Function
Locations
Acyl-CoA-binding protein that is unconventionally secreted by prespore cells; its processed peptide is the SDF-2 sporulation signal. Its intrinsic molecular function is acyl-CoA binding.
The non-cell-autonomous signalling relay that triggers rapid, synchronous encapsulation of prespore cells into spores during culmination in Dictyostelium discoideum. The acyl-CoA-binding protein AcbA is unconventionally secreted by prespore cells and cleaved at the prestalk cell surface by the ABC-transporter/ serine-protease TagC to release the peptide signal SDF-2. SDF-2 binds the membrane sensor histidine kinase DhkA and INHIBITS its phosphorelay; because DhkA (through the histidine-phosphotransfer protein RdeA) normally keeps the response-regulator cAMP phosphodiesterase RegA active, inhibiting DhkA lowers RegA activity, so intracellular cAMP rises and activates cAMP-dependent protein kinase (PKA-C released from PKA-R), which drives spore encapsulation. The net logic is a double negative — SDF-2 inhibits DhkA, DhkA activates RegA, RegA suppresses cAMP/PKA — so SDF-2 ultimately ACTIVATES encapsulation. The relay is self-amplifying (encapsulating cells release more AcbA). Phrased over functions and family selectors with D. discoideum representatives rather than a fixed gene list. OUT OF SCOPE: the parallel GABA/GrlE input that also triggers AcbA release (a separate module), the ACR/PKA culmination cAMP source, and spore-coat assembly. The histidine-phosphotransfer intermediate RdeA is described in the DhkA->RegA connection but is NOT separately grounded here because it has not yet been reviewed.
Dictyostelium-specific culmination signalling relay grounded to six reviewed proteins: AcbA (Q5FXM5), TagC (Q23868, GO:0004252), DhkA (Q54U87, GO:0000155), RegA (Q23917, GO:0004115), PKA-R (P05987, GO:0004862) and PKA-C (P34099, GO:0004691). GO molecular-function terms were taken from the completed DICDI reviews; each node uses a PANTHER family selector plus the D. discoideum representative member. The DhkA->RegA direction follows the Wang/Anjard-Loomis inhibition model adopted in the dhkA review (SDF-2 inhibits DhkA, lowering RegA and raising cAMP/PKA); the alternative Tekinay model is recorded as contested there. The histidine-phosphotransfer intermediate RdeA (Q54RR8, GO:0009927) is now grounded as its own node (rdea_relay) between DhkA and RegA, following the completed rdeA review. Named to signal Dictyostelium scope so it does not collide with a generic two-component / cAMP-PKA signalling module.
All recommended fields populated.
✗ none found
No MODULE:dicty_sdf2_encapsulation_relay deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
6 complete review(s) · 0 with deep research · 0 missing review · 7 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| acbA Q5FXM5 | ✓ | ✓ | ✗ |
| dhkA Q54U87 | ✓ | ✓ | ✗ |
| pkaC P34099 | ✓ | 52/54 | ✗ |
| pkaR P05987 | ✓ | ✓ | ✗ |
| rdeA Q54RR8 | ✓ | ✓ | ✗ |
| regA Q23917 | ✓ | ✓ | ✗ |
| tagC Q23868 | ✓ | ✓ | ✗ |
Acyl-CoA-binding protein that is unconventionally secreted by prespore cells; its processed peptide is the SDF-2 sporulation signal. Its intrinsic molecular function is acyl-CoA binding.
Prestalk cell-surface protein whose serine-protease domain cleaves secreted AcbA to liberate the diffusible SDF-2 peptide.
Membrane-spanning sensor histidine kinase that binds SDF-2 through its extracellular loop; ligand binding inhibits its autophosphorylation and downstream phosphorelay.
Cytosolic HPt intermediate that accepts phosphate on His-65 from the sensor kinase DhkA and transfers it to the RegA receiver aspartate, keeping RegA active; SDF-2 inhibition of DhkA reduces this flux.
Response-regulator cAMP phosphodiesterase; its receiver domain is kept phosphorylated (active) by the DhkA phosphorelay through the RdeA histidine-phosphotransfer protein, so degrading cAMP and holding PKA off until SDF-2 inhibits DhkA.
Regulatory subunit that binds and inhibits the PKA catalytic subunit; cAMP binding to PKA-R releases active PKA-C.
Catalytic subunit whose activation by cAMP is the master switch for terminal spore encapsulation during culmination.