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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target is the Drosophila melanogaster Ank2 locus, also designated CG42734, and not human ANK2/ankyrin-B. The literature supports annotation of fly Ank2 as a nonenzymatic, intracellular cytoskeletal adaptor and membrane-domain organizer, expressed predominantly in neurons. Its principal function is to connect neuronal membrane proteins—especially L1-family cell-adhesion molecules—with the spectrin-associated cytoskeleton and organized microtubule networks. Through giant isoforms, Ank2 stabilizes axons and presynaptic terminals, organizes neuromuscular-junction morphology, supports axonal transport, and establishes an axon-initial-segment-like proximal membrane domain. Recent work extends these functions to adult-brain axon and dendrite morphogenesis and long-term memory (schwartz2023ankyrin2isessential pages 4-6, schwartz2023ankyrin2isessential pages 1-2, pielage2008apresynapticgiant pages 1-2).
A critical limitation is that most experimental papers investigate the Ank2 locus or named isoforms, not the individual UniProt sequence record Q3KN55/RE55168p. Consequently, locus-level functions are strongly supported, but they should not all be assigned specifically to the Q3KN55 translation without transcript/protein mapping.
The supplied record identifies Q3KN55 as RE55168p from D. melanogaster, encoded by Ank2/CG42734. This agrees with the fly literature: Drosophila has a neuron-specific Ank2 locus distinct from its other ankyrin gene, and the relevant studies explicitly concern neuronal Ank2 in fly axons, brain, and neuromuscular junctions (NMJs) (pielage2008apresynapticgiant pages 1-2, spurrier2019expressionofa pages 1-3).
The symbol Ank2 is evolutionarily and taxonomically ambiguous. It must not be interpreted automatically as human ANK2, which encodes ankyrin-B. Drosophila giant Ank2 proteins share structural and functional features with giant vertebrate ankyrins, particularly ANK3/ankyrin-G. One recent fly paper reported 57% whole-protein similarity and 71.2% ankyrin-repeat identity to human ANK3, while AIS studies describe fly Ank2-L as an analog—and potentially an evolutionary ortholog—of giant AnkG rather than simply human ankyrin-B (schwartz2023ankyrin2isessential pages 1-2, spurrier2019expressionofa pages 1-3). Findings about human cardiac ANK2 therefore cannot be transferred directly to Q3KN55.
The supplied InterPro/Pfam calls—Ankyrin_rpt, Ank, Ank_2, and Ank_4—are fully consistent with the literature. Canonical Ank2 architecture includes an N-terminal membrane-binding region containing 24 ankyrin repeats, a central spectrin-binding region, a death domain, and variable C-terminal regulatory/extended sequences. The 24 repeats are approximately 33 residues each and can be divided experimentally into four six-repeat blocks, AnkD1–AnkD4 (schwartz2023ankyrin2isessential pages 1-2, weber2019theankyrinrepeat pages 2-4, weber2019theankyrinrepeat pages 1-2).
| Functional feature | Mechanistic interpretation | Key experimental evidence | Evidence strength / limitations | Key source / year |
|---|---|---|---|---|
| Identity and symbol ambiguity | The target is neuron-enriched Drosophila melanogaster Ank2/CG42734, associated with UniProt Q3KN55—not human ANK2/ankyrin-B. Fly Ank2 giant isoforms are structurally and functionally closer to giant ankyrins such as mammalian AnkG/ANK3; one comparison found 57% whole-protein and 71.2% ankyrin-repeat identity to human ANK3. | Fly studies distinguish neuron-specific Ank2 from the separate, more broadly expressed Drosophila ankyrin gene. Adult-brain and NMJ experiments explicitly study Drosophila Ank2. | High for locus identity and organism. Most experiments concern the Ank2 locus or named isoforms, not the specific RE55168p/Q3KN55 translation; accession-specific function should therefore not be overclaimed. | Schwartz et al., 2023; Pielage et al., 2008; Spurrier et al., 2019 (schwartz2023ankyrin2isessential pages 1-2, pielage2008apresynapticgiant pages 1-2, spurrier2019expressionofa pages 1-3) |
| Domain and isoform architecture | Ank2 is a nonenzymatic cytoskeletal adaptor. Its canonical architecture comprises an N-terminal membrane-binding region with 24 ankyrin repeats, a central spectrin-binding region, and variable C-terminal sequences. Giant isoforms add extended regions that support microtubule organization and spatial scaffolding. | The locus produces short and giant neuronal isoforms. Ank2-L is approximately 450 kDa/4,083 residues; Ank2-XL extends to approximately 11,640 residues, with common sequence to about residue 2,399. Ank2-XL includes a large repeat-rich spacer and C-terminal microtubule-related region. | High for locus-level architecture; moderate for mapping every feature to Q3KN55. Isoform nomenclature varies among studies—Ank2-S/M/L versus Ank2a/L/XL—so transcript equivalence requires database-level reconciliation. | Stephan et al., 2015; Weber et al., 2019; Schwartz et al., 2023 (schwartz2023ankyrin2isessential pages 1-2, stephan2015hierarchicalmicrotubuleorganization pages 3-4, weber2019theankyrinrepeat pages 2-4) |
| Axonal and NMJ localization | Giant Ank2 isoforms form a submembranous neuronal scaffold in axons and presynaptic terminals, linking membrane proteins and adhesion systems to spectrin and microtubules. | Ank2-L forms a lattice-like structure beneath the presynaptic membrane at larval NMJs. Adult-brain staining is widespread along axon tracts and colocalizes with neuronal Futsch but not the glial marker Repo; Ank2-L is present in mushroom-body α, β, and γ lobes and around the calyx. | High. Supported by isoform-directed immunohistochemistry and mutant analyses in larvae and adults. Exact localization of the Q3KN55/RE55168p product itself was not separately established. | Pielage et al., 2008; Schwartz et al., 2023 (schwartz2023ankyrin2isessential pages 4-6, pielage2008apresynapticgiant pages 1-2) |
| Neuroglian and cell-adhesion linkage | The ankyrin-repeat domain couples Neuroglian (Nrg)—the fly L1CAM homolog—and other synaptic adhesion molecules to the presynaptic cytoskeleton, stabilizing transsynaptic architecture. | Nrg and Ank2-L codistribute in the adult mushroom body. Nrg’s intracellular FIGQY motif mediates ankyrin association. Deleting selected Ank2 ankyrin-repeat subdomains disrupts synaptic Ank2-L targeting, CAM organization, and synaptic stability; the AnkD3 region containing repeats 13–18 is especially important. | High for functional linkage and ARD dependence; moderate for direct binding by each fly Ank2 subdomain. Some interaction assignments use conserved L1CAM–ankyrin binding logic together with localization and rescue phenotypes. | Weber et al., 2019; Schwartz et al., 2023; Pielage et al., 2008 (schwartz2023ankyrin2isessential pages 4-6, pielage2008apresynapticgiant pages 1-2, weber2019theankyrinrepeat pages 11-12, weber2019theankyrinrepeat pages 1-2) |
| Microtubule and Futsch/MAP1B organization | Ank2-L and Ank2-XL hierarchically organize presynaptic microtubules. Ank2-L supports terminal microtubule retention and synaptic stability, whereas Ank2-XL provides higher-order spacing and bouton organization; Futsch/MAP1B participates in this scaffold. | Loss of Ank2-L removes Futsch from terminal boutons and produces central microtubule aggregates. More than 90% of Ank2-XL-mutant NMJs exhibit large Futsch/microtubule aggregates, although terminal microtubules remain. Futsch co-precipitated with Ank2-XL in controls but not Ank2-XL deletion mutants; removing Futsch suppressed microtubule accumulation and restored bouton separation. Combined loss reduced microtubule spacing, membrane association, axon caliber, anterograde transport, release-site number, and neurotransmission without changing microtubule number per axonal cross-section. | High. Supported by genetics, imaging, ultrastructure, co-precipitation, transport assays, and interaction/suppression experiments. Direct physical microtubule binding is best established for extended C-terminal Ank2 regions rather than every isoform or repeat segment. | Pielage et al., 2008; Stephan et al., 2015 (stephan2015hierarchicalmicrotubuleorganization pages 12-14, pielage2008apresynapticgiant pages 1-2, stephan2015hierarchicalmicrotubuleorganization pages 3-4) |
| Ank2-L/Ank2-XL interdependence | Presynaptic scaffold assembly is hierarchical: Ank2-L is required to recruit or stabilize Ank2-XL, while Ank2-XL has a smaller reciprocal effect on Ank2-L. | Loss of Ank2-L severely reduces or disrupts presynaptic Ank2-XL. Loss of Ank2-XL abolishes XL staining but only slightly reduces Ank2-L without eliminating its presynaptic distribution. ARD deletion experiments further show reciprocal localization effects and identify AnkD2–AnkD4 as important for presynaptic Ank2-L targeting. | High. Genetic rescue and isoform-specific staining demonstrate asymmetric dependence. The molecular basis—direct heteromeric binding versus indirect scaffold dependence—remains unresolved. | Weber et al., 2019 (weber2019theankyrinrepeat pages 2-4, weber2019theankyrinrepeat pages 11-12, weber2019theankyrinrepeat pages 1-2) |
| Proximal-axon diffusion barrier and Shal localization | Giant Ank2 establishes an axon-initial-segment-like proximal domain that restricts membrane diffusion and patterns ion-channel localization. | FRAP showed significantly increased axonal diffusion in mutants disrupting L-exon-containing Ank2 isoforms (p < 0.02; 19 mutant axonal cells and 9 dendritic cells). GFP-Shal normally peaks about 10–50 μm from the soma; Ank2 trans-heterozygotes lost this peak, with Shal highest beside the soma and declining distally. Expressing an Ank2-L C-terminal fragment shortened the AIS-like region and caused axonal degeneration and neuron loss. | High for an Ank2-dependent proximal-axon scaffold; moderate for isoform assignment. Disrupting L isoforms also perturbs XL expression/localization, so L versus XL requirements could not be separated. The Drosophila structure is AIS-like and should not be assumed identical to the vertebrate AIS. | Jegla et al., 2016; Spurrier et al., 2019 (spurrier2019expressionofa pages 1-3, jegla2016bilateriangiantankyrins pages 19-22) |
| Adult neuronal morphogenesis | Ank2 supports axon growth/guidance and dendritic arbor maintenance beyond the larval NMJ, probably by stabilizing adhesion–cytoskeleton assemblies. | Pan-neuronal RNAi produced thin, missing, prematurely terminated, fused, or misoriented mushroom-body lobes; an independent RNAi line reproduced the phenotype. Knockdown in optic-lobe lobular plate tangential neurons shortened major dendritic branches and reduced total branch length (18–20 brains per genotype; t(36)=2.27, p<0.05). | Moderate to high. Independent RNAi and cell-type-specific morphology support causality, but the precise responsible isoform and molecular interaction remain unresolved. | Schwartz et al., 2023 (schwartz2023ankyrin2isessential pages 4-6, schwartz2023ankyrin2isessential pages 6-7) |
| Adult long-term memory | Ank2 is required acutely in adult mushroom-body circuitry for long-term courtship-suppression memory, particularly in γ neurons; this may reflect maintenance of axonal/synaptic architecture rather than a catalytic signaling activity. | Conditional adult mushroom-body knockdown impaired long-term memory while initial learning and immediate memory remained normal. Driver analysis localized a major requirement to mushroom-body γ neurons. Ank2 also genetically interacts with nuclear HDAC4, although the interaction does not require HDAC4’s predicted ankyrin-binding motif. | Moderate. Behavioral and conditional genetic evidence is strong, but no direct biochemical pathway from Ank2 to memory consolidation has been demonstrated. | Schwartz et al., 2023, peer-reviewed publication; supporting 2021 preprint analyses (schwartz2023ankyrin2isessential pages 1-2, schwartz2021ankyrin2isrequired pages 21-26, schwartz2021ankyrin2isrequired pages 1-3) |
Table: Evidence summary for the identity, architecture, localization, molecular interactions, and neuronal functions of Drosophila melanogaster Ank2/CG42734. The table distinguishes well-supported locus-level conclusions from findings that cannot yet be assigned specifically to the Q3KN55/RE55168p translation.
The Ank2 locus produces multiple products with distinct localization. The literature uses partly inconsistent nomenclature, including Ank2-S, Ank2-M, Ank2-L, Ank2a, and Ank2-XL. Reported distributions include a short form concentrated in neuronal somata, larger axonal forms, and giant Ank2-L/Ank2-XL proteins enriched in axons and presynaptic terminals (schwartz2023ankyrin2isessential pages 1-2, pielage2008apresynapticgiant pages 1-2).
Ank2-L is approximately 450 kDa and about 4,083 residues in one mapped model. Ank2-XL extends to approximately 11,640 residues, while the proteins share sequence through roughly residue 2,399. Ank2-XL contains a very large repeat-rich central region and a C-terminal microtubule-associated region. The giant central region is proposed to act as a molecular spacer that separates membrane-association and microtubule-binding activities, allowing three-dimensional organization of the axonal and presynaptic cytoskeleton (stephan2015hierarchicalmicrotubuleorganization pages 12-14, stephan2015hierarchicalmicrotubuleorganization pages 3-4).
These data establish that Ank2 is not an enzyme or transporter. It has no catalytic reaction or transported substrate. Its “substrates,” in a functional rather than enzymatic sense, are protein complexes and cytoskeletal structures whose localization and stability it organizes.
Ank2 functions as a multivalent scaffold. Its N-terminal ankyrin repeats recognize membrane-associated proteins, including cell-adhesion molecules and ion channels; its central region associates with spectrin; and extended giant-isoform regions interact with or organize microtubules. This architecture enables Ank2 to couple plasma-membrane organization to the spectrin–actin and microtubule cytoskeletons (schwartz2023ankyrin2isessential pages 1-2, pielage2008apresynapticgiant pages 1-2).
At the larval NMJ, Ank2-L forms a submembranous lattice-like presynaptic structure. Loss of Ank2-L disrupts microtubules, cell-adhesion-molecule organization, bouton-separating membrane constrictions, and subsynaptic domain spacing, leading to terminal destabilization, disassembly, and retraction. These observations support a structural “anchor” model rather than a conventional linear signaling-enzyme role (pielage2008apresynapticgiant pages 1-2).
A major membrane partner is Neuroglian (Nrg), the Drosophila L1-family cell-adhesion molecule. Nrg and Ank2-L codistribute in mushroom-body axons, and ankyrins interact with the conserved intracellular FIGQY region of L1-family CAMs. Selected Ank2 ankyrin-repeat subdomains are necessary for synaptic—but less consistently for general axonal—localization, organization of synaptic CAMs, and synaptic stability (schwartz2023ankyrin2isessential pages 4-6, weber2019theankyrinrepeat pages 1-2).
The ankyrin-repeat domain is functionally differentiated. AnkD3 comprises repeats 13–18 and is particularly important for Ank2 localization and synaptic maintenance; its deletion reduces axonal and synaptic protein abundance and fails to restore normal CAM organization or stability. Rescue experiments also found that an AnkD1 deletion could restore adult viability, AnkD4 deletion only pupal viability, and AnkD2, AnkD3, or AnkD2-replacement constructs failed to restore viability, demonstrating that the repeats are not interchangeable generic motifs (weber2019theankyrinrepeat pages 2-4, weber2019theankyrinrepeat pages 11-12).
In adult mushroom bodies, Ank2 has also been proposed to participate in an Nrg–Ank2–Moesin assembly. In this model, Ank2 stabilizes transaxonal Nrg adhesion while Moesin links the complex to actin. Similar axon-growth and guidance defects following Nrg or Moesin perturbation support the model, although a complete purified ternary complex has not been demonstrated (schwartz2023ankyrin2isessential pages 6-7).
Ank2-L and Ank2-XL organize microtubules hierarchically. Ank2-L loss removes the microtubule-associated protein Futsch/MAP1B from terminal boutons and causes central microtubule/Futsch aggregation. Ank2-XL mutants similarly show large aggregates in more than 90% of NMJs, but retain microtubules at terminal boutons, indicating distinct isoform functions (stephan2015hierarchicalmicrotubuleorganization pages 3-4).
Futsch co-precipitates with Ank2-XL in control tissue but not in Ank2-XL deletion mutants. Removing Futsch suppresses microtubule accumulations and restores bouton separation in Ank2-XL and Ank2-null backgrounds, demonstrating a specific genetic and biochemical relationship rather than mere colocalization. Combined Ank2/Futsch disruption reduces microtubule spacing and membrane association, axonal diameter, anterograde transport, release-site number, and neurotransmitter release, even though microtubule number per axonal cross-section remains unchanged (stephan2015hierarchicalmicrotubuleorganization pages 12-14).
Ank2-L is upstream of Ank2-XL in presynaptic scaffold assembly. Removing Ank2-L severely disrupts Ank2-XL abundance and localization. By contrast, removing Ank2-XL abolishes XL staining but only modestly reduces Ank2-L and does not eliminate its presynaptic distribution. Thus, Ank2-L recruits or stabilizes Ank2-XL, although whether this reflects direct isoform binding or dependence on a shared scaffold remains unresolved (weber2019theankyrinrepeat pages 2-4, weber2019theankyrinrepeat pages 1-2).
Ank2 is an intracellular, peripheral membrane-associated neuronal scaffold rather than a secreted or transmembrane protein. Its principal functional sites are:
Adult-brain immunohistochemistry showed widespread Ank2-L in optic and antennal lobes, mushroom bodies, and axon tracts. It codistributed with the neuronal microtubule-associated marker Futsch but not with the glial marker Repo, supporting predominantly neuronal expression (schwartz2023ankyrin2isessential pages 4-6).
Ank2 operates in a cell-adhesion–cytoskeleton pathway rather than a classical soluble signaling cascade. Its ankyrin repeats engage adhesion/membrane proteins, the spectrin-binding region anchors the submembranous skeleton, and giant C-terminal regions organize microtubules. The resulting assembly resists mechanical and developmental destabilization of presynaptic terminals (pielage2008apresynapticgiant pages 1-2).
Loss-of-function phenotypes include abnormal bouton morphology, failed bouton separation, microtubule disorganization, altered excitability, reduced release architecture, and presynaptic retraction. These phenotypes identify structural maintenance of mature synapses—not simply initial synapse formation—as a primary Ank2 function (stephan2015hierarchicalmicrotubuleorganization pages 12-14, pielage2008apresynapticgiant pages 1-2).
By controlling microtubule spacing and their association with the axonal cortex, Ank2 and Futsch maintain axonal caliber and efficient transport. The observation that transport slows despite an unchanged number of microtubules per cross-section indicates that microtubule geometry and membrane coupling, rather than microtubule abundance alone, determine transport competence (stephan2015hierarchicalmicrotubuleorganization pages 12-14).
Drosophila neurons possess an AIS-like proximal axonal compartment dependent on giant Ank2. FRAP experiments showed significantly increased axonal diffusion after disruption of L-exon-containing isoforms (p<0.02; 19 mutant axonal cells and 9 dendritic cells), indicating loss of a selective diffusion barrier. GFP-tagged Shal, a voltage-gated potassium channel, normally peaks approximately 10–50 μm from the soma; this peak was greatly reduced in Ank2 trans-heterozygotes, where Shal instead became highest beside the soma and declined distally (jegla2016bilateriangiantankyrins pages 19-22).
Expression of an Ank2-L C-terminal fragment severely shortened the AIS-like region in mushroom-body neurons and produced axonal degeneration and neuronal loss. This dominant-interference experiment links Ank2-dependent proximal-domain integrity to long-term axonal survival, although the fly AIS-like compartment should not be assumed identical in every respect to the vertebrate AIS (spurrier2019expressionofa pages 1-3).
The most directly relevant recent primary study was published in May 2023; the searches did not identify a focused 2024 primary study that supersedes it.
Schwartz and colleagues provided the first detailed characterization of Ank2 distribution in the adult fly brain. Pan-neuronal RNAi caused thin, missing, prematurely terminated, fused, or misoriented mushroom-body lobes, and an independent RNAi construct reproduced the range of abnormalities. This supports a requirement for Ank2 in axon growth, targeting, or maintenance rather than an off-target effect of a single RNAi reagent (schwartz2023ankyrin2isessential pages 4-6).
In optic-lobe lobular plate tangential neurons, Ank2 knockdown shortened major dendritic branches and significantly reduced total branch length. The analysis included 18–20 brains per genotype, with t(36)=2.27, p<0.05 (schwartz2023ankyrin2isessential pages 6-7). These findings extend Ank2 function from larval motor terminals to adult central-neuron morphogenesis.
Conditional adult knockdown in the mushroom body impaired long-term courtship-suppression memory while leaving learning and immediate memory comparatively intact. Driver analysis identified a particularly important requirement in mushroom-body γ neurons. Thus, Ank2 is required not only during development but also in the adult neural processes that sustain long-term memory (schwartz2023ankyrin2isessential pages 1-2, schwartz2021ankyrin2isrequired pages 21-26).
Ank2 also genetically interacts with nuclear HDAC4, but the relationship does not require HDAC4’s predicted ankyrin-binding motif. This is evidence for pathway-level interaction, not yet for direct Ank2–HDAC4 binding. The most conservative interpretation is that nuclear transcriptional regulation and Ank2-dependent cytoskeletal organization converge on neuronal morphology and memory, while the intervening molecular mechanism remains unknown (schwartz2021ankyrin2isrequired pages 1-3).
The best-supported annotation is that Ank2 is a neuronal membrane–cytoskeleton organizer essential for axonal and synaptic stability. This conclusion rests on convergent mutant, RNAi, rescue, immunolocalization, ultrastructural, biochemical co-precipitation, live-transport, electrophysiological, and behavioral evidence (pielage2008apresynapticgiant pages 1-2, stephan2015hierarchicalmicrotubuleorganization pages 12-14, weber2019theankyrinrepeat pages 2-4).
Evidence is strongest at the Ank2 locus and Ank2-L/XL isoform levels. Assignment to the specific Q3KN55/RE55168p sequence is less certain because the accession was not used to identify experimental constructs in the retrieved papers. Isoform nomenclature also varies among publications, making direct equivalence between Ank2-S/M/L and Ank2a/L/XL unsafe without transcript-coordinate reconciliation.
There is no established therapeutic or industrial implementation directed at fly Ank2. Its current applications are primarily experimental:
Molecular function: Nonenzymatic ankyrin-repeat cytoskeletal adaptor; binds or organizes neuronal membrane proteins and cell-adhesion complexes, associates with the spectrin-based membrane skeleton, and couples these structures to organized microtubules.
Primary biological role: Establishment and maintenance of axonal and presynaptic architecture, including synaptic CAM distribution, presynaptic microtubule organization, bouton separation, axonal caliber and transport, and proximal-axon membrane-domain organization.
Cellular component/localization: Cytoplasmic face of neuronal plasma membranes; axonal submembrane cortex; proximal axon/AIS-like domain; presynaptic NMJ boutons; adult-brain axon tracts and mushroom-body lobes.
Associated processes: Synapse stabilization, prevention of presynaptic retraction, microtubule organization, axonal transport, ion-channel localization, neuronal morphogenesis, axon guidance/maintenance, dendritic arborization, and long-term memory.
Not supported: Catalytic activity, transport of a molecular substrate, secretion, or integral membrane topology.
References
(schwartz2023ankyrin2isessential pages 4-6): Silvia Schwartz, Sarah J Wilson, Tracy K Hale, and Helen L Fitzsimons. Ankyrin2 is essential for neuronal morphogenesis and long-term courtship memory in drosophila. Molecular Brain, May 2023. URL: https://doi.org/10.1186/s13041-023-01026-w, doi:10.1186/s13041-023-01026-w. This article has 10 citations and is from a peer-reviewed journal.
(schwartz2023ankyrin2isessential pages 1-2): Silvia Schwartz, Sarah J Wilson, Tracy K Hale, and Helen L Fitzsimons. Ankyrin2 is essential for neuronal morphogenesis and long-term courtship memory in drosophila. Molecular Brain, May 2023. URL: https://doi.org/10.1186/s13041-023-01026-w, doi:10.1186/s13041-023-01026-w. This article has 10 citations and is from a peer-reviewed journal.
(pielage2008apresynapticgiant pages 1-2): Jan Pielage, Ling Cheng, Richard D. Fetter, Pete M. Carlton, John W. Sedat, and Graeme W. Davis. A presynaptic giant ankyrin stabilizes the nmj through regulation of presynaptic microtubules and transsynaptic cell adhesion. Neuron, 58:195-209, Apr 2008. URL: https://doi.org/10.1016/j.neuron.2008.02.017, doi:10.1016/j.neuron.2008.02.017. This article has 214 citations and is from a highest quality peer-reviewed journal.
(spurrier2019expressionofa pages 1-3): Joshua Spurrier, Arvind K. Shukla, Tyler Buckley, Svetlana Smith-Trunova, Irina Kuzina, Qun Gu, and Edward Giniger. Expression of a fragment of ankyrin 2 disrupts the structure of the axon initial segment and causes axonal degeneration in drosophila. Molecular Neurobiology, 56:5689-5700, Jan 2019. URL: https://doi.org/10.1007/s12035-019-1477-6, doi:10.1007/s12035-019-1477-6. This article has 11 citations and is from a peer-reviewed journal.
(weber2019theankyrinrepeat pages 2-4): Tobias Weber, Raiko Stephan, Eliza Moreno, and Jan Pielage. The ankyrin repeat domain controls presynaptic localization of drosophila ankyrin2 and is essential for synaptic stability. Frontiers in Cell and Developmental Biology, Aug 2019. URL: https://doi.org/10.3389/fcell.2019.00148, doi:10.3389/fcell.2019.00148. This article has 13 citations.
(weber2019theankyrinrepeat pages 1-2): Tobias Weber, Raiko Stephan, Eliza Moreno, and Jan Pielage. The ankyrin repeat domain controls presynaptic localization of drosophila ankyrin2 and is essential for synaptic stability. Frontiers in Cell and Developmental Biology, Aug 2019. URL: https://doi.org/10.3389/fcell.2019.00148, doi:10.3389/fcell.2019.00148. This article has 13 citations.
(stephan2015hierarchicalmicrotubuleorganization pages 3-4): Raiko Stephan, Bernd Goellner, Eliza Moreno, C. Andrew Frank, Tabea Hugenschmidt, Christel Genoud, Hermann Aberle, and Jan Pielage. Hierarchical microtubule organization controls axon caliber and transport and determines synaptic structure and stability. Developmental cell, 33 1:5-21, Apr 2015. URL: https://doi.org/10.1016/j.devcel.2015.02.003, doi:10.1016/j.devcel.2015.02.003. This article has 96 citations and is from a highest quality peer-reviewed journal.
(weber2019theankyrinrepeat pages 11-12): Tobias Weber, Raiko Stephan, Eliza Moreno, and Jan Pielage. The ankyrin repeat domain controls presynaptic localization of drosophila ankyrin2 and is essential for synaptic stability. Frontiers in Cell and Developmental Biology, Aug 2019. URL: https://doi.org/10.3389/fcell.2019.00148, doi:10.3389/fcell.2019.00148. This article has 13 citations.
(stephan2015hierarchicalmicrotubuleorganization pages 12-14): Raiko Stephan, Bernd Goellner, Eliza Moreno, C. Andrew Frank, Tabea Hugenschmidt, Christel Genoud, Hermann Aberle, and Jan Pielage. Hierarchical microtubule organization controls axon caliber and transport and determines synaptic structure and stability. Developmental cell, 33 1:5-21, Apr 2015. URL: https://doi.org/10.1016/j.devcel.2015.02.003, doi:10.1016/j.devcel.2015.02.003. This article has 96 citations and is from a highest quality peer-reviewed journal.
(jegla2016bilateriangiantankyrins pages 19-22): Timothy Jegla, Michelle M. Nguyen, Chengye Feng, Daniel J. Goetschius, Esteban Luna, Damian B. van Rossum, Bishoy Kamel, Aditya Pisupati, Elliott S. Milner, and Melissa M. Rolls. Bilaterian giant ankyrins have a common evolutionary origin and play a conserved role in patterning the axon initial segment. Dec 2016. URL: https://doi.org/10.1371/journal.pgen.1006457, doi:10.1371/journal.pgen.1006457. This article has 50 citations and is from a domain leading peer-reviewed journal.
(schwartz2023ankyrin2isessential pages 6-7): Silvia Schwartz, Sarah J Wilson, Tracy K Hale, and Helen L Fitzsimons. Ankyrin2 is essential for neuronal morphogenesis and long-term courtship memory in drosophila. Molecular Brain, May 2023. URL: https://doi.org/10.1186/s13041-023-01026-w, doi:10.1186/s13041-023-01026-w. This article has 10 citations and is from a peer-reviewed journal.
(schwartz2021ankyrin2isrequired pages 21-26): Silvia Schwartz, Sarah J Wilson, Tracy K Hale, and Helen L Fitzsimons. Ankyrin2 is required for neuronal morphogenesis and long-term memory and interacts genetically with hdac4. bioRxiv, Jul 2021. URL: https://doi.org/10.1101/2021.07.18.452850, doi:10.1101/2021.07.18.452850. This article has 0 citations.
(schwartz2021ankyrin2isrequired pages 1-3): Silvia Schwartz, Sarah J Wilson, Tracy K Hale, and Helen L Fitzsimons. Ankyrin2 is required for neuronal morphogenesis and long-term memory and interacts genetically with hdac4. bioRxiv, Jul 2021. URL: https://doi.org/10.1101/2021.07.18.452850, doi:10.1101/2021.07.18.452850. This article has 0 citations.