Function
Processes
Locations
Hub adaptor that links PI(4,5)P2, vesicle cargo, accessory proteins and clathrin.
The retrieval stage of the synaptic vesicle cycle, in which vesicle membrane and resident proteins deposited in the presynaptic plasma membrane by exocytosis are recovered and re-formed into release-competent vesicles at the presynaptic endocytic zone. In the classical clathrin-mediated route, the AP-2 adaptor complex, the neuron-specific assembly protein AP180 and the synaptotagmin-sorting adaptor stonin-2 recognise vesicle cargo and PI(4,5)P2 and nucleate a clathrin coat; BAR-domain proteins (endophilin, amphiphysin, syndapin) shape the invaginating membrane and recruit the GTPase dynamin, which constricts and severs the neck; synaptojanin-1 hydrolyses PI(4,5)P2 and auxilin recruits HSC70 to strip the clathrin coat, yielding a naked vesicle ready for re-acidification and loading. The same coat, curvature, fission and uncoating machinery is reused when membrane is first retrieved by clathrin-independent ultrafast or bulk endocytosis and vesicles are then regenerated by clathrin-dependent budding from a synaptic endosome. The module conforms, with stated deviations, to the generic MODULE:vesicle_coat_budding motif. Exemplars are human. Grounded in GO:0048488 (synaptic vesicle endocytosis).
Human-centric exemplars with family-level descriptors so the module stays reusable. The mechanistic parts (coat assembly, curvature, fission, uncoating) are shared by both retrieval routes; the root variant set records only where the coat forms (plasma membrane vs synaptic endosome). Kiss-and-run retrieval is not modeled. Stonin-2 and AP2M1 both belong to the AP-mu PANTHER family (PTHR10529); the two descriptors are kept as distinct roles, each grounded at family level so that the worm orthologs (unc-41, dpy-23) fit. Loading and release stages are in MODULE:synaptic_vesicle_neurotransmitter_loading and MODULE:synaptic_vesicle_exocytosis; MODULE:synaptic_vesicle_cycle is the umbrella. Caenorhabditis elegans orthologs are listed as second representative members (dpy-23, apb-1, apa-2, aps-2, unc-11, unc-41, chc-1, clic-1, unc-57, amph-1, sdpn-1, dyn-1, unc-26, dnj-25, hsp-1); the worm has one dynamin (dyn-1) and one endophilin (unc-57), and ultrafast endocytosis was first described at its neuromuscular junction. Two caveats from the worm gene reviews: amph-1 and sdpn-1 are grounded here by orthology only, since their worm literature covers intestinal endocytic recycling and nuclear positioning rather than synaptic vesicle retrieval; and the worm has a single beta-adaptin (apb-1) shared between AP-1 and AP-2, so its AP-1 annotations are correct rather than over-propagated.
knowledge_gaps[1] · provenance
(0/1)knowledge_gaps[2] · provenance
(0/1)✗ none found
No MODULE:synaptic_vesicle_endocytosis deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
4 conformance issue(s):
✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.
16 complete review(s) · 18 with deep research · 11 missing review · 3 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| amph-1 Q21004 | ✓ | ✓ | ✓ |
| AP2M1 Q96CW1 | ✓ | 128/184 | ✗ |
| AP2S1 P53680 | ✓ | ✓ | ✓ |
| apa-2 Q22601 | ✓ | ✓ | ✓ |
| apb-1 Q9N4F3 | ✓ | ✓ | ✓ |
| aps-2 Q19123 | ✓ | ✓ | ✓ |
| chc-1 P34574 | ✓ | 31/33 | ✓ |
| clic-1 P90961 | ✓ | ✓ | ✓ |
| CLTC Q00610 | ✓ | ✓ | ✓ |
| DNAJC6 O75061 | ✓ | ✓ | ✗ |
| dnj-25 A0A486WXP9 | ✓ | ✓ | ✓ |
| dpy-23 P35603 | ✓ | 22/23 | ✓ |
| dyn-1 P39055 | ✓ | 45/47 | ✓ |
| hsp-1 P09446 | ✓ | ✓ | ✓ |
| HSPA8 P11142 | ✓ | ✓ | ✓ |
| SYNJ1 (Homo sapiens) O43426 | ✗ | — | — |
| SNAP91 (Homo sapiens) O60641 | ✗ | — | — |
| AP2A1 (Homo sapiens) O95782 | ✗ | — | — |
| CLTA (Homo sapiens) P09496 | ✗ | — | — |
| AMPH (Homo sapiens) P49418 | ✗ | — | — |
| AP2B1 (Homo sapiens) P63010 | ✗ | — | — |
| PICALM Q13492 | ✓ | ✓ | ✗ |
| DNM1 (Homo sapiens) Q05193 | ✗ | — | — |
| STON2 (Homo sapiens) Q8WXE9 | ✗ | — | — |
| SH3GL2 (Homo sapiens) Q99962 | ✗ | — | — |
| PACSIN1 (Homo sapiens) Q9BY11 | ✗ | — | — |
| DNM3 (Homo sapiens) Q9UQ16 | ✗ | — | — |
| sdpn-1 Q6AHQ8 | ✓ | ✓ | ✓ |
| unc-11 Q9XZI6 | ✓ | 40/41 | ✓ |
| unc-26 G5ECL2 | ✓ | ✓ | ✓ |
| unc-41 P90761 | ✓ | ✓ | ✓ |
| unc-57 B1V8A0 | ✓ | ✓ | ✓ |
Adaptors bind PI(4,5)P2 and vesicle cargo (synaptotagmin, VAMP2, SV2) on the plasma membrane and recruit clathrin triskelia, which polymerise into the coat of the forming pit.
Hub adaptor that links PI(4,5)P2, vesicle cargo, accessory proteins and clathrin.
ANTH-domain PI(4,5)P2 binder that sorts VAMP2 into the pit and sets the size of the regenerated vesicle.
mu-homology-domain adaptor dedicated to retrieving synaptotagmin into the pit via AP-2.
Polymerises into the polyhedral lattice that stabilises the budding pit.
N-BAR (endophilin, amphiphysin) and F-BAR (syndapin/PACSIN) proteins bind and bend the membrane, generating and stabilising the tubular neck of the pit, and their SH3 domains recruit dynamin and synaptojanin to it.
Senses/induces neck curvature and recruits dynamin and synaptojanin-1 through its SH3 domain, coupling fission to uncoating.
Binds AP-2 and clathrin and recruits dynamin to the neck via its SH3 domain.
Neuronal F-BAR protein that tubulates membrane and recruits dynamin; also implicated in bulk retrieval.
Dynamin polymerises around the neck; GTP hydrolysis drives constriction and membrane fission, releasing the coated vesicle.
Mechanochemical scission of the neck for both clathrin-coated pits and ultrafast/bulk invaginations.
Synaptojanin-1 dephosphorylates PI(4,5)P2 to release adaptors from the membrane; auxilin binds the clathrin lattice and recruits HSC70, whose ATP hydrolysis disassembles the coat, leaving a naked vesicle that can re-acidify and be reloaded.
Removes the PI(4,5)P2 anchor of AP-2/AP180 so that adaptors dissociate after fission.
Binds the clathrin lattice after fission and, through its J domain, targets HSC70 to it.
ATP-driven disassembly of the clathrin lattice, directed by auxilin.
Both routes reuse the coat, curvature, fission and uncoating parts above; they differ in whether the clathrin coat forms directly on the plasma membrane or on a synaptic endosome after clathrin-independent uptake.
The classical route: a clathrin-coated pit forms in the presynaptic endocytic zone and buds a vesicle directly from the plasma membrane over seconds to tens of seconds.
The coat forms on the plasma membrane and the budded vesicle is uncoated directly.
Clathrin-independent, dynamin- and actin-dependent invagination at the edge of the active zone retrieves membrane within tens of milliseconds (ultrafast) or as large cisternae after strong stimulation (bulk); synaptic vesicles are then regenerated by clathrin-dependent budding from the resulting synaptic endosome.
Severs the clathrin-independent invagination to form a synaptic endosome.
Clathrin coats bud uniform synaptic vesicles from the endosomal intermediate.