KRIT1/CCM1 is a multidomain scaffold and Rap1 effector that organizes endothelial cell junctions and vascular signaling. Its N-terminal interaction motifs, ankyrin repeats and C-terminal FERM domain couple CCM-complex partners, integrin regulation, microtubule association and membrane recruitment. It supports vascular barrier integrity and endothelial polarity and restrains excessive angiogenic signaling. Human loss-of-function variants cause cerebral cavernous malformations.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001937 negative regulation of endothelial cell proliferation | IMP PMID:20616044 Cerebral cavernous malformation protein CCM1 inhibits sprout... | KEEP AS NON CORE | Summary: Human endothelial perturbation supports this antiangiogenic/developmental regulatory effect. Reason: CCM1 perturbation directly changes endothelial proliferation, migration, apoptosis and sprouting in primary human endothelial cells. These are documented consequences of the junctional signaling regulator. Broad developmental-process annotations are retained as non-core; they do not identify a distinct enzyme function or germline piRNA mechanism. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0003158 endothelium development | NAS PMID:17657516 CCM3 interacts with CCM2 indicating common pathogenesis for ... | KEEP AS NON CORE | Summary: Vascular developmental regulation is supported by the CCM1 scaffold mechanism. Reason: KRIT1 regulates endothelial organization and quiescence, with experimental vascular-development phenotypes. The generic developmental/regulatory term is compatible but less informative than the endothelial-junction and angiogenesis mechanisms. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0005515 protein binding | IPI PMID:16037064 CCM1 and CCM2 protein interactions in cell signaling: implic... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:16037064 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:17657516 CCM3 interacts with CCM2 indicating common pathogenesis for ... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:17657516 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:17916086 Krit 1 interactions with microtubules and membranes are regu... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:17916086 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:17916086 Krit 1 interactions with microtubules and membranes are regu... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:17916086 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:20332120 CCM1 regulates vascular-lumen organization by inducing endot... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:20332120 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:23007647 Structural basis of the junctional anchorage of the cerebral... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:23007647 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:23007647 Structural basis of the junctional anchorage of the cerebral... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:23007647 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:25525273 Structural basis for the disruption of the cerebral cavernou... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:25525273 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:25814554 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:25814554 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:25910212 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:25910212 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:26780829 Heart of glass anchors Rasip1 at endothelial cell-cell junct... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:26780829 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:27027284 Cerebral cavernous malformations arise from endothelial gain... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:27027284 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:32296183 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:33961781 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:33961781 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:33961781 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: Retain the curated interaction as a non-core observation rather than generic core binding. Reason: The IPI row from PMID:40205054 records a physical interaction. KRIT1 has a defined scaffold/Rap1-effector role, but generic protein binding does not establish the function of every partner. No interaction is rejected because a title foregrounds another protein. |
| GO:0005546 phosphatidylinositol-4,5-bisphosphate binding | IDA PMID:17916086 Krit 1 interactions with microtubules and membranes are regu... | ACCEPT | Summary: KRIT1 binds PIP2-containing membranes. Reason: The primary sedimentation/liposome study demonstrates PIP2-liposome association enhanced by Rap1. This directly supports the lipid-binding activity within its membrane-recruitment mechanism. Supporting Evidence: PMID:17916086 Krit1 binds to phosphatidylinositol 4,5-P(2)-containing liposomes |
| GO:0005576 extracellular region | HDA PMID:22664934 Comparison of tear protein levels in breast cancer patients ... | KEEP AS NON CORE | Summary: Retain extracellular proteomics detection as a non-core observation. Reason: The HDA source records detection outside cells. KRIT1 is principally an intracellular scaffold; this observation alone does not establish a secreted physiological function. Detection is retained without inferring a secretion mechanism. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | ACCEPT | Summary: Microtubule association contributes to KRIT1 spatial regulation. Reason: In vitro binding and cellular localization demonstrate microtubule association, and Rap1/ICAP1 alter that association. This is a mechanistic localization/binding property of the scaffold rather than evidence of a microtubule motor. Supporting Evidence: PMID:17916086 Krit1 binds in vitro to microtubules through its N- and C-termini |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:0005886 plasma membrane | IDA PMID:17916086 Krit 1 interactions with microtubules and membranes are regu... | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:0005911 cell-cell junction | IDA PMID:20332120 CCM1 regulates vascular-lumen organization by inducing endot... | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:0005911 cell-cell junction | IDA PMID:23007647 Structural basis of the junctional anchorage of the cerebral... | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:0007264 small GTPase-mediated signal transduction | TAS PMID:9285558 Association of Krev-1/rap1a with Krit1, a novel ankyrin repe... | ACCEPT | Summary: KRIT1 is a direct Rap1 effector in small-GTPase signaling. Reason: The GTP-dependent Rap1 interaction and structure-guided mutagenesis establish direct participation in the signaling mechanism, without implying intrinsic GTPase catalytic activity. Supporting Evidence: PMID:21633110 native KRIT1 protein binds the effector loop of Rap1A but not H-Ras in a GTP-dependent manner |
| GO:0008017 microtubule binding | IBA GO_REF:0000033 | ACCEPT | Summary: Microtubule association contributes to KRIT1 spatial regulation. Reason: In vitro binding and cellular localization demonstrate microtubule association, and Rap1/ICAP1 alter that association. This is a mechanistic localization/binding property of the scaffold rather than evidence of a microtubule motor. Supporting Evidence: PMID:17916086 Krit1 binds in vitro to microtubules through its N- and C-termini |
| GO:0008017 microtubule binding | IDA PMID:17916086 Krit 1 interactions with microtubules and membranes are regu... | ACCEPT | Summary: Microtubule association contributes to KRIT1 spatial regulation. Reason: In vitro binding and cellular localization demonstrate microtubule association, and Rap1/ICAP1 alter that association. This is a mechanistic localization/binding property of the scaffold rather than evidence of a microtubule motor. Supporting Evidence: PMID:17916086 Krit1 binds in vitro to microtubules through its N- and C-termini |
| GO:0009948 anterior/posterior axis specification | IBA GO_REF:0000033 | UNDECIDED | Summary: The anterior/posterior-axis IBA requires direct assessment of the ancestral developmental evidence. Reason: Vascular morphogenesis and polarity evidence do not by themselves establish anterior/posterior axis specification. The PAINT assertion is a curated phylogenetic judgment and is not rejected, but the pertinent developmental evidence has not been resolved in this review. |
| GO:0010596 negative regulation of endothelial cell migration | IMP PMID:20616044 Cerebral cavernous malformation protein CCM1 inhibits sprout... | KEEP AS NON CORE | Summary: Human endothelial perturbation supports this antiangiogenic/developmental regulatory effect. Reason: CCM1 perturbation directly changes endothelial proliferation, migration, apoptosis and sprouting in primary human endothelial cells. These are documented consequences of the junctional signaling regulator. Broad developmental-process annotations are retained as non-core; they do not identify a distinct enzyme function or germline piRNA mechanism. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0016525 negative regulation of angiogenesis | IBA GO_REF:0000033 | ACCEPT | Summary: Human endothelial perturbation supports this antiangiogenic/developmental regulatory effect. Reason: CCM1 perturbation directly changes endothelial proliferation, migration, apoptosis and sprouting in primary human endothelial cells. These are documented consequences of the junctional signaling regulator. Broad developmental-process annotations are retained as non-core; they do not identify a distinct enzyme function or germline piRNA mechanism. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0016525 negative regulation of angiogenesis | IEA GO_REF:0000120 | ACCEPT | Summary: Human endothelial perturbation supports this antiangiogenic/developmental regulatory effect. Reason: CCM1 perturbation directly changes endothelial proliferation, migration, apoptosis and sprouting in primary human endothelial cells. These are documented consequences of the junctional signaling regulator. Broad developmental-process annotations are retained as non-core; they do not identify a distinct enzyme function or germline piRNA mechanism. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0016525 negative regulation of angiogenesis | IMP PMID:20616044 Cerebral cavernous malformation protein CCM1 inhibits sprout... | ACCEPT | Summary: Human endothelial perturbation supports this antiangiogenic/developmental regulatory effect. Reason: CCM1 perturbation directly changes endothelial proliferation, migration, apoptosis and sprouting in primary human endothelial cells. These are documented consequences of the junctional signaling regulator. Broad developmental-process annotations are retained as non-core; they do not identify a distinct enzyme function or germline piRNA mechanism. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0030695 GTPase regulator activity | IEA GO_REF:0000117 | MODIFY | Summary: Direct Rap1 binding is established; intrinsic GTPase regulation is not the demonstrated mechanism. Reason: The early two-hybrid paper suggested KRIT1 might regulate Krev-1, but later direct binding and mutagenesis establish a GTP-dependent Rap1 effector. These experiments do not show nucleotide exchange or GTPase activation. Use small GTPase binding to express the demonstrated molecular interaction. Proposed replacements: small GTPase binding Supporting Evidence: PMID:21633110 native KRIT1 protein binds the effector loop of Rap1A but not H-Ras in a GTP-dependent manner |
| GO:0030695 GTPase regulator activity | TAS PMID:9285558 Association of Krev-1/rap1a with Krit1, a novel ankyrin repe... | MODIFY | Summary: Direct Rap1 binding is established; intrinsic GTPase regulation is not the demonstrated mechanism. Reason: The early two-hybrid paper suggested KRIT1 might regulate Krev-1, but later direct binding and mutagenesis establish a GTP-dependent Rap1 effector. These experiments do not show nucleotide exchange or GTPase activation. Use small GTPase binding to express the demonstrated molecular interaction. Proposed replacements: small GTPase binding Supporting Evidence: PMID:21633110 native KRIT1 protein binds the effector loop of Rap1A but not H-Ras in a GTP-dependent manner |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Generic complex membership is compatible with the CCM scaffold. Reason: KRIT1 forms defined partner assemblies, but the generic protein-containing-complex term does not specify which functional assembly. It is a compatible non-core annotation. Supporting Evidence: PMID:20332120 We propose that VEC, CCM1 and Rap1 form a signaling complex. |
| GO:0033622 integrin activation | IDA PMID:23317506 Mechanism for KRIT1 release of ICAP1-mediated suppression of... | ACCEPT | Summary: KRIT1 promotes integrin activation by competing for ICAP1. Reason: The cocrystal/competition study demonstrates a bidentate KRIT1βICAP1 interface and antagonism of ICAP1-mediated integrin inhibition. This is direct scaffold regulation of integrin activation. Supporting Evidence: PMID:23317506 KRIT1 directly competes with integrin Ξ²1 to bind ICAP1 |
| GO:0045454 cell redox homeostasis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: KRIT1 affects cellular redox homeostasis through signaling regulation. Reason: Loss and restoration of KRIT1 modulate ROS and FOXO1/SOD2 levels. The phenotype supports redox homeostasis but does not imply intrinsic antioxidant enzyme activity. Supporting Evidence: PMID:20668652 KRIT1 loss/down-regulation is associated with a significant increase in intracellular ROS levels. |
| GO:0045454 cell redox homeostasis | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: KRIT1 affects cellular redox homeostasis through signaling regulation. Reason: Loss and restoration of KRIT1 modulate ROS and FOXO1/SOD2 levels. The phenotype supports redox homeostasis but does not imply intrinsic antioxidant enzyme activity. Supporting Evidence: PMID:20668652 KRIT1 loss/down-regulation is associated with a significant increase in intracellular ROS levels. |
| GO:0045454 cell redox homeostasis | IMP PMID:20668652 KRIT1 regulates the homeostasis of intracellular reactive ox... | KEEP AS NON CORE | Summary: KRIT1 affects cellular redox homeostasis through signaling regulation. Reason: Loss and restoration of KRIT1 modulate ROS and FOXO1/SOD2 levels. The phenotype supports redox homeostasis but does not imply intrinsic antioxidant enzyme activity. Supporting Evidence: PMID:20668652 KRIT1 loss/down-regulation is associated with a significant increase in intracellular ROS levels. |
| GO:0045765 regulation of angiogenesis | NAS PMID:17657516 CCM3 interacts with CCM2 indicating common pathogenesis for ... | KEEP AS NON CORE | Summary: Vascular developmental regulation is supported by the CCM1 scaffold mechanism. Reason: KRIT1 regulates endothelial organization and quiescence, with experimental vascular-development phenotypes. The generic developmental/regulatory term is compatible but less informative than the endothelial-junction and angiogenesis mechanisms. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
| GO:0070161 anchoring junction | IEA GO_REF:0000044 | ACCEPT | Summary: Membrane/junctional and cytoplasmic pools are supported by KRIT1 recruitment experiments. Reason: Rap1-dependent release from microtubules permits junctional recruitment, while CCM1 participates in the VE-cadherin polarity complex. The selected horse sequence retains the corresponding scaffold architecture and extensive sequence conservation, supporting transfer of these broad compartments. Supporting Evidence: PMID:20332120 Both VEC and CCM1 control Rap1 concentration at cell-cell junctions. PMID:21633110 Rap1 binding released KRIT1 from microtubules |
| GO:2000114 regulation of establishment of cell polarity | IBA GO_REF:0000033 | ACCEPT | Summary: KRIT1 directly supports endothelial polarity-complex organization. Reason: CCM1 interacts with VE-cadherin and organizes adherens-junction association with the Par polarity complex; loss disrupts cell polarity. This is a specific regulatory role of the scaffold. Supporting Evidence: PMID:20332120 In the absence of any of these proteins, AJs are dismantled, cell polarity is lost |
| GO:2000114 regulation of establishment of cell polarity | IEA GO_REF:0000120 | ACCEPT | Summary: KRIT1 directly supports endothelial polarity-complex organization. Reason: CCM1 interacts with VE-cadherin and organizes adherens-junction association with the Par polarity complex; loss disrupts cell polarity. This is a specific regulatory role of the scaffold. Supporting Evidence: PMID:20332120 In the absence of any of these proteins, AJs are dismantled, cell polarity is lost |
| GO:2000114 regulation of establishment of cell polarity | IMP PMID:20332120 CCM1 regulates vascular-lumen organization by inducing endot... | ACCEPT | Summary: KRIT1 directly supports endothelial polarity-complex organization. Reason: CCM1 interacts with VE-cadherin and organizes adherens-junction association with the Par polarity complex; loss disrupts cell polarity. This is a specific regulatory role of the scaffold. Supporting Evidence: PMID:20332120 In the absence of any of these proteins, AJs are dismantled, cell polarity is lost |
| GO:2000352 negative regulation of endothelial cell apoptotic process | IMP PMID:20616044 Cerebral cavernous malformation protein CCM1 inhibits sprout... | KEEP AS NON CORE | Summary: Human endothelial perturbation supports this antiangiogenic/developmental regulatory effect. Reason: CCM1 perturbation directly changes endothelial proliferation, migration, apoptosis and sprouting in primary human endothelial cells. These are documented consequences of the junctional signaling regulator. Broad developmental-process annotations are retained as non-core; they do not identify a distinct enzyme function or germline piRNA mechanism. Supporting Evidence: PMID:20616044 CCM1 inhibits endothelial proliferation, apoptosis, migration, lumen formation, and sprouting angiogenesis in primary human endothelial cells. |
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