MEK-1 is the MAP kinase kinase of the Neurospora crassa MIK-1βMEK-1βMAK-1 signaling module. It is required for MAK-1 phosphorylation and helps control cell wall integrity, vegetative growth, asexual development and sexual differentiation. MEK-1 also accumulates at the contact sites of fusing germlings, linking this signaling module to local remodeling during cell fusion.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000165 MAPK cascade | IEA GO_REF:0000117 | ACCEPT | Summary: MEK-1 is the middle kinase of the experimentally characterized MIK-1βMEK-1βMAK-1 cascade. Reason: MEK-1 is the middle kinase of the experimentally characterized MIK-1βMEK-1βMAK-1 cascade. The broad MAPK cascade annotation is correct but less informative than the cell integrity cascade assignment. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0000166 nucleotide binding | IEA GO_REF:0000104 | ACCEPT | Summary: The protein kinase ATP-binding site and active catalytic domain support ATP-dependent phosphotransfer. Reason: The protein kinase ATP-binding site and active catalytic domain support ATP-dependent phosphotransfer. Nucleotide binding is broad but true for this kinase. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0000196 cell integrity MAPK cascade | IBA GO_REF:0000033 | ACCEPT | Summary: Primary Neurospora experiments identify MEK-1 as the MAPKK upstream of MAK-1 and show loss of MAK-1 phosphorylation in the deletion mutant. Reason: Primary Neurospora experiments identify MEK-1 as the MAPKK upstream of MAK-1 and show loss of MAK-1 phosphorylation in the deletion mutant. The MIK-1βMEK-1βMAK-1 module regulates fungal development and cell wall integrity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0000196 cell integrity MAPK cascade | IEA GO_REF:0000107 | ACCEPT | Summary: Primary Neurospora experiments identify MEK-1 as the MAPKK upstream of MAK-1 and show loss of MAK-1 phosphorylation in the deletion mutant. Reason: Primary Neurospora experiments identify MEK-1 as the MAPKK upstream of MAK-1 and show loss of MAK-1 phosphorylation in the deletion mutant. The MIK-1βMEK-1βMAK-1 module regulates fungal development and cell wall integrity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0000935 division septum | IEA GO_REF:0000107 | UNDECIDED | Summary: The direct microscopy study locates MEK-1 at contacts between fusing germlings, which is not equivalent to a division septum. Reason: The direct microscopy study locates MEK-1 at contacts between fusing germlings, which is not equivalent to a division septum. The fission-yeast ortholog transfer may be valid, but a target-specific septal localization or convincing conservation of that precise pattern remains unresolved. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0004672 protein kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. Reason: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. These broad kinase or transferase terms are correct; MAP kinase kinase activity states the biological specificity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0004674 protein serine/threonine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. Reason: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. These broad kinase or transferase terms are correct; MAP kinase kinase activity states the biological specificity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0004707 MAP kinase activity | IEA GO_REF:0000003 | MODIFY | Summary: The EC-derived row calls MEK-1 a MAP kinase, but primary experiments distinguish MEK-1 (MAPKK) from its downstream MAPK MAK-1. Reason: The EC-derived row calls MEK-1 a MAP kinase, but primary experiments distinguish MEK-1 (MAPKK) from its downstream MAPK MAK-1. GO:0004708 captures phosphorylation of a MAPK substrate, the appropriate kinase tier for this protein. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0004708 MAP kinase kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: MEK-1 is the MAP kinase kinase, and MAK-1 phosphorylation depends on it in Neurospora. Reason: MEK-1 is the MAP kinase kinase, and MAK-1 phosphorylation depends on it in Neurospora. The target kinase-domain architecture and MAPKK phylogenetic placement agree with this pathway position. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0004708 MAP kinase kinase activity | IEA GO_REF:0000107 | ACCEPT | Summary: MEK-1 is the MAP kinase kinase, and MAK-1 phosphorylation depends on it in Neurospora. Reason: MEK-1 is the MAP kinase kinase, and MAK-1 phosphorylation depends on it in Neurospora. The target kinase-domain architecture and MAPKK phylogenetic placement agree with this pathway position. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: The protein kinase ATP-binding site and active catalytic domain support ATP-dependent phosphotransfer. Reason: The protein kinase ATP-binding site and active catalytic domain support ATP-dependent phosphotransfer. Nucleotide binding is broad but true for this kinase. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: The conserved fungal MAPKK localization inference is compatible with direct Neurospora microscopy showing MEK-1 recruitment to germling contact sites. Reason: The conserved fungal MAPKK localization inference is compatible with direct Neurospora microscopy showing MEK-1 recruitment to germling contact sites. Cytoplasm is a broad compartment that includes this cortical signaling pool; the experiment does not imply uniform distribution. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0016301 kinase activity | IEA GO_REF:0000104 | ACCEPT | Summary: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. Reason: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. These broad kinase or transferase terms are correct; MAP kinase kinase activity states the biological specificity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0016740 transferase activity | IEA GO_REF:0000104 | ACCEPT | Summary: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. Reason: The conserved catalytic protein kinase domain and experimentally established MAPKK function support phosphorylation activity. These broad kinase or transferase terms are correct; MAP kinase kinase activity states the biological specificity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0050850 positive regulation of calcium-mediated signaling | IEA GO_REF:0000107 | UNDECIDED | Summary: The transferred positive regulation of calcium-mediated signaling is more specific than the demonstrated cell integrity MAPK cascade. Reason: The transferred positive regulation of calcium-mediated signaling is more specific than the demonstrated cell integrity MAPK cascade. Calcium-sensitive fusion phenotypes or downstream CSR-3 behavior do not establish that MEK-1 positively regulates calcium signaling itself. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
| GO:0060237 regulation of fungal-type cell wall organization | IBA GO_REF:0000033 | ACCEPT | Summary: Primary Neurospora experiments identify MEK-1 as the MAPKK upstream of MAK-1 and show loss of MAK-1 phosphorylation in the deletion mutant. Reason: Primary Neurospora experiments identify MEK-1 as the MAPKK upstream of MAK-1 and show loss of MAK-1 phosphorylation in the deletion mutant. The MIK-1βMEK-1βMAK-1 module regulates fungal development and cell wall integrity. Supporting Evidence: PMID:18849472 The MAK-1 MAPK was not phosphorylated in Ξ mik-1 and Ξ mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. PMID:41071819 In a first step, we confirmed the accumulation of the kinase MAK-1 at the contact sites and showed the same localization pattern for both its upstream kinases (Fig 7). |
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