Medea is the shared Drosophila co-Smad transcription factor for BMP and activin-family signaling. It associates with activated Mad in the BMP branch and with Smox in the activin branch, forming heteromeric complexes that accumulate in the nucleus and regulate target genes. Medea directly contributes to regulatory DNA binding and can support transcriptional activation or Schnurri-dependent repression according to the enhancer context. It shuttles between cytosol and nucleus, with SUMOylation promoting nuclear export. These functions support embryonic dorsal–ventral patterning, imaginal-disc and neural development, stem-cell regulation and synaptic maturation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IDA PMID:12705870 Conversion of an extracellular Dpp/BMP morphogen gradient in... | ACCEPT | Summary: Medea participates in repression of Pol II-transcribed target genes. Reason: Mad/Medea recruits Schnurri at defined silencer elements such as brinker. Direct transcriptional repression in this complex coexists with activation at other regulatory elements; it is not an annotation-sign contradiction. Supporting Evidence: PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0000122 negative regulation of transcription by RNA polymerase II | IDA PMID:17008448 Schnurri transcription factors from Drosophila and vertebrat... | ACCEPT | Summary: Medea participates in repression of Pol II-transcribed target genes. Reason: Mad/Medea recruits Schnurri at defined silencer elements such as brinker. Direct transcriptional repression in this complex coexists with activation at other regulatory elements; it is not an annotation-sign contradiction. Supporting Evidence: PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding | IDA PMID:20010841 A conserved activation element in BMP signaling during Droso... | ACCEPT | Summary: Medea binds cis-regulatory DNA as part of SMAD transcriptional complexes. Reason: The tinman-enhancer study identifies Medea as a DNA-binding factor, and the dad activating-element study demonstrates competitive Mad/Medea DNA binding. The conclusion is based on fly primary data rather than presumed properties of vertebrate SMAD4. Supporting Evidence: PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: Medea binds cis-regulatory DNA as part of SMAD transcriptional complexes. Reason: The tinman-enhancer study identifies Medea as a DNA-binding factor, and the dad activating-element study demonstrates competitive Mad/Medea DNA binding. The conclusion is based on fly primary data rather than presumed properties of vertebrate SMAD4. Supporting Evidence: PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IDA PMID:9694800 Smad proteins act in combination with synergistic and antago... | ACCEPT | Summary: Medea binds cis-regulatory DNA as part of SMAD transcriptional complexes. Reason: The tinman-enhancer study identifies Medea as a DNA-binding factor, and the dad activating-element study demonstrates competitive Mad/Medea DNA binding. The conclusion is based on fly primary data rather than presumed properties of vertebrate SMAD4. Supporting Evidence: PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. |
| GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific | IBA GO_REF:0000033 | ACCEPT | Summary: Medea is a DNA-binding transcription factor with context-dependent activating and repressive roles. Reason: Direct enhancer binding and both activator and repressor complexes support the inherited general transcription-factor activity. Its behavior depends on its R-Smad partners, DNA sequence and additional factors such as Schnurri. Supporting Evidence: PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0001227 DNA-binding transcription repressor activity, RNA polymerase II-specific | IDA PMID:12705870 Conversion of an extracellular Dpp/BMP morphogen gradient in... | ACCEPT | Summary: Medea participates in a DNA-bound transcriptional repressor complex. Reason: The Mad/Medea/Schnurri complex represses brinker from a defined silencer; retain repressor activity without implying that Medea alone is a dedicated repressor. Supporting Evidence: PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0001227 DNA-binding transcription repressor activity, RNA polymerase II-specific | IDA PMID:17008448 Schnurri transcription factors from Drosophila and vertebrat... | ACCEPT | Summary: Medea participates in a DNA-bound transcriptional repressor complex. Reason: The Mad/Medea/Schnurri complex represses brinker from a defined silencer; retain repressor activity without implying that Medea alone is a dedicated repressor. Supporting Evidence: PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific | IDA PMID:20010841 A conserved activation element in BMP signaling during Droso... | ACCEPT | Summary: Medea can activate transcription through BMP-responsive regulatory elements. Reason: Mad/Medea-mediated activation at the dad enhancer and the NMJ motif study establish activating behavior. This is compatible with repression at other targets and does not depend on an assumed universal activation mechanism. Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:36029115 both motifs mediate direct gene activation, with no involvement of the BMP derepression pathway regulators Schnurri and Brinker. |
| GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific | IDA PMID:36029115 Dichotomous cis-regulatory motifs mediate the maturation of ... | ACCEPT | Summary: Medea can activate transcription through BMP-responsive regulatory elements. Reason: Mad/Medea-mediated activation at the dad enhancer and the NMJ motif study establish activating behavior. This is compatible with repression at other targets and does not depend on an assumed universal activation mechanism. Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:36029115 both motifs mediate direct gene activation, with no involvement of the BMP derepression pathway regulators Schnurri and Brinker. |
| GO:0001745 compound eye morphogenesis | IMP PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | KEEP AS NON CORE | Summary: Medea contributes to compound-eye development. Reason: The original gene study establishes later developmental requirements for Dpp signaling, including imaginal tissues; its experimental eye phenotype is retained as a specific developmental output, independently consistent with the eye/glial Dpp functions. Supporting Evidence: PMID:9502733 Loss of Medea also blocks dpp signaling during later development PMID:16176948 gcm is reduced or absent in dpp mutants or Medea clones |
| GO:0005515 protein binding | IPI PMID:15046722 Highwire regulates presynaptic BMP signaling essential for s... | REMOVE | Summary: Highwire binding is real but bare protein binding is uninformative. Reason: The primary directly reports Hiw binding to Medea. Under the protein-binding policy, remove the generic label without denying the interaction; an E3-ligase regulatory or substrate role cannot be inferred solely from this association. Supporting Evidence: PMID:15046722 Here we show that Hiw binds to the Smad protein Medea (Med). |
| GO:0005634 nucleus | EXP PMID:14534137 Stepwise formation of a SMAD activity gradient during dorsal... | ACCEPT | Summary: Medea enters and functions in the nucleus. Reason: Primary localization and signal-dependent Mad association demonstrate nuclear accumulation; SUMO-dependent export shows this is a regulated shuttle rather than an exclusively nuclear protein. All nucleus rows are judged consistently. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:18794353 Med is SUMO modified in the nucleus, and we provide evidence that SUMOylation triggers Med nuclear export. |
| GO:0005634 nucleus | EXP PMID:18794353 Medea SUMOylation restricts the signaling range of the Dpp m... | ACCEPT | Summary: Medea enters and functions in the nucleus. Reason: Primary localization and signal-dependent Mad association demonstrate nuclear accumulation; SUMO-dependent export shows this is a regulated shuttle rather than an exclusively nuclear protein. All nucleus rows are judged consistently. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:18794353 Med is SUMO modified in the nucleus, and we provide evidence that SUMOylation triggers Med nuclear export. |
| GO:0005634 nucleus | IDA PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Medea enters and functions in the nucleus. Reason: Primary localization and signal-dependent Mad association demonstrate nuclear accumulation; SUMO-dependent export shows this is a regulated shuttle rather than an exclusively nuclear protein. All nucleus rows are judged consistently. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:18794353 Med is SUMO modified in the nucleus, and we provide evidence that SUMOylation triggers Med nuclear export. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Medea enters and functions in the nucleus. Reason: Primary localization and signal-dependent Mad association demonstrate nuclear accumulation; SUMO-dependent export shows this is a regulated shuttle rather than an exclusively nuclear protein. All nucleus rows are judged consistently. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:18794353 Med is SUMO modified in the nucleus, and we provide evidence that SUMOylation triggers Med nuclear export. |
| GO:0005634 nucleus | IPI PMID:9502724 Medea is a Drosophila Smad4 homolog that is differentially r... | ACCEPT | Summary: Medea enters and functions in the nucleus. Reason: Primary localization and signal-dependent Mad association demonstrate nuclear accumulation; SUMO-dependent export shows this is a regulated shuttle rather than an exclusively nuclear protein. All nucleus rows are judged consistently. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:18794353 Med is SUMO modified in the nucleus, and we provide evidence that SUMOylation triggers Med nuclear export. |
| GO:0005667 transcription regulator complex | IEA GO_REF:0000002 | MODIFY | Summary: Medea forms heteromeric SMAD and SMAD-containing transcriptional repressor complexes. Reason: The broad transcription regulator complex is correct but the partner-defined assemblies are known. Preserve both the heteromeric SMAD complex and the Schnurri-associated Pol II repressor complex rather than choosing a single regulatory polarity. Proposed replacements: heteromeric SMAD protein complex RNA polymerase II transcription repressor complex Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0005667 transcription regulator complex | IPI PMID:20010841 A conserved activation element in BMP signaling during Droso... | MODIFY | Summary: Medea forms heteromeric SMAD and SMAD-containing transcriptional repressor complexes. Reason: The broad transcription regulator complex is correct but the partner-defined assemblies are known. Preserve both the heteromeric SMAD complex and the Schnurri-associated Pol II repressor complex rather than choosing a single regulatory polarity. Proposed replacements: heteromeric SMAD protein complex RNA polymerase II transcription repressor complex Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0005737 cytoplasm | EXP PMID:14534137 Stepwise formation of a SMAD activity gradient during dorsal... | MODIFY | Summary: Medea occupies the cytosol during its regulated nuclear shuttle. Reason: The cytoplasmic pool is more precisely represented by the experimentally annotated cytosol term. Physical association with Mad promotes nuclear entry, whereas SUMOylation promotes export; no membrane-enclosed cytoplasmic compartment is inferred. Proposed replacements: cytosol Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005737 cytoplasm | EXP PMID:18794353 Medea SUMOylation restricts the signaling range of the Dpp m... | MODIFY | Summary: Medea occupies the cytosol during its regulated nuclear shuttle. Reason: The cytoplasmic pool is more precisely represented by the experimentally annotated cytosol term. Physical association with Mad promotes nuclear entry, whereas SUMOylation promotes export; no membrane-enclosed cytoplasmic compartment is inferred. Proposed replacements: cytosol Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005737 cytoplasm | EXP PMID:9502724 Medea is a Drosophila Smad4 homolog that is differentially r... | MODIFY | Summary: Medea occupies the cytosol during its regulated nuclear shuttle. Reason: The cytoplasmic pool is more precisely represented by the experimentally annotated cytosol term. Physical association with Mad promotes nuclear entry, whereas SUMOylation promotes export; no membrane-enclosed cytoplasmic compartment is inferred. Proposed replacements: cytosol Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005737 cytoplasm | EXP PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | MODIFY | Summary: Medea occupies the cytosol during its regulated nuclear shuttle. Reason: The cytoplasmic pool is more precisely represented by the experimentally annotated cytosol term. Physical association with Mad promotes nuclear entry, whereas SUMOylation promotes export; no membrane-enclosed cytoplasmic compartment is inferred. Proposed replacements: cytosol Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005737 cytoplasm | HDA PMID:26896675 A genome-wide resource for the analysis of protein localisat... | MODIFY | Summary: Medea occupies the cytosol during its regulated nuclear shuttle. Reason: The cytoplasmic pool is more precisely represented by the experimentally annotated cytosol term. Physical association with Mad promotes nuclear entry, whereas SUMOylation promotes export; no membrane-enclosed cytoplasmic compartment is inferred. Proposed replacements: cytosol Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Medea occupies the cytosol during its regulated nuclear shuttle. Reason: The cytoplasmic pool is more precisely represented by the experimentally annotated cytosol term. Physical association with Mad promotes nuclear entry, whereas SUMOylation promotes export; no membrane-enclosed cytoplasmic compartment is inferred. Proposed replacements: cytosol Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005829 cytosol | IDA PMID:9502724 Medea is a Drosophila Smad4 homolog that is differentially r... | ACCEPT | Summary: Medea has a soluble cytosolic pool. Reason: Original localization experiments place Medea in the cytoplasm/cytosol and show partner-dependent nuclear translocation. This location is compatible with its nuclear activity. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0005829 cytosol | IDA PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Medea has a soluble cytosolic pool. Reason: Original localization experiments place Medea in the cytoplasm/cytosol and show partner-dependent nuclear translocation. This location is compatible with its nuclear activity. Supporting Evidence: PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | MODIFY | Summary: Medea both activates and represses Pol II-dependent transcription. Reason: Refine the broad transcription-regulation terms to the two supported polarities. Mad/Medea activates specific enhancers and represses other targets through Schnurri; neither polarity should be discarded. Proposed replacements: positive regulation of transcription by RNA polymerase II negative regulation of transcription by RNA polymerase II Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0006357 regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | MODIFY | Summary: Medea both activates and represses Pol II-dependent transcription. Reason: Refine the broad transcription-regulation terms to the two supported polarities. Mad/Medea activates specific enhancers and represses other targets through Schnurri; neither polarity should be discarded. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000344419 SUPPORTS TRANSFER The ancestral node is traced from the seeded supporting entities. No target-specific loss or erroneous node placement is claimed; the inherited broad function is refined using target-specific evidence. Proposed replacements: positive regulation of transcription by RNA polymerase II negative regulation of transcription by RNA polymerase II Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0007476 imaginal disc-derived wing morphogenesis | IMP PMID:11290719 Transgenic analysis of the Smad family of TGF-beta signal tr... | KEEP AS NON CORE | Summary: Medea contributes to imaginal-disc-derived wing morphogenesis. Reason: The original Medea study directly describes a wing-primordium phenotype; this independently supports the developmental role in the transgenic annotation. Supporting Evidence: PMID:9502724 In the wing primordium, loss of Medea most severely affects regions receiving low DPP signal. |
| GO:0007480 imaginal disc-derived leg morphogenesis | IMP PMID:11290719 Transgenic analysis of the Smad family of TGF-beta signal tr... | UNDECIDED | Summary: The precise Medea leg-morphogenesis phenotype needs full-text confirmation. Reason: The available transgenic-study abstract does not expose the Medea-specific leg assay. General imaginal-disc signaling function is insufficient to resolve this precise organ annotation. No wrong-gene attribution is alleged. |
| GO:0007507 heart development | TAS PMID:10973066 Genetics of heart development. | KEEP AS NON CORE | Summary: Medea participates in the Dpp-dependent cardiac developmental program. Reason: Primary analysis of the tinman enhancer establishes direct Medea-dependent transcription in dorsal mesoderm, the developmental field that includes the heart. The review-supported cardiac outcome is retained as a contextual function rather than the core shared-Smad activity. Supporting Evidence: PMID:9694800 induction of visceral mesoderm, dorsal muscles, and the heart by Dpp is, at least in part, effected through the transcriptional activation and function of the homeobox gene tinman PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. |
| GO:0007507 heart development | TAS PMID:12027431 Control of cardiac development by an evolutionarily conserve... | KEEP AS NON CORE | Summary: Medea participates in the Dpp-dependent cardiac developmental program. Reason: Primary analysis of the tinman enhancer establishes direct Medea-dependent transcription in dorsal mesoderm, the developmental field that includes the heart. The review-supported cardiac outcome is retained as a contextual function rather than the core shared-Smad activity. Supporting Evidence: PMID:9694800 induction of visceral mesoderm, dorsal muscles, and the heart by Dpp is, at least in part, effected through the transcriptional activation and function of the homeobox gene tinman PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. |
| GO:0009653 anatomical structure morphogenesis | IBA GO_REF:0000033 | MODIFY | Summary: Resolved morphogenetic outputs include wing and compound-eye development. Reason: Refine the broad anatomical-structure morphogenesis assertion to the experimentally documented developmental contexts already annotated. This does not restrict the shared co-Smad to activin alone. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000344419 SUPPORTS TRANSFER The ancestral node is traced from the seeded supporting entities. No target-specific loss or erroneous node placement is claimed; the inherited broad function is refined using target-specific evidence. Proposed replacements: imaginal disc-derived wing morphogenesis compound eye morphogenesis Supporting Evidence: PMID:9502724 In the wing primordium, loss of Medea most severely affects regions receiving low DPP signal. PMID:16176948 gcm is reduced or absent in dpp mutants or Medea clones |
| GO:0009791 post-embryonic development | IEA GO_REF:0000117 | MODIFY | Summary: A documented post-embryonic output is wing morphogenesis. Reason: Replace the broad developmental-stage assertion with the independently established wing-primordium phenotype. Proposed replacements: imaginal disc-derived wing morphogenesis Supporting Evidence: PMID:9502724 In the wing primordium, loss of Medea most severely affects regions receiving low DPP signal. |
| GO:0009950 dorsal/ventral axis specification | IMP PMID:9502722 The Drosophila Medea gene is required downstream of dpp and ... | KEEP AS NON CORE | Summary: Medea is required for embryonic dorsal–ventral specification and patterning. Reason: Maternal/zygotic genetic loss produces ventralization and prevents dorsal-fate induction downstream of activated Tkv. These precise developmental outputs are retained separately from the core transcriptional mechanism. Supporting Evidence: PMID:9502722 Complete elimination of maternal and zygotic Medea activity in the early embryo results in a ventralized phenotype identical to that of null dpp mutants |
| GO:0009953 dorsal/ventral pattern formation | IMP PMID:9502724 Medea is a Drosophila Smad4 homolog that is differentially r... | KEEP AS NON CORE | Summary: Medea is required for embryonic dorsal–ventral specification and patterning. Reason: Maternal/zygotic genetic loss produces ventralization and prevents dorsal-fate induction downstream of activated Tkv. These precise developmental outputs are retained separately from the core transcriptional mechanism. Supporting Evidence: PMID:9502722 Complete elimination of maternal and zygotic Medea activity in the early embryo results in a ventralized phenotype identical to that of null dpp mutants |
| GO:0009953 dorsal/ventral pattern formation | IMP PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | KEEP AS NON CORE | Summary: Medea is required for embryonic dorsal–ventral specification and patterning. Reason: Maternal/zygotic genetic loss produces ventralization and prevents dorsal-fate induction downstream of activated Tkv. These precise developmental outputs are retained separately from the core transcriptional mechanism. Supporting Evidence: PMID:9502722 Complete elimination of maternal and zygotic Medea activity in the early embryo results in a ventralized phenotype identical to that of null dpp mutants |
| GO:0030154 cell differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Medea-dependent transcription contributes to cell differentiation in several developmental settings. Reason: The co-Smad regulates different cell-fate programs, including dorsal mesoderm and lamina glia. Cell differentiation is retained as the general common outcome across these settings, rather than asserting one cell type encompasses all Medea functions. Supporting Evidence: PMID:16176948 DPP signaling mediates the maturation of the lamina glia required for the correct R axon projection pattern by controlling the expression of gcm. |
| GO:0030509 BMP signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:11071761 The zinc finger protein schnurri acts as a Smad partner in m... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:12705870 Conversion of an extracellular Dpp/BMP morphogen gradient in... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:17008448 Schnurri transcription factors from Drosophila and vertebrat... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:18588885 Specificity of the inhibitory effects of Dad on TGF-beta fam... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:20010841 A conserved activation element in BMP signaling during Droso... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:36029115 Dichotomous cis-regulatory motifs mediate the maturation of ... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IDA PMID:9693372 Interplay of signal mediators of decapentaplegic (Dpp): mole... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IGI PMID:7705627 Genetic screens to identify elements of the decapentaplegic ... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IGI PMID:9502722 The Drosophila Medea gene is required downstream of dpp and ... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IGI PMID:9502722 The Drosophila Medea gene is required downstream of dpp and ... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IGI PMID:9502722 The Drosophila Medea gene is required downstream of dpp and ... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IGI PMID:9502724 Medea is a Drosophila Smad4 homolog that is differentially r... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IGI PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IMP PMID:15046722 Highwire regulates presynaptic BMP signaling essential for s... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IMP PMID:22745309 Fat facets deubiquitylation of Medea/Smad4 modulates interpr... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IMP PMID:40955849 Drosophila Dpp and BMP signaling directly regulates dpp tran... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IMP PMID:8702167 Characterization of Medea, a gene required for maximal funct... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030509 BMP signaling pathway | IMP PMID:9502722 The Drosophila Medea gene is required downstream of dpp and ... | ACCEPT | Summary: Medea is the shared co-Smad transcriptional effector of BMP signaling. Reason: Mad-dependent association, nuclear translocation, enhancer binding and genetic loss independently establish a core Dpp/BMP role. Studies of morphogen dosage, SUMO/ubiquitin regulation, transcriptional elements and tissue outputs support that same function. Activin participation does not make these BMP annotations non-core. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9502724 MEDEA is localized in the cytoplasm, is not regulated by phosphorylation, and requires physical association with MAD for nuclear translocation. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0030707 follicle cell of egg chamber development | IMP PMID:16256740 BMP signaling is required for controlling somatic stem cell ... | KEEP AS NON CORE | Summary: Medea-dependent BMP signaling regulates ovarian somatic stem-cell maintenance and follicle-lineage development. Reason: The primary stem-cell study establishes a direct BMP requirement in somatic stem-cell self-renewal and division, with effects on their differentiated follicle lineage. This is a tissue-specific developmental output of the co-Smad. Supporting Evidence: PMID:16256740 BMP signaling is required in SSCs to directly control their maintenance and division, but is dispensable for proliferation of their differentiated progeny. |
| GO:0030718 germ-line stem cell population maintenance | IMP PMID:9695953 decapentaplegic is essential for the maintenance and divisio... | UNDECIDED | Summary: The exact Medea assay for female germline stem-cell maintenance/division needs verification. Reason: The available PMID:9695953 abstract describes Dpp and Saxophone and does not expose a Medea-specific assay. Moreover, PMID:9502724 distinguishes dispensability of Medea during oogenesis from essential Mad functions, so precise stage/endpoint context matters. This is not sufficient to reject the curated stem-cell claim; retain uncertainty rather than equating all oogenesis with stem-cell maintenance. |
| GO:0031290 retinal ganglion cell axon guidance | IMP PMID:16176948 DPP signaling controls development of the lamina glia requir... | KEEP AS NON CORE | Summary: Medea-dependent Dpp signaling in lamina glia supports retinal axon targeting. Reason: The primary identifies Medea mutant clones with reduced glial differentiation markers and impaired retinal axon projection. This is a non-autonomous glial contribution to guidance, not a claim that Medea is a secreted guidance cue. Supporting Evidence: PMID:16176948 gcm is reduced or absent in dpp mutants or Medea clones PMID:16176948 DPP signaling mediates the maturation of the lamina glia required for the correct R axon projection pattern by controlling the expression of gcm. |
| GO:0032924 activin receptor signaling pathway | IDA PMID:10320478 Drosophila dSmad2 and Atr-I transmit activin/TGFbeta signals... | ACCEPT | Summary: Medea also transduces activin-family signals with Smox. Reason: Receptor-dependent Smox phosphorylation induces Smox–Medea heteromeric complexes. This activin role coexists with the canonical Mad/Medea BMP role; Medea is not an activin-exclusive family member. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0032924 activin receptor signaling pathway | IDA PMID:9887103 The Drosophila activin receptor baboon signals through dSmad... | ACCEPT | Summary: Medea also transduces activin-family signals with Smox. Reason: Receptor-dependent Smox phosphorylation induces Smox–Medea heteromeric complexes. This activin role coexists with the canonical Mad/Medea BMP role; Medea is not an activin-exclusive family member. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0035019 somatic stem cell population maintenance | IMP PMID:16256740 BMP signaling is required for controlling somatic stem cell ... | KEEP AS NON CORE | Summary: Medea-dependent BMP signaling regulates ovarian somatic stem-cell maintenance and follicle-lineage development. Reason: The primary stem-cell study establishes a direct BMP requirement in somatic stem-cell self-renewal and division, with effects on their differentiated follicle lineage. This is a tissue-specific developmental output of the co-Smad. Supporting Evidence: PMID:16256740 BMP signaling is required in SSCs to directly control their maintenance and division, but is dispensable for proliferation of their differentiated progeny. |
| GO:0042078 germ-line stem cell division | IMP PMID:9695953 decapentaplegic is essential for the maintenance and divisio... | UNDECIDED | Summary: The exact Medea assay for female germline stem-cell maintenance/division needs verification. Reason: The available PMID:9695953 abstract describes Dpp and Saxophone and does not expose a Medea-specific assay. Moreover, PMID:9502724 distinguishes dispensability of Medea during oogenesis from essential Mad functions, so precise stage/endpoint context matters. This is not sufficient to reject the curated stem-cell claim; retain uncertainty rather than equating all oogenesis with stem-cell maintenance. |
| GO:0045705 negative regulation of salivary gland boundary specification | TAS PMID:11598957 Organ formation in Drosophila: specification and morphogenes... | UNDECIDED | Summary: The precise negative regulation of the salivary-gland boundary is not resolved. Reason: The cached review abstract discusses organ formation broadly but does not expose the Medea-specific evidence or regulatory sign. General BMP pathway function cannot settle this narrow annotation. The original curator attribution is not declared erroneous. |
| GO:0045887 positive regulation of synaptic assembly at neuromuscular junction | IMP PMID:15046722 Highwire regulates presynaptic BMP signaling essential for s... | KEEP AS NON CORE | Summary: Medea-dependent presynaptic BMP signaling promotes NMJ assembly/growth. Reason: The primary identifies Medea in the presynaptic BMP cascade and shows that pathway mutants reduce NMJ size and transmission. This is a specific synaptic developmental output, not a general synaptic assembly activity of the protein. Supporting Evidence: PMID:15046722 Med is part of a presynaptic bone morphogenetic protein (BMP) signaling cascade consisting of three receptor subunits, Wit, Tkv, and Sax, in addition to the Smad transcription factor Mad. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:10320478 Drosophila dSmad2 and Atr-I transmit activin/TGFbeta signals... | ACCEPT | Summary: Medea-containing complexes can activate Pol II-dependent transcription. Reason: Direct activator-element recognition and promoter induction establish positive transcriptional regulation. Repression through Schnurri occurs at other elements and does not contradict these activating functions. Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:11071761 The zinc finger protein schnurri acts as a Smad partner in m... | ACCEPT | Summary: Medea-containing complexes can activate Pol II-dependent transcription. Reason: Direct activator-element recognition and promoter induction establish positive transcriptional regulation. Repression through Schnurri occurs at other elements and does not contradict these activating functions. Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:20010841 A conserved activation element in BMP signaling during Droso... | ACCEPT | Summary: Medea-containing complexes can activate Pol II-dependent transcription. Reason: Direct activator-element recognition and promoter induction establish positive transcriptional regulation. Repression through Schnurri occurs at other elements and does not contradict these activating functions. Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IMP PMID:9694800 Smad proteins act in combination with synergistic and antago... | ACCEPT | Summary: Medea-containing complexes can activate Pol II-dependent transcription. Reason: Direct activator-element recognition and promoter induction establish positive transcriptional regulation. Repression through Schnurri occurs at other elements and does not contradict these activating functions. Supporting Evidence: PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. |
| GO:0048639 positive regulation of developmental growth | IEA GO_REF:0000117 | MODIFY | Summary: A specific positive developmental output is neuromuscular synaptic assembly. Reason: Refine the broad developmental-growth claim to the experimentally annotated positive regulation of synaptic assembly at the NMJ. Other developmental phenotypes are separately retained rather than inferred from a generic growth statement. Proposed replacements: positive regulation of synaptic assembly at neuromuscular junction Supporting Evidence: PMID:15046722 Med is part of a presynaptic bone morphogenetic protein (BMP) signaling cascade consisting of three receptor subunits, Wit, Tkv, and Sax, in addition to the Smad transcription factor Mad. |
| GO:0048666 neuron development | IMP PMID:16437159 Baboon/dSmad2 TGF-beta signaling is required during late lar... | KEEP AS NON CORE | Summary: Medea participates in activin-associated neuronal development. Reason: The co-Smad provides a transcriptional partner for Smox in the neural developmental pathway. The original study is not rejected because its title foregrounds Babo/dSmad2; the annotation is retained as a contextual developmental role. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:16437159 We found that Baboon(Babo)/dSmad2-mediated TGF-beta signaling, known to be essential for remodeling of larval functional neurons, is also indispensable for proper morphogenesis of these adult-specific neurons. |
| GO:0051240 positive regulation of multicellular organismal process | IEA GO_REF:0000117 | MODIFY | Summary: The supported positive multicellular output is NMJ synaptic assembly. Reason: The generic organismal-process label is refined to a specific curated output supported by the presynaptic BMP study. Proposed replacements: positive regulation of synaptic assembly at neuromuscular junction Supporting Evidence: PMID:15046722 Med is part of a presynaptic bone morphogenetic protein (BMP) signaling cascade consisting of three receptor subunits, Wit, Tkv, and Sax, in addition to the Smad transcription factor Mad. |
| GO:0060395 SMAD protein signal transduction | IBA GO_REF:0000033 | ACCEPT | Summary: Medea directly participates in SMAD signal transduction. Reason: Medea is a signal-responsive partner that assembles with R-Smads, enters the nucleus and contributes to regulatory DNA recognition. It is neither an R-Smad kinase nor an inert downstream substrate. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. |
| GO:0060395 SMAD protein signal transduction | IDA PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Medea directly participates in SMAD signal transduction. Reason: Medea is a signal-responsive partner that assembles with R-Smads, enters the nucleus and contributes to regulatory DNA recognition. It is neither an R-Smad kinase nor an inert downstream substrate. Supporting Evidence: PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:20010841 activating input by the Smad signal transducers Mothers against Dpp (Mad) and Medea via competitive DNA binding. |
| GO:0070411 I-SMAD binding | IBA GO_REF:0000033 | UNDECIDED | Summary: Direct Medea binding to an inhibitory SMAD remains unverified. Reason: The inspected fly primary evidence establishes Mad/Smox binding and Dad effects on receptor/R-Smad signaling, but does not establish a direct Medea–Dad interaction. The inherited assertion is not rejected on the basis of missing target evidence and no lineage-specific loss is claimed. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000344419 UNRESOLVED The ancestral node is traced from the seeded supporting entities. No target-specific loss or erroneous node placement is claimed; the target evidence remains insufficient to adjudicate this function. |
| GO:0071144 heteromeric SMAD protein complex | IBA GO_REF:0000033 | ACCEPT | Summary: Medea forms heteromeric complexes with the R-Smads Mad and Smox. Reason: Independent biochemical evidence establishes both BMP and activin R-Smad complexes. The shared co-Smad function does not imply that all complexes have identical stoichiometry, DNA targets or regulatory polarity. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0071144 heteromeric SMAD protein complex | IDA PMID:9693372 Interplay of signal mediators of decapentaplegic (Dpp): mole... | ACCEPT | Summary: Medea forms heteromeric complexes with the R-Smads Mad and Smox. Reason: Independent biochemical evidence establishes both BMP and activin R-Smad complexes. The shared co-Smad function does not imply that all complexes have identical stoichiometry, DNA targets or regulatory polarity. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0071144 heteromeric SMAD protein complex | IPI PMID:10320478 Drosophila dSmad2 and Atr-I transmit activin/TGFbeta signals... | ACCEPT | Summary: Medea forms heteromeric complexes with the R-Smads Mad and Smox. Reason: Independent biochemical evidence establishes both BMP and activin R-Smad complexes. The shared co-Smad function does not imply that all complexes have identical stoichiometry, DNA targets or regulatory polarity. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0071144 heteromeric SMAD protein complex | IPI PMID:18588885 Specificity of the inhibitory effects of Dad on TGF-beta fam... | ACCEPT | Summary: Medea forms heteromeric complexes with the R-Smads Mad and Smox. Reason: Independent biochemical evidence establishes both BMP and activin R-Smad complexes. The shared co-Smad function does not imply that all complexes have identical stoichiometry, DNA targets or regulatory polarity. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0071144 heteromeric SMAD protein complex | IPI PMID:9502724 Medea is a Drosophila Smad4 homolog that is differentially r... | ACCEPT | Summary: Medea forms heteromeric complexes with the R-Smads Mad and Smox. Reason: Independent biochemical evidence establishes both BMP and activin R-Smad complexes. The shared co-Smad function does not imply that all complexes have identical stoichiometry, DNA targets or regulatory polarity. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0071144 heteromeric SMAD protein complex | IPI PMID:9887103 The Drosophila activin receptor baboon signals through dSmad... | ACCEPT | Summary: Medea forms heteromeric complexes with the R-Smads Mad and Smox. Reason: Independent biochemical evidence establishes both BMP and activin R-Smad complexes. The shared co-Smad function does not imply that all complexes have identical stoichiometry, DNA targets or regulatory polarity. Supporting Evidence: PMID:10320478 dSMAD2 complexes with MEDEA only in the presence of ATR-I and PUNT. PMID:9502724 MEDEA is most similar to mammalian Smad4 and forms heteromeric complexes with MAD. PMID:9887103 Activated Babo associates with dSmad2 but not Mad, phosphorylates the carboxy-terminal SSXS motif and induces heteromeric complex formation with Medea, the Drosophila Smad4 homolog. |
| GO:0090571 RNA polymerase II transcription repressor complex | IPI PMID:12705870 Conversion of an extracellular Dpp/BMP morphogen gradient in... | ACCEPT | Summary: Medea participates in the SMAD/Schnurri transcriptional repressor complex. Reason: The brinker silencer recruits a defined Mad/Medea/Schnurri assembly that produces transcriptional repression. This complex-specific function is retained alongside activating assemblies. Supporting Evidence: PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0090571 RNA polymerase II transcription repressor complex | IPI PMID:17008448 Schnurri transcription factors from Drosophila and vertebrat... | ACCEPT | Summary: Medea participates in the SMAD/Schnurri transcriptional repressor complex. Reason: The brinker silencer recruits a defined Mad/Medea/Schnurri assembly that produces transcriptional repression. This complex-specific function is retained alongside activating assemblies. Supporting Evidence: PMID:12705870 the brk silencer serves as a direct target for a protein complex consisting of the Smad homologs Mad/Medea and the zinc finger protein Schnurri. |
| GO:0160108 animal gross anatomical part developmental process | IEA GO_REF:0000117 | MODIFY | Summary: The resolved anatomical developmental outputs include eye, wing and heart development. Reason: Replace the broad animal-part developmental term with supported organ-level roles. The co-Smad is pleiotropic, so several specific outputs are retained. Proposed replacements: compound eye morphogenesis imaginal disc-derived wing morphogenesis heart development Supporting Evidence: PMID:9502724 In the wing primordium, loss of Medea most severely affects regions receiving low DPP signal. PMID:16176948 gcm is reduced or absent in dpp mutants or Medea clones PMID:9694800 Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. |
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Download this section (compressed HTML)Medea (Med) encodes a protein that belongs to the highly conserved Smad family. It can bind its siblings encoded by Mad or Smox to facilitate signal transduction for the product of dpp or Activin ligands in the TGF-beta family. Med-complexes function as transcriptional regulators. Many developmental roles include dorsal-ventral patterning, patterning and proliferation of the wing disc and gene expression in the mushroom body of the larval brain.
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