-adaptin localized to synapses and coelomocyte plasma membranes. |
DPY-23 contributes structurally to AP-2 assembly/stability. Persistence of residual complex helps explain the incomplete synaptic defect. | Gu et al.; Dec. 2008; 10.1083/jcb.200806088 (gu2008μ2adaptinfacilitates pages 6-7, gu2008μ2adaptinfacilitates pages 8-8) |
| Wntless recycling and Wnt secretion | Direct: DPY-23 acts principally in Wnt-producing cells and is required to internalize MIG-14/Wntless from the plasma membrane. | Tissue-specific rescue: hypodermal DPY-23::GFP completely rescued Q-cell and partly rescued HSN migration defects; neuronal expression did not. egl-20-promoter expression partly rescued both. In dpy-23 mutants, MIG-14::GFP accumulated near the plasma membrane and in large membrane-associated vesicles; excess MIG-14 rescued dpy-23 defects. |
DPY-23/AP-2 initiates MIG-14 endocytosis; retromer subsequently retrieves internalized MIG-14 for reuse, sustaining Wnt secretion. The sequential recycling model is an inference supported by localization, rescue, and genetic interaction. | Pan et al.; Jan. 2008; 10.1016/j.devcel.2007.12.001 (pan2008c.elegansap2 pages 4-5) |
| GLR-1 glutamate-receptor trafficking | Direct: Loss of APM-2 decreases GLR-1 abundance in ventral-nerve-cord puncta and causes intracellular receptor accumulation. | apm-2(gm17) reduced GLR-1::GFP punctal fluorescence by 26%; independent null allele e840 reduced it by 30% (both p<0.001). Rescue and adult-neuron experiments placed the requirement in GLR-1-expressing interneurons; retained receptor accumulated in Syntaxin-13- and RAB-14-positive endosomes. |
Beyond conventional surface uptake, DPY-23/AP-2 supports an early secretory or endosomal trafficking step needed to deliver or maintain GLR-1 at synaptic regions. | Garafalo et al.; May 2015; 10.1091/mbc.e14-06-1048 (garafalo2015theap2clathrin pages 1-4) |
| Sensory-cilium membrane organization | Direct: DPY-23 localizes at the AWB olfactory-cilium base/periciliary membrane compartment (PCMC), and dpy-23 loss expands ciliary membrane morphology. Loss of tub-1 suppresses that expansion. |
DPY-23::GFP and phosphoinositide-reporter imaging plus epistasis: tub-1; dpy-23 cilia resembled tub-1 single mutants; a DPY-23::GFP comparison reached p<0.001. |
Inference from genetics and localization: TUB-1 acts partly through PCMC-localized DPY-23 to position PPK-1/PIP5K and regulate PI(4,5)P2 distribution, ciliary membrane shape, and signaling-protein traffic. | DiTirro et al.; July 2019; 10.7554/eLife.48789 (ditirro2019thecaenorhabditiselegans pages 16-17) |
| NEKL kinase–endocytosis interaction | Direct: Partial or complete reduction of DPY-23 strongly suppresses developmental arrest caused by combined NEKL-2/NEKL-3 dysfunction. | Suppressor genetics: dpy-23(fd155) encodes S434T and allowed 98% of nekl-2; nekl-3 animals to reach adulthood versus 1–2% of parental double mutants; Y275D allele fd277, predicted-null fd279, and RNAi also suppressed. |
DPY-23/AP-2 activity is functionally antagonistic to the tested NEKL-deficient state. A direct biochemical phosphorylation relationship was not demonstrated in this experiment. | Joseph et al.; Feb. 18, 2020; 10.1371/journal.pgen.1008633 (joseph2020controlofclathrinmediated pages 3-5) |
| DBL-1/BMP pathway | Direct reporter observations: dpy-23(e840) reduces tagged DBL-1 abundance while increasing a downstream pathway reporter. |
GFP::DBL-1 fluorescence was 39.87 ± 14.82 relative units versus control 100 ± 15.57 (p=0.0005); spp-9p::GFP was 120.47 ± 13.55 (p=0.0015). |
DPY-23 influences DBL-1 abundance and BMP-associated output, but whether it transports DBL-1 or regulates its receptor complex is proposed rather than directly demonstrated. | Lakdawala; 2022 dissertation/report; DOI not supplied (lakdawala2022identifyingandcharacterizing pages 33-39) |
| SEL-5/AAK1 phosphorylation—recent development | Direct: SEL-5 loss reduces phosphorylation of DPY-23 at T160, the worm counterpart of mammalian AP2M1 T156; however, nonphosphorylatable DPY-23 does not reproduce SEL-5/retromer developmental defects. | Phospho-specific immunoblotting used endogenous DPY-23, DPY-23::GFP, and DPY-23(T160A)::GFP control. In genetic assays, vps-29; dpy-23(mew25) did not show the QL-descendant migration or shortened-canal phenotypes of sel-5 vps-29; kinase-inactive SEL-5 rescued those phenotypes. MIG-14 abundance/localization was not significantly altered in sel-5 vps-29. |
DPY-23 T160 is phosphorylated partly through SEL-5/AAK1, but this modification is dispensable for the examined Wnt-dependent migration and excretory-canal outgrowth. SEL-5 therefore has a kinase-independent/scaffolding role in these contexts. | Knop et al.; July 19, 2024; 10.7554/eLife.91054 (knop2024caenorhabditiseleganssel5aak1 pages 15-16, knop2024caenorhabditiseleganssel5aak1 pages 6-7, knop2024caenorhabditiseleganssel5aak1 pages 7-8) |
Table: Direct genetic, imaging, physiological, and biochemical evidence defining DPY-23/APM-2 function in C. elegans. Interpretive or pathway-level inferences are explicitly distinguished from experimental observations.
The historical “Dpy” phenotype reflects altered body morphology/cuticle biology, but it is not the protein’s primary biochemical activity. Depending on allele and tissue, mutants can also exhibit uncoordination, egg-laying defects, altered Wnt-dependent cell migration, perturbed synaptic physiology, receptor-trafficking defects, and abnormal ciliary membrane morphology. Full genomic rescue establishes that these phenotypes belong to the dpy-23/apm-2 locus. (gu2008μ2adaptinfacilitates pages 2-3)
Phenotypic interpretation requires caution. Neuronal APM-2 rescued synaptic-vesicle number, whereas skin expression—not neuronal expression—rescued some whole-animal thrashing and aldicarb phenotypes. Therefore, locomotor or pharmacological readouts can include non-neuronal contributions and should not automatically be treated as direct measures of synaptic AP-2 function. (gu2008μ2adaptinfacilitates pages 5-6)
DPY-23 is primarily a research model, not a clinical target with a worm-specific therapeutic implementation. Its practical applications include:
These uses have broader relevance because AP2M1/AP-2, Wntless-retromer recycling, synaptic-vesicle retrieval, and ciliary trafficking are conserved. Nevertheless, human disease or therapeutic claims should be made at the pathway level, not attributed directly to worm DPY-23 without cross-species validation.
Primary function: DPY-23 is the μ2 medium/cargo-recognition subunit of the C. elegans AP-2 clathrin-adaptor complex. It stabilizes AP-2 and helps select transmembrane cargo at PI(4,5)P2-rich plasma-membrane domains for clathrin-associated internalization.
Principal location: cytoplasmic face of the plasma membrane and specialized endocytic zones, including neuronal synapses, Wnt-producing hypodermal cells, coelomocyte membranes, and the periciliary membrane compartment of sensory neurons.
Best-supported processes: clathrin-mediated endocytosis; synaptic-vesicle recycling; MIG-14/Wntless internalization and retromer-dependent recycling; neuronal receptor trafficking; and ciliary membrane/phosphoinositide organization.
Regulation: DPY-23 is phosphorylated at T160 partly through SEL-5/AAK1, although this modification is dispensable for the specific Wnt-dependent migration and excretory-canal phenotypes tested in 2024. AP-2/DPY-23 activity also interacts genetically with NEKL kinase pathways. (joseph2020controlofclathrinmediated pages 3-5, knop2024caenorhabditiseleganssel5aak1 pages 15-16, knop2024caenorhabditiseleganssel5aak1 pages 6-7)
Evidence confidence: high for identity, AP-2 membership, synaptic localization/function, MIG-14 internalization, and GLR-1/ciliary trafficking phenotypes; moderate for exact cargo recognition by purified worm DPY-23 and for the proposed linear ciliary and BMP mechanisms, which rely partly on conserved AP-2 biology or genetic inference.
References
(gu2008μ2adaptinfacilitates pages 2-3): Mingyu Gu, Kim Schuske, Shigeki Watanabe, Qiang Liu, Paul Baum, Gian Garriga, and Erik M. Jorgensen. Μ2 adaptin facilitates but is not essential for synaptic vesicle recycling in caenorhabditis elegans. The Journal of Cell Biology, 183:881-892, Dec 2008. URL: https://doi.org/10.1083/jcb.200806088, doi:10.1083/jcb.200806088. This article has 69 citations.
(gu2008μ2adaptinfacilitates pages 1-2): Mingyu Gu, Kim Schuske, Shigeki Watanabe, Qiang Liu, Paul Baum, Gian Garriga, and Erik M. Jorgensen. Μ2 adaptin facilitates but is not essential for synaptic vesicle recycling in caenorhabditis elegans. The Journal of Cell Biology, 183:881-892, Dec 2008. URL: https://doi.org/10.1083/jcb.200806088, doi:10.1083/jcb.200806088. This article has 69 citations.
(gu2008μ2adaptinfacilitates pages 1-1): Mingyu Gu, Kim Schuske, Shigeki Watanabe, Qiang Liu, Paul Baum, Gian Garriga, and Erik M. Jorgensen. Μ2 adaptin facilitates but is not essential for synaptic vesicle recycling in caenorhabditis elegans. The Journal of Cell Biology, 183:881-892, Dec 2008. URL: https://doi.org/10.1083/jcb.200806088, doi:10.1083/jcb.200806088. This article has 69 citations.
(pan2008c.elegansap2 pages 4-5): Chun-Liang Pan, Paul D. Baum, Mingyu Gu, Erik M. Jorgensen, Scott G. Clark, and Gian Garriga. C. elegans ap-2 and retromer control wnt signaling by regulating mig-14/wntless. Developmental cell, 14 1:132-9, Jan 2008. URL: https://doi.org/10.1016/j.devcel.2007.12.001, doi:10.1016/j.devcel.2007.12.001. This article has 262 citations and is from a highest quality peer-reviewed journal.
(ditirro2019thecaenorhabditiselegans pages 16-17): Danielle DiTirro, Alison Philbrook, Kendrick Rubino, and Piali Sengupta. The caenorhabditis elegans tubby homolog dynamically modulates olfactory cilia membrane morphogenesis and phospholipid composition. Jul 2019. URL: https://doi.org/10.7554/elife.48789, doi:10.7554/elife.48789. This article has 28 citations and is from a domain leading peer-reviewed journal.
(garafalo2015theap2clathrin pages 1-4): Steven D. Garafalo, Eric S. Luth, Benjamin J. Moss, Michael I. Monteiro, Emily Malkin, and Peter Juo. The ap2 clathrin adaptor protein complex regulates the abundance of glr-1 glutamate receptors in the ventral nerve cord of caenorhabditis elegans. Molecular Biology of the Cell, 26:1887-1900, May 2015. URL: https://doi.org/10.1091/mbc.e14-06-1048, doi:10.1091/mbc.e14-06-1048. This article has 13 citations and is from a domain leading peer-reviewed journal.
(gu2008μ2adaptinfacilitates pages 6-7): Mingyu Gu, Kim Schuske, Shigeki Watanabe, Qiang Liu, Paul Baum, Gian Garriga, and Erik M. Jorgensen. Μ2 adaptin facilitates but is not essential for synaptic vesicle recycling in caenorhabditis elegans. The Journal of Cell Biology, 183:881-892, Dec 2008. URL: https://doi.org/10.1083/jcb.200806088, doi:10.1083/jcb.200806088. This article has 69 citations.
(gu2008μ2adaptinfacilitates pages 8-8): Mingyu Gu, Kim Schuske, Shigeki Watanabe, Qiang Liu, Paul Baum, Gian Garriga, and Erik M. Jorgensen. Μ2 adaptin facilitates but is not essential for synaptic vesicle recycling in caenorhabditis elegans. The Journal of Cell Biology, 183:881-892, Dec 2008. URL: https://doi.org/10.1083/jcb.200806088, doi:10.1083/jcb.200806088. This article has 69 citations.
(gu2008μ2adaptinfacilitates pages 5-6): Mingyu Gu, Kim Schuske, Shigeki Watanabe, Qiang Liu, Paul Baum, Gian Garriga, and Erik M. Jorgensen. Μ2 adaptin facilitates but is not essential for synaptic vesicle recycling in caenorhabditis elegans. The Journal of Cell Biology, 183:881-892, Dec 2008. URL: https://doi.org/10.1083/jcb.200806088, doi:10.1083/jcb.200806088. This article has 69 citations.
(lakdawala2022identifyingandcharacterizing pages 33-39): MF Lakdawala. Identifying and characterizing regulators of a bone morphogenetic protein cell signaling pathway in caenorhabditis elegans. Unknown journal, 2022.
(joseph2020controlofclathrinmediated pages 3-5): Braveen B. Joseph, Yu Wang, Phil Edeen, Vladimir Lažetić, Barth D. Grant, and David S. Fay. Control of clathrin-mediated endocytosis by nima family kinases. Feb 2020. URL: https://doi.org/10.1371/journal.pgen.1008633, doi:10.1371/journal.pgen.1008633. This article has 49 citations and is from a domain leading peer-reviewed journal.
(knop2024caenorhabditiseleganssel5aak1 pages 6-7): Filip Knop, Apolena Zounarová, Vojtěch Šabata, Teije Corneel Middelkoop, and Marie Macůrková. Caenorhabditis elegans sel-5/aak1 regulates cell migration and cell outgrowth independently of its kinase activity. Jul 2024. URL: https://doi.org/10.7554/elife.91054, doi:10.7554/elife.91054. This article has 8 citations and is from a domain leading peer-reviewed journal.
(knop2024caenorhabditiseleganssel5aak1 pages 7-8): Filip Knop, Apolena Zounarová, Vojtěch Šabata, Teije Corneel Middelkoop, and Marie Macůrková. Caenorhabditis elegans sel-5/aak1 regulates cell migration and cell outgrowth independently of its kinase activity. Jul 2024. URL: https://doi.org/10.7554/elife.91054, doi:10.7554/elife.91054. This article has 8 citations and is from a domain leading peer-reviewed journal.
(knop2024caenorhabditiseleganssel5aak1 pages 15-16): Filip Knop, Apolena Zounarová, Vojtěch Šabata, Teije Corneel Middelkoop, and Marie Macůrková. Caenorhabditis elegans sel-5/aak1 regulates cell migration and cell outgrowth independently of its kinase activity. Jul 2024. URL: https://doi.org/10.7554/elife.91054, doi:10.7554/elife.91054. This article has 8 citations and is from a domain leading peer-reviewed journal.
(knop2024caenorhabditiseleganssel5aak1 pages 1-2): Filip Knop, Apolena Zounarová, Vojtěch Šabata, Teije Corneel Middelkoop, and Marie Macůrková. Caenorhabditis elegans sel-5/aak1 regulates cell migration and cell outgrowth independently of its kinase activity. Jul 2024. URL: https://doi.org/10.7554/elife.91054, doi:10.7554/elife.91054. This article has 8 citations and is from a domain leading peer-reviewed journal.