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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 identity is verified: Caenorhabditis elegans apa-2 encodes APA-2, the α-adaptin/large α subunit of the heterotetrameric AP-2 clathrin adaptor complex. This matches UniProt Q22601, ORF T20B5.1, and the supplied large-adaptin, AP2-α, ARM-like, and clathrin/coatomer-adaptin domain annotations. The literature examined does not indicate confusion with a different similarly named gene. Direct worm studies use multiple apa-2 null or severe-loss alleles and rescuing APA-2::GFP constructs, making the identification highly secure. (gu2013ap2hemicomplexescontribute pages 2-4, gu2013ap2hemicomplexescontribute pages 15-16)
APA-2 is not an enzyme or transporter. Its primary function is structural and organizational: as the large subunit of the α–σ2 half of AP-2, it helps couple membrane-associated cargo and accessory proteins to clathrin-mediated membrane-remodeling machinery. Its best-supported sites of action are the cytoplasmic face of the plasma membrane, synaptic endocytic zones, intestinal basolateral membrane, coelomocyte membrane, and corpse-containing phagosomes. Its most precisely demonstrated functions are cargo endocytosis, synaptic-vesicle recycling, and CED-1-dependent apoptotic-cell clearance. (gu2013ap2hemicomplexescontribute pages 8-10, gu2013ap2hemicomplexescontribute pages 6-8, chen2013clathrinandap2 pages 3-4)
Primary genetic literature explicitly identifies apa-2 as the gene for AP-2 α-adaptin. Particularly strong alleles include b1044, a 925-bp deletion removing residues 93–318 of the trunk; ox422, a premature stop at Lys215; and ox421, which deletes the complete open reading frame. A functional APA-2::GFP transgene rescues mutant phenotypes, linking the cloned locus, tagged protein, and biological activity. (gu2013ap2hemicomplexescontribute pages 2-4, gu2013ap2hemicomplexescontribute pages 15-16)
The supplied UniProt architecture is fully consistent with this assignment. Large adaptin subunits have an extended α-solenoid/ARM-like trunk forming the AP-2 core, followed by flexible hinge and appendage or “ear” regions that organize coat-associated factors. The direct worm evidence establishes the trunk’s importance because both b1044 and ox422 disrupt it. Precise residue-level functions of all Q22601 domains have not, however, been determined experimentally in the worm; the detailed ARM-repeat and appendage interpretation is therefore family/structural inference rather than an APA-2-specific atomic structure. (gu2013ap2hemicomplexescontribute pages 2-4)
AP-2 contains α/APA-2, β, μ2/APM-2, and σ2/APS-2 subunits. Worm genetics revealed that it is not simply an indivisible heterotetramer: α–σ2 and μ2–β can retain partial function as “hemicomplexes.” In μ2-deficient animals, α-adaptin and σ2 remain membrane or synapse associated, although α abundance falls to approximately 60% by immunoblot or 40% by fluorescence. Conversely, loss of APA-2 destabilizes σ2 while μ2 and β remain comparatively stable. This provides strong in-vivo evidence that APA-2 is the principal large structural component of the α–σ2 hemicomplex. (gu2013ap2hemicomplexescontribute pages 6-8, gu2008μ2adaptinfacilitates pages 6-6)
The two halves are partially redundant but cargo-selective. Simultaneous α- and μ2-adaptin loss caused 95.70 ± 4.30% embryonic lethality and reduced brood size to 3.4 ± 3.1 progeny, versus 247.3 ± 8.8 in wild type. Thus, single-subunit viability should not be interpreted as AP-2 dispensability; residual hemicomplex activity masks the full requirement. (gu2013ap2hemicomplexescontribute pages 4-6)
APA-2’s clearest cargo-sorting role involves dileucine-signal-dependent internalization. An intestinal eGFP–CD4 reporter carrying an ExxxLL signal accumulated at the basolateral membrane in apa-2(ox422) animals, with fluorescence of 14,907 ± 990 versus 1,998 ± 275 in wild type (p<0.0001). The stronger α-subunit phenotype relative to μ2 loss supports preferential recognition or handling of this cargo class by the α–σ2 arm. By contrast, MIG-14/Wntless trafficking depends more strongly on μ2, demonstrating that the two halves are not functionally interchangeable. (gu2013ap2hemicomplexescontribute pages 4-6, gu2013ap2hemicomplexescontribute pages 6-8)
A rescuing APA-2::GFP reporter is broadly expressed, with particularly evident expression in the nervous system, intestine, and hypodermis. In GABAergic neurons, APA-2 colocalizes with synaptobrevin at synaptic varicosities in the dorsal and ventral nerve cords. It is also found at the coelomocyte plasma membrane and at intestinal membranes, consistent with a cytoplasmic, membrane-recruited endocytic adaptor rather than a secreted, luminal, or integral-membrane protein. (gu2013ap2hemicomplexescontribute pages 8-10, gu2013ap2hemicomplexescontribute pages 2-4, gu2013ap2hemicomplexescontribute pages 6-8)
APA-2 additionally associates with germ-cell-corpse phagosomes. Phagosomal APA-2::GFP labeling is reduced after depletion of clathrin heavy chain CHC-1, while apa-2 or β-subunit depletion suppresses phagosomal CHC-1 labeling. This reciprocal dependence supports assembly or stabilization of an AP-2–clathrin coat on phagosomal membranes. (chen2013clathrinandap2 pages 3-4, chen2013clathrinandap2 pages 17-17)
Localization should be understood as dynamic. At the complex level, AP-2 cycles between a closed cytosolic state and an open membrane-associated state that exposes membrane- and cargo-binding surfaces. FCHO-1 promotes opening and stable clustering: in fcho-1 mutants, AP-2 remains membrane-associated but its membrane dwell time decreases from about 35 seconds to under 10 seconds. This is strong AP-2-complex evidence, although it does not establish an APA-2-only biochemical activity. (hollopeter2014themembraneassociatedproteins pages 11-12)
APA-2 participates in recovery of synaptic-vesicle membrane and proteins after neurotransmitter release. Neuronal APA-2 loss reduced synaptic vesicle numbers to 71% of wild type in cholinergic neurons and 59% in GABAergic neurons; nervous-system expression of APA-2 restored the defect. When both α and μ2 activities were removed, vesicle abundance fell to 28% and 31%, respectively, and large vacuoles or abnormal vesicular profiles accumulated. These findings support AP-2-dependent retrieval at the plasma membrane and likely an additional role in regenerating synaptic vesicles from endosomal intermediates. (gu2013ap2hemicomplexescontribute pages 8-10, gu2013ap2hemicomplexescontribute pages 15-16)
Synaptotagmin, UNC-47, and synaptogyrin remain substantially synaptically localized even in α/μ2-deficient animals, implying that other adaptors or AP-2-independent routes can retrieve some vesicle proteins. Therefore, APA-2 is important but not the only synaptic endocytic adaptor in the worm. (gu2013ap2hemicomplexescontribute pages 8-10)
Besides artificial dileucine cargo, AP-2 influences endogenous MIG-14/Wntless and GLR-1 glutamate-receptor trafficking. Mutations in APA-2/α, APM-2/μ2, or APS-2/σ2 reduce GLR-1 abundance at ventral-nerve-cord synapses. The GLR-1 study proposed an unexpected AP-2-dependent step early in the secretory pathway rather than a simple defect in surface internalization. Because the available experiments concern several AP-2 subunits and do not show direct APA-2–GLR-1 binding, this role should be assigned to the complex rather than uniquely to APA-2. (garafalo2015theap2clathrin pages 1-4)
APA-2 has a directly demonstrated role in phagocytic receptor signaling. The intracellular region of CED-1 binds APA-2 in vitro, whereas the other tested AP-2 subunits did not detectably bind CED-1. APA-2::GFP localizes to corpse-containing phagosomes, and the tagged transgene rescues corpse accumulation following apa-2 depletion. These results make APA-2 a physical bridge between CED-1 and the larger AP-2/clathrin machinery. (chen2013clathrinandap2 pages 3-4)
At the complex level, AP-2 and clathrin facilitate both corpse engulfment and phagosome maturation. They act with CED-6/Gulp in actin remodeling and promote recruitment of LST-4/Snx9-family and DYN-1/dynamin machinery. In clathrin or AP-2 β-subunit depletion experiments, 48–56% of corpses were not fully internalized, corpse persistence exceeded 120 minutes, and actin recruitment to CED-1- or CED-6-positive phagosomes fell from 77–85% to 35–41%. These numerical phenotypes demonstrate pathway importance, but they are whole-complex measurements and should not all be attributed solely to APA-2. (chen2013clathrinandap2 pages 3-4, chen2013clathrinandap2 pages 2-3, chen2013clathrinandap2 pages 1-2)
FCHO-1 is an upstream AP-2 activator. Its conserved approximately 90-residue activator segment binds the AP-2 core and stabilizes the open state, exposing membrane- and cargo-binding sites and enabling productive clathrin-coated-pit assembly. FCHO-1’s relevant contact was mapped to the AP-2 core rather than exclusively to the α appendage. (hollopeter2014themembraneassociatedproteins pages 11-12)
NCAP-1, the worm NECAP ortholog, acts oppositely. Loss of NCAP-1 bypasses the need for FCHO-1 and causes open, phosphorylated AP-2 to accumulate. NECAP preferentially recognizes open/phosphorylated AP-2 and is interpreted as promoting adaptor inactivation or recycling late in endocytosis. APA-2::GFP was used to monitor complex localization and dynamics, but the regulatory mechanism applies to AP-2 as a conformational unit rather than proving that APA-2 alone is the regulated substrate. (beacham2018necapsarenegative pages 11-15)
The highest-confidence APA-2-specific partners or associations are therefore σ2/APS-2 within the hemicomplex, CED-1 through direct intracellular-domain binding, and clathrin-associated membranes through reciprocal recruitment at phagosomes. Associations with FCHO-1, NCAP-1, phosphoinositides, and cargo-recognition machinery are best described at AP-2-complex level unless a direct APA-2 interaction was separately demonstrated. (gu2013ap2hemicomplexescontribute pages 6-8, chen2013clathrinandap2 pages 3-4, beacham2018necapsarenegative pages 11-15)
Single apa-2 mutants are viable but show jowls, variable dumpiness, egg-laying defects, mild uncoordination, and impaired thrashing. Tissue-specific rescue demonstrates that these are not merely nonspecific sickness phenotypes: neuronal expression rescues relevant body-length/locomotor effects, while hypodermal expression rescues cuticle-associated defects. Without compensating tissue rescue, synaptic-vesicle depletion can be more severe—56% of wild type in cholinergic neurons and 29% in GABAergic neurons. (gu2013ap2hemicomplexescontribute pages 8-10, gu2013ap2hemicomplexescontribute pages 2-4)
These pleiotropic effects are secondary to the core membrane-trafficking role. The mechanistically most informative phenotypes are cargo retention at the membrane, reduced synaptic-vesicle numbers, destabilization of σ2, synthetic lethality with μ2 loss, and impaired phagosome formation/maturation.
A targeted search prioritizing 2023–2024 did not identify a new peer-reviewed study that revises the molecular annotation of APA-2 itself. The decisive gene-specific mechanistic literature remains concentrated in 2013–2018. Recent endocytosis research continues to support the broader framework in which AP-2 is the major clathrin-associated cargo adaptor, but it does not supersede the worm-specific genetic, localization, and interaction evidence summarized here.
This absence of recent gene-specific papers is biologically informative rather than a reason to substitute literature on a different “APA-2.” The correct annotation should remain conservative: APA-2 is a validated AP-2 α-adaptin with direct roles in cargo endocytosis, synaptic-vesicle recycling, and CED-1-dependent corpse clearance; claims about atomic structure, lipid specificity, phosphorylation, or conformational cycling should generally be labeled as AP-2-family or complex-level inference.
The most important real-world use of apa-2 is as an experimental genetic handle on conserved clathrin-mediated endocytosis. Viable α-subunit null animals permit separation of α–σ2 from μ2–β functions, tissue-specific rescue permits assignment of neuronal versus epithelial requirements, and APA-2::GFP enables live analysis of membrane recruitment and coat regulation. The system has been used to study synaptic-vesicle recycling, cargo-signal specificity, glutamate-receptor trafficking, FCHO/NECAP conformational control, and efferocytosis. (gu2013ap2hemicomplexescontribute pages 8-10, garafalo2015theap2clathrin pages 1-4, hollopeter2014themembraneassociatedproteins pages 11-12, chen2013clathrinandap2 pages 3-4, beacham2018necapsarenegative pages 11-15)
The strongest expert interpretation from the primary studies is that AP-2 is neither a rigid obligate tetramer nor the only endocytic route. Instead, APA-2 helps form a partially autonomous α–σ2 module with preferential cargo functions, while the complete tetramer provides maximal efficiency and organismal viability. This model explains why apa-2 single mutants survive but α/μ2 double loss is nearly lethal and produces severe synaptic defects. (gu2013ap2hemicomplexescontribute pages 4-6, gu2013ap2hemicomplexescontribute pages 6-8)
The evidence hierarchy is summarized below.
| Functional claim | Direct evidence / quantitative result | Evidence level | Confidence | Primary source / date |
|---|---|---|---|---|
Identity: apa-2 encodes AP-2 α-adaptin (Q22601) |
C. elegans genetic studies explicitly identify apa-2 as the α-subunit gene. Likely-null alleles include b1044 (925-bp deletion removing residues 93–318), ox422 (premature stop at Lys215), and ox421 (entire ORF deleted). A functional APA-2::GFP transgene rescues mutant phenotypes. (gu2013ap2hemicomplexescontribute pages 2-4, gu2013ap2hemicomplexescontribute pages 15-16) |
APA-2-specific | High | Gu et al., eLife, March 2013; https://doi.org/10.7554/eLife.00190 |
| Structural role in an α–σ2 AP-2 hemicomplex | AP-2 comprises α, β, μ2, and σ2 subunits. In μ2-deficient worms, α-adaptin and σ2 remain localized, although α abundance falls to approximately 60% by immunoblot or 40% by fluorescence. Loss of α destabilizes σ2 while μ2 and β remain comparatively stable, supporting separable α–σ2 and μ2–β hemicomplexes. (gu2013ap2hemicomplexescontribute pages 4-6, gu2013ap2hemicomplexescontribute pages 6-8, gu2008μ2adaptinfacilitates pages 6-6) | APA-2-specific genetics and AP-2-complex interpretation | High | Gu et al., J. Cell Biol., December 2008; https://doi.org/10.1083/jcb.200806088; Gu et al., eLife, March 2013; https://doi.org/10.7554/eLife.00190 |
| Plasma-membrane, synaptic, intestinal, and phagosomal localization | Functional APA-2::GFP is broadly expressed, especially in nervous system, intestine, and hypodermis. In GABA neurons it colocalizes with synaptobrevin at nerve-cord synaptic varicosities; α-adaptin also localizes to the coelomocyte plasma membrane. APA-2::GFP associates with germ-cell-corpse phagosomes, and this labeling is reduced by chc-1 RNAi. (gu2013ap2hemicomplexescontribute pages 8-10, gu2013ap2hemicomplexescontribute pages 2-4, gu2013ap2hemicomplexescontribute pages 6-8, chen2013clathrinandap2 pages 3-4, chen2013clathrinandap2 pages 17-17) |
APA-2-specific tagged-protein localization | High | Gu et al., eLife, March 2013; https://doi.org/10.7554/eLife.00190; Chen et al., PLoS Genetics, May 2013; https://doi.org/10.1371/journal.pgen.1003517 |
| Endocytosis of dileucine-motif cargo | An eGFP–CD4 reporter carrying an ExxxLL motif accumulates on intestinal basolateral membranes in apa-2(ox422): fluorescence 14,907 ± 990, versus 1,998 ± 275 in wild type (p<0.0001). The stronger defect relative to μ2 loss supports a cargo-selective contribution from the α–σ2 hemicomplex. (gu2013ap2hemicomplexescontribute pages 4-6, gu2013ap2hemicomplexescontribute pages 6-8) |
APA-2-specific genetic cargo assay | High | Gu et al., eLife, March 2013; https://doi.org/10.7554/eLife.00190 |
| Synaptic-vesicle recycling | Neuronal APA-2 loss reduces synaptic vesicles to 71% of wild type in acetylcholine neurons and 59% in GABA neurons; neuron-specific APA-2 expression rescues the defect. Simultaneous α/μ2 loss reduces vesicles to 28% and 31%, respectively, and produces large vesicles/vacuoles, demonstrating partially independent hemicomplex activity. (gu2013ap2hemicomplexescontribute pages 8-10, gu2013ap2hemicomplexescontribute pages 15-16) | APA-2-specific genetics, rescue, and electron microscopy | High | Gu et al., eLife, March 2013; https://doi.org/10.7554/eLife.00190 |
| CED-1 binding and apoptotic-cell clearance | The intracellular region of the engulfment receptor CED-1 binds APA-2 directly in vitro, whereas other tested AP-2 subunits did not. APA-2::GFP localizes to corpse-containing phagosomes and rescues corpse accumulation caused by apa-2 RNAi. AP-2/clathrin depletion impairs corpse internalization and phagosome maturation; complex-level measurements include >120-min corpse persistence and reduced actin recruitment from 77–85% to 35–41%. (chen2013clathrinandap2 pages 3-4, chen2013clathrinandap2 pages 2-3, chen2013clathrinandap2 pages 1-2) |
Direct APA-2 binding/localization plus AP-2-complex functional evidence | High for interaction and localization; moderate for assigning all complex phenotypes specifically to APA-2 | Chen et al., PLoS Genetics, May 2013; https://doi.org/10.1371/journal.pgen.1003517 |
| FCHO-1 activates AP-2 | In fcho-1 mutants, AP-2 remains membrane-associated but fails to cluster; membrane dwell time falls from approximately 35 s to <10 s. FCHO-1 directly binds the AP-2 core through a conserved 90-residue activator region and promotes the open state that exposes membrane- and cargo-binding sites. These experiments concern AP-2 as a complex rather than a unique catalytic activity of APA-2. (hollopeter2014themembraneassociatedproteins pages 11-12) |
AP-2-complex regulation | High for AP-2; moderate when attributed specifically to APA-2 | Hollopeter et al., eLife, October 2014; https://doi.org/10.7554/eLife.03648 |
| NCAP-1/NECAP negatively regulates AP-2 | Loss of the sole worm NECAP, NCAP-1, bypasses the requirement for FCHO-1 and causes open, phosphorylated AP-2 to accumulate. NECAP preferentially recognizes open/phosphorylated AP-2 and promotes return toward an inactive state; APA-2::GFP was used in coelomocyte localization and FRAP analyses, but the available excerpt supplies no APA-2-specific numerical result. (beacham2018necapsarenegative pages 11-15) | AP-2-complex regulation; APA-2 used as reporter | High for complex-level regulation; moderate for APA-2-specific interpretation | Beacham et al., eLife, September 2018; preprint URL https://doi.org/10.1101/192898 |
| GLR-1 glutamate-receptor trafficking | Null mutations affecting APA-2/α, APM-2/μ2, or APS-2/σ2 reduce GLR-1 abundance at ventral-nerve-cord synapses. The study proposed an unexpected AP-2-dependent trafficking step early in the secretory pathway, but the available evidence does not provide an APA-2-specific effect size or direct APA-2–GLR-1 binding. (garafalo2015theap2clathrin pages 1-4) | APA-2 genetic association within an AP-2-complex phenotype | Moderate | Garafalo et al., Molecular Biology of the Cell, May 2015; https://doi.org/10.1091/mbc.e14-06-1048 |
Table: Evidence matrix distinguishing direct APA-2 findings from AP-2-complex-level interpretations for C. elegans apa-2/Q22601. Quantitative genetic, localization, cargo-trafficking, regulatory, and pathway evidence is linked to primary sources.
Recommended functional description: “AP-2 complex α subunit; large cytosolic adaptin that forms the α–σ2 hemicomplex and, within AP-2, recruits and organizes cargo- and clathrin-associated machinery at the cytoplasmic face of plasma and phagosomal membranes. Required for efficient dileucine-cargo internalization, synaptic-vesicle recycling, selected receptor trafficking, and CED-1-dependent apoptotic-cell engulfment/phagosome maturation.”
Primary location: cytoplasmic peripheral membrane protein recruited to plasma-membrane endocytic sites, neuronal synapses, intestinal basolateral membranes, coelomocyte membranes, and corpse-containing phagosomes.
Evidence confidence: high for identity, α–σ2 structural role, membrane/synaptic/phagosomal localization, dileucine-cargo endocytosis, synaptic-vesicle recycling, and CED-1 binding; moderate for APA-2-specific assignment of functions demonstrated only after perturbing AP-2 as a whole; inferential for detailed domain mechanics not solved directly for Q22601.
References
(gu2013ap2hemicomplexescontribute pages 2-4): Mingyu Gu, Qiang Liu, Shigeki Watanabe, Lin Sun, Gunther Hollopeter, Barth D Grant, and Erik M Jorgensen. Ap2 hemicomplexes contribute independently to synaptic vesicle endocytosis. eLife, Mar 2013. URL: https://doi.org/10.7554/elife.00190, doi:10.7554/elife.00190. This article has 103 citations and is from a domain leading peer-reviewed journal.
(gu2013ap2hemicomplexescontribute pages 15-16): Mingyu Gu, Qiang Liu, Shigeki Watanabe, Lin Sun, Gunther Hollopeter, Barth D Grant, and Erik M Jorgensen. Ap2 hemicomplexes contribute independently to synaptic vesicle endocytosis. eLife, Mar 2013. URL: https://doi.org/10.7554/elife.00190, doi:10.7554/elife.00190. This article has 103 citations and is from a domain leading peer-reviewed journal.
(gu2013ap2hemicomplexescontribute pages 8-10): Mingyu Gu, Qiang Liu, Shigeki Watanabe, Lin Sun, Gunther Hollopeter, Barth D Grant, and Erik M Jorgensen. Ap2 hemicomplexes contribute independently to synaptic vesicle endocytosis. eLife, Mar 2013. URL: https://doi.org/10.7554/elife.00190, doi:10.7554/elife.00190. This article has 103 citations and is from a domain leading peer-reviewed journal.
(gu2013ap2hemicomplexescontribute pages 6-8): Mingyu Gu, Qiang Liu, Shigeki Watanabe, Lin Sun, Gunther Hollopeter, Barth D Grant, and Erik M Jorgensen. Ap2 hemicomplexes contribute independently to synaptic vesicle endocytosis. eLife, Mar 2013. URL: https://doi.org/10.7554/elife.00190, doi:10.7554/elife.00190. This article has 103 citations and is from a domain leading peer-reviewed journal.
(chen2013clathrinandap2 pages 3-4): Didi Chen, Youli Jian, Xuezhao Liu, Yuanya Zhang, Jingjing Liang, Xiaying Qi, Hongwei Du, Wei Zou, Lianwan Chen, Yongping Chai, Guangshuo Ou, Long Miao, Yingchun Wang, and Chonglin Yang. Clathrin and ap2 are required for phagocytic receptor-mediated apoptotic cell clearance in caenorhabditis elegans. PLoS Genetics, 9:e1003517, May 2013. URL: https://doi.org/10.1371/journal.pgen.1003517, doi:10.1371/journal.pgen.1003517. This article has 65 citations and is from a domain leading peer-reviewed journal.
(gu2008μ2adaptinfacilitates pages 6-6): 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.
(gu2013ap2hemicomplexescontribute pages 4-6): Mingyu Gu, Qiang Liu, Shigeki Watanabe, Lin Sun, Gunther Hollopeter, Barth D Grant, and Erik M Jorgensen. Ap2 hemicomplexes contribute independently to synaptic vesicle endocytosis. eLife, Mar 2013. URL: https://doi.org/10.7554/elife.00190, doi:10.7554/elife.00190. This article has 103 citations and is from a domain leading peer-reviewed journal.
(chen2013clathrinandap2 pages 17-17): Didi Chen, Youli Jian, Xuezhao Liu, Yuanya Zhang, Jingjing Liang, Xiaying Qi, Hongwei Du, Wei Zou, Lianwan Chen, Yongping Chai, Guangshuo Ou, Long Miao, Yingchun Wang, and Chonglin Yang. Clathrin and ap2 are required for phagocytic receptor-mediated apoptotic cell clearance in caenorhabditis elegans. PLoS Genetics, 9:e1003517, May 2013. URL: https://doi.org/10.1371/journal.pgen.1003517, doi:10.1371/journal.pgen.1003517. This article has 65 citations and is from a domain leading peer-reviewed journal.
(hollopeter2014themembraneassociatedproteins pages 11-12): Gunther Hollopeter, Jeffrey J Lange, Ying Zhang, Thien N Vu, Mingyu Gu, Michael Ailion, Eric J Lambie, Brian D Slaughter, Jay R Unruh, Laurence Florens, and Erik M Jorgensen. The membrane-associated proteins fcho and sgip are allosteric activators of the ap2 clathrin adaptor complex. eLife, Oct 2014. URL: https://doi.org/10.7554/elife.03648, doi:10.7554/elife.03648. This article has 120 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.
(chen2013clathrinandap2 pages 2-3): Didi Chen, Youli Jian, Xuezhao Liu, Yuanya Zhang, Jingjing Liang, Xiaying Qi, Hongwei Du, Wei Zou, Lianwan Chen, Yongping Chai, Guangshuo Ou, Long Miao, Yingchun Wang, and Chonglin Yang. Clathrin and ap2 are required for phagocytic receptor-mediated apoptotic cell clearance in caenorhabditis elegans. PLoS Genetics, 9:e1003517, May 2013. URL: https://doi.org/10.1371/journal.pgen.1003517, doi:10.1371/journal.pgen.1003517. This article has 65 citations and is from a domain leading peer-reviewed journal.
(chen2013clathrinandap2 pages 1-2): Didi Chen, Youli Jian, Xuezhao Liu, Yuanya Zhang, Jingjing Liang, Xiaying Qi, Hongwei Du, Wei Zou, Lianwan Chen, Yongping Chai, Guangshuo Ou, Long Miao, Yingchun Wang, and Chonglin Yang. Clathrin and ap2 are required for phagocytic receptor-mediated apoptotic cell clearance in caenorhabditis elegans. PLoS Genetics, 9:e1003517, May 2013. URL: https://doi.org/10.1371/journal.pgen.1003517, doi:10.1371/journal.pgen.1003517. This article has 65 citations and is from a domain leading peer-reviewed journal.
(beacham2018necapsarenegative pages 11-15): Gwendolyn M Beacham, Edward A Partlow, Jeffrey J Lange, and Gunther Hollopeter. Necaps are negative regulators of the ap2 clathrin adaptor complex. eLife, Sep 2018. URL: https://doi.org/10.1101/192898, doi:10.1101/192898. This article has 40 citations and is from a domain leading peer-reviewed journal.