DdCAD-1 (also called gp24 or CadA) is the calcium-dependent (EDTA/EGTA-sensitive) homophilic cell-cell adhesion molecule of the social amoeba Dictyostelium discoideum. It is a 24 kDa, 213-residue protein composed of two beta-sandwich domains (an N-terminal betagamma-crystallin-like domain and a C-terminal immunoglobulin-like domain); the N-terminal domain mediates homophilic binding whereas the C-terminal domain tethers the protein to the plasma membrane. DdCAD-1 is a soluble calcium-binding protein that lacks a signal peptide and a transmembrane domain; it is synthesized in the cytoplasm at the onset of starvation-induced development and reaches the cell surface by an unconventional secretion route in which it is imported into and transported by contractile vacuoles and then anchored to the plasma membrane by the ABC transporter ABCB4. Calcium binding and association with calmodulin are required for its import into contractile vacuoles. On the cell surface it establishes the earliest (contact-site-B) adhesions that drive aggregation, and its differential distribution between prestalk and prespore cells contributes to cell sorting, cell-type proportioning, and morphogenesis of the fruiting body (sorocarp). Independently of development, secreted DdCAD-1 also acts as a calcium-dependent, galactose-specific lectin that agglutinates Gram-negative bacteria such as Klebsiella pneumoniae, forming a protective interface that shields feeding amoebae from bacterial toxicity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005509 calcium ion binding | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference of calcium ion binding is well supported by direct experimental evidence for DdCAD-1. The protein carries multiple Ca2+-binding sites and calcium is required for its adhesion and its import into contractile vacuoles. Reason: Calcium binding is a genuine and central property of DdCAD-1, demonstrated directly by 45Ca2+ overlay and NMR structures, so the IBA inference is corroborated by experimental data. Supporting Evidence: PMID:8227052 Binding studies showed that 45Ca2+ could bind to gp24 blotted onto nitrocellulose membrane |
| GO:0005516 calmodulin binding | IBA GO_REF:0000033 | ACCEPT | Summary: Calmodulin binding by DdCAD-1 is supported by direct experimental evidence. Ca2+-bound calmodulin interacts with DdCAD-1 and promotes its import into contractile vacuoles. Reason: Co-immunoprecipitation and pull-down assays demonstrate a direct DdCAD-1 / Ca2+-calmodulin interaction, corroborating the phylogenetic inference. Supporting Evidence: PMID:23441816 Co-immunoprecipitation and pull-down studies showed that only Ca(2+) -bound calmodulin was able to bind DdCAD-1 |
| GO:0005911 cell-cell junction | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: DdCAD-1 concentrates at cell-cell contact regions during early development, so a broad cell-cell junction assignment is defensible, but Dictyostelium adhesion sites are not classic junctions and this is not the most informative descriptor of the protein's activity. Reason: DdCAD-1 is enriched in cell contact regions, but the core statement of its function is captured by external side of plasma membrane and calcium-dependent cell-cell adhesion; the junction term is retained as a non-core localization. Supporting Evidence: PMID:8806827 A high concentration of DdCAD-1 also becomes associated with lamellipodia and filopodia, which often appear to participate in cell contact formation |
| GO:0009897 external side of plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: DdCAD-1 acts on the ecto-surface of the plasma membrane, where it mediates homophilic adhesion. This is directly supported by immunofluorescence and is a core localization. Reason: The phylogenetic inference matches direct experimental evidence that DdCAD-1 is associated with the outer face of the plasma membrane. Supporting Evidence: PMID:8663243 immunofluorescence microscopy demonstrates the association of DdCAD-1 with the ecto-surface of the plasma membrane |
| GO:0016339 calcium-dependent cell-cell adhesion | IBA GO_REF:0000033 | ACCEPT | Summary: This is the defining function of DdCAD-1, strongly supported by biochemical and genetic evidence. It mediates the EDTA/EGTA-sensitive calcium-dependent adhesion of the early developmental stage. Reason: Calcium-dependent homophilic cell-cell adhesion is the core evolved function of DdCAD-1 and is directly demonstrated experimentally. Supporting Evidence: PMID:8227052 It is therefore likely that gp24 mediates cell-cell interactions via a Ca(2+)-dependent mechanism |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: DdCAD-1 is presented on the plasma membrane after transport by contractile vacuoles. Plasma membrane localization is well supported. Reason: The UniProt-derived location matches direct evidence that DdCAD-1 is transported to and anchored at the plasma membrane. Supporting Evidence: PMID:17057715 It is synthesized as a soluble protein and then transported to the plasma membrane by contractile vacuoles |
| GO:0016020 membrane | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: The generic membrane term is subsumed by the more specific and experimentally supported plasma membrane and external side of plasma membrane annotations. Reason: The generic membrane term is an uninformative parent of the specific plasma membrane localization already annotated for DdCAD-1; it adds no information. |
| GO:0098609 cell-cell adhesion | IEA GO_REF:0000002 | MODIFY | Summary: The general cell-cell adhesion term is correct but a more specific child term, calcium-dependent cell-cell adhesion, precisely captures the DdCAD-1 mechanism and is already annotated with experimental support. Reason: DdCAD-1 mediates specifically calcium-dependent (EDTA/EGTA-sensitive) cell-cell adhesion; the more specific term should replace the generic one. Proposed replacements: calcium-dependent cell-cell adhesion Supporting Evidence: PMID:8227052 It is therefore likely that gp24 mediates cell-cell interactions via a Ca(2+)-dependent mechanism |
| GO:0005515 protein binding | IPI PMID:23441816 Ca(2+) -calmodulin interacts with DdCAD-1 and promotes DdCAD... | MODIFY | Summary: This IPI records the DdCAD-1 / calmodulin interaction. The bare protein binding term is uninformative; the specific partner is calmodulin, already annotated as calmodulin binding. Reason: The interacting partner in this reference is Ca2+-calmodulin, so the more informative molecular function calmodulin binding should be used instead of generic protein binding. Proposed replacements: calmodulin binding Supporting Evidence: PMID:23441816 the data show that calmodulin forms a complex with DdCAD-1 and promotes the docking and import of DdCAD-1 into contractile vacuoles |
| GO:0042802 identical protein binding | IPI PMID:17057715 Solution structures of the adhesion molecule DdCAD-1 reveal ... | ACCEPT | Summary: DdCAD-1 self-associates to form a Ca2+-bound homodimer, the molecular basis of its homophilic adhesion. Identical protein binding correctly captures this self-interaction. Reason: NMR structural analysis supports a DdCAD-1 dimer model underlying homophilic cell-cell adhesion, directly justifying identical protein binding. Supporting Evidence: PMID:17057715 we propose a model for the Ca(2+)-bound DdCAD-1 dimer as a basis for understanding DdCAD-1-mediated cell-cell adhesion |
| GO:0071944 cell periphery | IDA PMID:38986731 Trafficking of adhesion and aggregation-modulating proteins ... | ACCEPT | Summary: DdCAD-1 localizes to the cell periphery in growth-phase and starved cells, consistent with its role as a surface adhesion molecule. Reason: Direct localization evidence places CadA at the cell periphery; this is a correct, if general, localization. Supporting Evidence: PMID:38986731 As for CadA, it localizes to the cell periphery in growth-phase and starved cells |
| GO:0005516 calmodulin binding | IPI PMID:23441816 Ca(2+) -calmodulin interacts with DdCAD-1 and promotes DdCAD... | ACCEPT | Summary: Direct co-immunoprecipitation and pull-down evidence shows DdCAD-1 binds Ca2+-calmodulin, an interaction that promotes its docking and import into contractile vacuoles. Reason: Calmodulin binding is directly demonstrated and is functionally relevant to the unconventional secretion of DdCAD-1. Supporting Evidence: PMID:23441816 Co-immunoprecipitation and pull-down studies showed that only Ca(2+) -bound calmodulin was able to bind DdCAD-1 |
| GO:0031012 extracellular matrix | IDA PMID:26152465 Proteomic profiling of the extracellular matrix (slime sheat... | KEEP AS NON CORE | Summary: DdCAD-1 was detected by LC/MS/MS in the slug extracellular matrix (slime sheath). Because DdCAD-1 is a secreted protein, its presence in the ECM is plausible but is a secondary localization rather than its core site of action. Reason: Proteomic detection in the slime sheath is consistent with DdCAD-1 being unconventionally secreted, but the ECM is not where it performs its core homophilic adhesion function. Supporting Evidence: PMID:26152465 An LC/MS/MS analysis of slug ECM revealed the presence of a large number of proteins in two wild-type strains, NC4 and WS380B |
| GO:0000331 contractile vacuole | IDA PMID:19875452 Cell adhesion molecule DdCAD-1 is imported into contractile ... | ACCEPT | Summary: DdCAD-1 is imported into contractile vacuoles by membrane invagination and transported to the plasma membrane. This is a core, well-established localization central to its unconventional secretion. Reason: Both in vivo time-lapse imaging and in vitro reconstitution demonstrate DdCAD-1 import into contractile vacuoles. Supporting Evidence: PMID:19875452 Both morphological and biochemical characterizations showed that DdCAD-1-GFP was imported into contractile vacuoles |
| GO:0000331 contractile vacuole | IDA PMID:9265658 The cell adhesion molecule DdCAD-1 in Dictyostelium is targe... | ACCEPT | Summary: Immunofluorescence and subcellular fractionation show preferential association of DdCAD-1 with contractile vacuoles, the organelle that transports it to the cell surface. Reason: This foundational study established contractile vacuoles as the transport route for DdCAD-1, a core localization. Supporting Evidence: PMID:9265658 Immunofluorescence microscopy and subcellular fractionation revealed a preferential association of DdCAD-1 with contractile vacuoles |
| GO:0001726 ruffle | IDA PMID:8806827 Novel redistribution of the Ca(2+)-dependent cell adhesion m... | KEEP AS NON CORE | Summary: During redistribution before aggregation, DdCAD-1 becomes enriched on membrane ruffles. This is a dynamic, developmental-stage-specific localization rather than a core site of function. Reason: Enrichment on membrane ruffles is directly observed but reflects the protein's redistribution to the cell surface, not a distinct core function. Supporting Evidence: PMID:8806827 DdCAD-1 become localized predominantly at the cell periphery and an enrichment of DdCAD-1 occurs on membrane ruffles |
| GO:0005576 extracellular region | IDA PMID:31355329 Social amoebae establish a protective interface with their b... | ACCEPT | Summary: Secreted CadA acts extracellularly as a bacterial agglutinin at the plaque edge. Its activity in the extracellular region is directly demonstrated in the bacterial defense context. Reason: Recombinant CadA secreted/deposited extracellularly agglutinates bacteria and protects amoebae, establishing a genuine extracellular site of action. Supporting Evidence: PMID:31355329 CadA, a cell adhesion protein that functions in D. discoideum development, is also a bacterial agglutinin that forms a protective interface at the plaque edge that limits exposure of vegetative amoebae to bacteria |
| GO:0005737 cytoplasm | IDA PMID:19875452 Cell adhesion molecule DdCAD-1 is imported into contractile ... | ACCEPT | Summary: DdCAD-1 is synthesized as a soluble cytoplasmic protein before being imported into contractile vacuoles. Cytoplasmic localization is a core part of its biosynthesis and trafficking. Reason: DdCAD-1 lacks a signal peptide and is made as a soluble cytosolic protein, directly documented in this study. Supporting Evidence: PMID:19875452 DdCAD-1 is synthesized in the cytoplasm as a soluble protein and then transported by contractile vacuoles to the plasma membrane for surface presentation or secretion |
| GO:0005737 cytoplasm | IDA PMID:8663243 Molecular cloning and characterization of DdCAD-1, a Ca2+-de... | ACCEPT | Summary: The founding studies place a large fraction of DdCAD-1 in the cytosol, consistent with its lack of a signal peptide. Reason: Cytoplasmic (cytosolic) localization of soluble DdCAD-1 is well-established and forms part of its normal life cycle. Supporting Evidence: PMID:9265658 DdCAD-1 is present on the cell surface as well as in the cytosol |
| GO:0005811 lipid droplet | HDA PMID:24036346 Dictyostelium lipid droplets host novel proteins. | MARK AS OVER ANNOTATED | Summary: This assignment comes from a high-throughput proteomic survey of purified lipid droplets. The study focused on novel lipid droplet proteins and DdCAD-1 is an abundant soluble/secreted protein prone to co-purifying as a contaminant. Lipid droplet residence is not consistent with DdCAD-1 biology. Reason: A large-scale organelle proteomics hit is a weak basis for localization of an abundant secreted adhesion molecule; there is no functional rationale for DdCAD-1 in lipid droplets. Supporting Evidence: PMID:24036346 to further identify the lipid constituents and proteins of lipid droplets |
| GO:0005938 cell cortex | TAS PMID:15366765 Comparison of molecular mechanisms mediating cell contact ph... | KEEP AS NON CORE | Summary: A traceable author statement from a comparative review places DdCAD-1 at the cell cortex/periphery. This is consistent with its surface localization but is a general descriptor. Reason: Cortical/peripheral localization overlaps with the better-supported external side of plasma membrane and cell periphery annotations and is retained as non-core. |
| GO:0009897 external side of plasma membrane | IDA PMID:8663243 Molecular cloning and characterization of DdCAD-1, a Ca2+-de... | ACCEPT | Summary: Direct immunofluorescence shows DdCAD-1 on the ecto-surface of the plasma membrane, its principal functional location for homophilic adhesion. Reason: This is a core localization directly demonstrated by the founding characterization of DdCAD-1. Supporting Evidence: PMID:8663243 immunofluorescence microscopy demonstrates the association of DdCAD-1 with the ecto-surface of the plasma membrane |
| GO:0030027 lamellipodium | IDA PMID:8806827 Novel redistribution of the Ca(2+)-dependent cell adhesion m... | KEEP AS NON CORE | Summary: DdCAD-1 becomes concentrated on lamellipodia during the redistribution that precedes aggregation, where these structures form cell contacts. Reason: This is a dynamic developmental localization reflecting surface redistribution rather than a separate core function. Supporting Evidence: PMID:8806827 A high concentration of DdCAD-1 also becomes associated with lamellipodia and filopodia, which often appear to participate in cell contact formation |
| GO:0030139 endocytic vesicle | IDA PMID:7593293 Identification of major proteins associated with Dictyosteli... | MARK AS OVER ANNOTATED | Summary: This assignment derives from a proteomic catalog of magnetically isolated endocytic vesicles that reported the major protein constituents, including a 25 kDa ORF product. DdCAD-1 is an abundant protein and its appearance in such preparations is most likely incidental rather than functional. Reason: Detection in a bulk endocytic-vesicle proteome does not establish a functional role or stable residence for DdCAD-1 in endocytic vesicles. Supporting Evidence: PMID:7593293 This strategy allowed the identification of the major protein constituents of the vesicles |
| GO:0030175 filopodium | IDA PMID:8806827 Novel redistribution of the Ca(2+)-dependent cell adhesion m... | KEEP AS NON CORE | Summary: DdCAD-1 concentrates on filopodia that participate in early cell contact formation, a dynamic developmental localization. Reason: Filopodial enrichment reflects the surface redistribution of DdCAD-1 during aggregation rather than a distinct core function. Supporting Evidence: PMID:8806827 A high concentration of DdCAD-1 also becomes associated with lamellipodia and filopodia, which often appear to participate in cell contact formation |
| GO:0045335 phagocytic vesicle | HDA PMID:16926386 Proteomics fingerprinting of phagosome maturation and eviden... | MARK AS OVER ANNOTATED | Summary: This comes from a large-scale two-dimensional gel / mass spectrometry survey that identified 179 phagosomal proteins. DdCAD-1 is not a phagosomal component by function, and its detection in this catalog is most plausibly a co-purification artifact. Reason: High-throughput phagosome proteomics is a weak basis for asserting functional phagocytic vesicle localization of an abundant secreted adhesion molecule. Supporting Evidence: PMID:16926386 we identified 179 phagosomal proteins in the amoeba Dictyostelium |
| GO:0045335 phagocytic vesicle | HDA PMID:19482547 Proteomic analysis of Legionella-containing phagosomes isola... | MARK AS OVER ANNOTATED | Summary: This assignment derives from a proteomic survey of Legionella-containing phagosomes that identified 157 host proteins. DdCAD-1's appearance is most likely incidental co-purification rather than a functional localization. Reason: A bulk phagosome proteome hit does not establish a functional role for DdCAD-1 in phagocytic vesicles. Supporting Evidence: PMID:19482547 identified 157 phagosome host proteins |
| GO:0016339 calcium-dependent cell-cell adhesion | IMP PMID:12135922 Disruption of the gene encoding the cell adhesion molecule D... | ACCEPT | Summary: Disruption of cadA reduces EDTA-sensitive (calcium-dependent) cell adhesion by ~50%, providing genetic (loss-of-function) evidence for the core adhesion function of DdCAD-1. Reason: The cadA-null phenotype directly demonstrates DdCAD-1's requirement for calcium-dependent cell-cell adhesion; this is a core function. Supporting Evidence: PMID:12135922 The cadA-null cells showed a 50% reduction in EDTA-sensitive cell adhesion |
| GO:0005886 plasma membrane | IDA PMID:17057715 Solution structures of the adhesion molecule DdCAD-1 reveal ... | ACCEPT | Summary: DdCAD-1 is transported to and functions at the plasma membrane, where its C-terminal domain tethers it to a membrane anchor while the N-terminal domain mediates homophilic binding. Reason: Plasma membrane is a core functional location for DdCAD-1, supported by structural and localization studies. Supporting Evidence: PMID:17057715 Whereas the N-terminal domain has a major role in homophilic binding, the C-terminal domain tethers the protein to the cell membrane |
| GO:0005911 cell-cell junction | IDA PMID:8663243 Molecular cloning and characterization of DdCAD-1, a Ca2+-de... | KEEP AS NON CORE | Summary: DdCAD-1 acts at cell-cell contact regions during early development. Dictyostelium adhesion sites are not classic junctions, so this term is retained as a supporting, non-core descriptor. Reason: The more precise statement of DdCAD-1 activity is external side of plasma membrane plus calcium-dependent cell-cell adhesion; the junction term is a general localization. Supporting Evidence: PMID:8663243 immunofluorescence microscopy demonstrates the association of DdCAD-1 with the ecto-surface of the plasma membrane |
| GO:0007157 heterophilic cell-cell adhesion | IDA PMID:31355329 Social amoebae establish a protective interface with their b... | KEEP AS NON CORE | Summary: This annotation reflects CadA's calcium- and galactose-dependent agglutination of Gram-negative bacteria (binding a non-self bacterial surface). The classic DdCAD-1 amoebal adhesion is homophilic; this heterophilic activity is a distinct lectin-mediated, non-core role. Reason: The heterophilic binding here is CadA binding bacterial surface carbohydrates rather than amoeba-amoeba adhesion; it is a genuine but secondary (moonlighting) function captured more mechanistically by carbohydrate binding. Supporting Evidence: PMID:31355329 This suggests that CadA is a lectin that binds to carbohydrates on the surface of K. pneumoniae, perhaps to their lipopolysaccharide, which is rich in galactose moieties |
| GO:0016339 calcium-dependent cell-cell adhesion | IGI PMID:16622066 An activated Ras protein alters cell adhesion by dephosphory... | ACCEPT | Summary: Genetic interaction with RasG modulates DdCAD-1-dependent cohesion; activated RasG increases DdCAD-1 surface localization and calcium-dependent cell adhesion. Supports the core adhesion function. Reason: The RasG-dependent change in cohesion is DdCAD-1-dependent, reinforcing DdCAD-1's role in calcium-dependent cell-cell adhesion. Supporting Evidence: PMID:16622066 This increased cohesion was DdCAD-1-dependent and was correlated with increased localization of DdCAD-1 at the cell surface |
| GO:0031152 aggregation involved in sorocarp development | TAS PMID:15366765 Comparison of molecular mechanisms mediating cell contact ph... | KEEP AS NON CORE | Summary: DdCAD-1 mediates the earliest adhesive contacts that enable aggregation at the onset of development. Its involvement in aggregation is a downstream developmental consequence of its adhesion activity. Reason: Aggregation is a developmental process DdCAD-1 contributes to via its core adhesion function; retained as a non-core process annotation. |
| GO:0050829 defense response to Gram-negative bacterium | IMP PMID:31355329 Social amoebae establish a protective interface with their b... | KEEP AS NON CORE | Summary: cadA-null amoebae have strongly reduced viability on dense lawns of Klebsiella pneumoniae, and secreted CadA agglutinates the bacteria and protects amoebae from their toxicity. This is a well-supported but secondary (moonlighting) function distinct from developmental adhesion. Reason: The bacterial-defense role is genuine and directly demonstrated by loss-of-function and rescue experiments, but it is a separate, non-core function from the protein's developmental cell-adhesion role. Supporting Evidence: PMID:31355329 This interface is important for amoebal survival when bacteria-to-amoebae ratios are high |
| GO:0051702 biological process involved in interaction with symbiont | IDA PMID:31355329 Social amoebae establish a protective interface with their b... | KEEP AS NON CORE | Summary: Secreted CadA binds and agglutinates associated bacteria, imposing structure on the bacterial population at the plaque edge. This captures the same bacterial-interaction moonlighting role. Reason: CadA's direct interaction with bacterial associates is documented, but it is a secondary function relative to its developmental adhesion role. Supporting Evidence: PMID:31355329 CadA, a cell adhesion protein that functions in D. discoideum development, is also a bacterial agglutinin that forms a protective interface at the plaque edge that limits exposure of vegetative amoebae to bacteria |
| GO:0005515 protein binding | IPI PMID:24426151 ATP-Binding Cassette Transporter B4 Anchors the Cell Adhesio... | KEEP AS NON CORE | Summary: This IPI records the interaction between DdCAD-1 and its plasma membrane anchor, identified by cross-linking and mass spectrometry as the ABC transporter ABCB4. The bare protein binding term is uninformative but no specific molecular-function term captures the anchoring interaction. Reason: The interaction with the ABCB4 anchor is real and functionally relevant to surface presentation, but generic protein binding is not a core molecular function; retained as non-core rather than as core adhesion machinery. Supporting Evidence: PMID:24426151 to identify ABCB4 as the anchor protein of DdCAD-1 |
| GO:0005509 calcium ion binding | IDA PMID:17057715 Solution structures of the adhesion molecule DdCAD-1 reveal ... | ACCEPT | Summary: NMR solution structures of Ca2+-free and Ca2+-bound DdCAD-1 directly demonstrate calcium binding, which is required for adhesion and for contractile-vacuole import. A core molecular function. Reason: Structural determination of the Ca2+-bound form provides direct evidence for calcium ion binding by DdCAD-1. Supporting Evidence: PMID:17057715 we propose a model for the Ca(2+)-bound DdCAD-1 dimer as a basis for understanding DdCAD-1-mediated cell-cell adhesion |
| GO:0005509 calcium ion binding | IDA PMID:8227052 Characterization of the cell adhesion molecule gp24 in Dicty... | ACCEPT | Summary: 45Ca2+ overlay assays and calcium-induced gel-mobility shifts directly demonstrate that DdCAD-1 (gp24) is a calcium-binding protein. A core molecular function. Reason: Direct 45Ca2+ binding to gp24 establishes calcium ion binding as an intrinsic property of DdCAD-1. Supporting Evidence: PMID:8227052 Binding studies showed that 45Ca2+ could bind to gp24 blotted onto nitrocellulose membrane |
| GO:1904643 response to curcumin | IDA PMID:26449461 Curcumin inhibits development and cell adhesion in Dictyoste... | KEEP AS NON CORE | Summary: This annotation stems from the observation that curcumin treatment suppresses expression of DdCAD (and csA) and delays adhesion. This makes DdCAD a target affected by curcumin rather than a protein with a functional role in a curcumin response. Reason: The evidence shows DdCAD expression is down-regulated by curcumin, an indirect drug effect; it is at best a peripheral process annotation, not a core function. Supporting Evidence: PMID:26449461 expression of the extracellular matrix/cell adhesion proteins (DdCAD and csA) |
| GO:0010468 regulation of gene expression | IDA PMID:12135922 Disruption of the gene encoding the cell adhesion molecule D... | UNDECIDED | Summary: The cadA-null study documents altered cell-type proportioning (increased prestalk proportion) and aberrant sorting, but the cached abstract does not describe a direct role for DdCAD-1 in regulating gene expression, and full text was not available for verification. Reason: The relevant publication is available only as an abstract, which does not substantiate a molecular role in regulation of gene expression; the documented phenotype is adhesion-driven cell sorting and proportioning. Per policy this experimental annotation is left undecided pending full-text verification rather than removed. |
| GO:0030587 sorocarp development | IMP PMID:12135922 Disruption of the gene encoding the cell adhesion molecule D... | KEEP AS NON CORE | Summary: cadA-null cells complete development but show abnormal slug morphology, delayed culmination, reduced spore yield, and altered cell-type proportioning, implicating DdCAD-1 in normal fruiting-body development. Reason: DdCAD-1 contributes to sorocarp development through its adhesion and cell-sorting activities; a genuine developmental role but downstream of its core molecular function. Supporting Evidence: PMID:12135922 These results indicate that, in addition to cell-cell adhesion, DdCAD-1 plays a role in cell type proportioning and pattern formation |
| GO:0031288 sorocarp morphogenesis | IMP PMID:21561987 The cell adhesion molecule DdCAD-1 regulates morphogenesis t... | KEEP AS NON CORE | Summary: Differential spatiotemporal distribution of DdCAD-1 on prestalk versus prespore cells governs cell sorting in slugs, contributing to morphogenesis of the fruiting body. Reason: DdCAD-1 influences morphogenesis via differential adhesion and sorting; a developmental role downstream of its core adhesion function. Supporting Evidence: PMID:21561987 These results show that DdCAD-1 influences the sorting behavior of cells in slugs by its differential distribution on the prestalk and prespore cells |
| GO:0016339 calcium-dependent cell-cell adhesion | IDA PMID:17057715 Solution structures of the adhesion molecule DdCAD-1 reveal ... | ACCEPT | Summary: Structural and mutational analyses define the Ca2+-bound DdCAD-1 dimer as the molecular basis of calcium-dependent cell-cell adhesion, the core function of the protein. Reason: Direct structural evidence links calcium binding and homophilic dimerization to DdCAD-1-mediated calcium-dependent cell-cell adhesion. Supporting Evidence: PMID:17057715 Our results provide new insights into Ca(2+)-dependent mechanisms for cell-cell adhesion |
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