CLV2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0001653 peptide receptor activity	IMP PMID:28607033 Perception of root-active CLE peptides requires CORYNE funct...	MODIFY	Summary: clv2 and crn mutants are resistant to many root-active CLE peptides, which shows that CLV2 is required for CLE perception (Hazak et al. 2017). The IMP evidence shows the requirement, but not that CLV2 by itself binds the ligand and starts signalling. Direct CLE binding by CLV2 is contested: it was reported by radioligand assays and not detected by photoaffinity labelling. CLV2 works with CRN and with the CLV1/BAM/CIK receptor kinases. Reason: Coreceptor activity (combining with the messenger in cooperation with a nearby primary receptor) fits the role of the kinase-less CLV2/CRN complex better than a stand-alone peptide receptor activity. It is the best available term, although its definition (combining with the messenger) leans toward the radioligand-binding side of the dispute over direct CLE binding. Proposed replacements: coreceptor activity Supporting Evidence: PMID:28607033 the receptor-like protein CLAVATA 2 (CLV2) and the pseudokinase CORYNE (CRN) are necessary to fully sense root-active CLE peptides PMID:25754504 In contrast, the CLV2/CRN complex and RPK2 are not involved in direct ligand interactions but may act as co-receptors. PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 file:ARATH/CLV2/CLV2-deep-research-falcon.md direct binding of CLV3 or another CLE peptide by the physiological CLV2–CRN heteromer has not been established
GO:0005515 protein binding	IPI PMID:19843317 Analysis of interactions among the CLAVATA3 receptors reveal...	MODIFY	Summary: CLV2 interacts with the pseudokinase CRN through the transmembrane and juxtamembrane regions. The interaction is shown by luciferase complementation and co-IP, and by co-IP in stable Arabidopsis lines. It forms the CLV2/CRN receptor complex needed for ER export of both proteins. Reason: Generic protein binding is uninformative. CRN is a receptor-like (pseudo)kinase, and the CLV2-CRN association is a receptor-complex interaction. Proposed replacements: signaling receptor binding Supporting Evidence: PMID:19843317 CLV2 can directly interact with CRN in the absence of CLV3 PMID:20626648 Transgenic Arabidopsis plants stably expressing CLV2-MYC and CRN-GFP were used to assess interactions in vivo. Here we also observed robust co-IP between the two proteins PMID:19933383 CRN readily forms homomers and interacts with CLV2 through the transmembrane domain and adjacent juxtamembrane sequences.
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 interacts with the pseudokinase CRN through the transmembrane and juxtamembrane regions. The interaction is shown by luciferase complementation and co-IP, and by co-IP in stable Arabidopsis lines. It forms the CLV2/CRN receptor complex needed for ER export of both proteins. Reason: Generic protein binding is uninformative. CRN is a receptor-like (pseudo)kinase, and the CLV2-CRN association is a receptor-complex interaction. Proposed replacements: signaling receptor binding Supporting Evidence: PMID:19843317 CLV2 can directly interact with CRN in the absence of CLV3 PMID:20626648 Transgenic Arabidopsis plants stably expressing CLV2-MYC and CRN-GFP were used to assess interactions in vivo. Here we also observed robust co-IP between the two proteins PMID:19933383 CRN readily forms homomers and interacts with CLV2 through the transmembrane domain and adjacent juxtamembrane sequences.
GO:0005515 protein binding	IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul...	MODIFY	Summary: CLV2 shows saturable radioligand binding of the CLV3 CLE peptide (Kd about 32 nM) and competition by several other CLE peptides in membrane fractions and immunoprecipitates (Guo et al. 2010). This is a ligand-binding interaction with a CLE peptide, not generic protein binding. Direct binding was not reproduced by photoaffinity labelling (Shinohara and Matsubayashi 2015), so the claim is contested. Reason: The curator's evidence is saturable, competable radioligand binding of CLE peptides by CLV2 (Kd about 32 nM), which is a ligand-binding measurement, so peptide hormone binding is the specific term for what was assayed; generic protein binding is uninformative. The replacement records the reported interaction only. Because photoaffinity labelling did not detect it (see summary), it is not used as a core function, which is coreceptor activity. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:20626648 Binding was saturable for all receptors with a very similar Kd for each receptor: 30 nM for CLV1, 32 nM for CLV2, 26 nM for BAM1, and 36 nM for BAM2 PMID:20626648 CLV1 and CLV2 displayed similar binding affinities for a number of CLEs, including CLE1, CLE5, CLE18, CLE22, CLE26, CLE41 and CLE42
GO:0005515 protein binding	IPI PMID:27229734 Shared and distinct functions of the pseudokinase CORYNE (CR...	MODIFY	Summary: CLV2 interacts with the pseudokinase CRN through the transmembrane and juxtamembrane regions. The interaction is shown by luciferase complementation and co-IP, and by co-IP in stable Arabidopsis lines. It forms the CLV2/CRN receptor complex needed for ER export of both proteins. Reason: Generic protein binding is uninformative. CRN is a receptor-like (pseudo)kinase, and the CLV2-CRN association is a receptor-complex interaction. Proposed replacements: signaling receptor binding Supporting Evidence: PMID:19843317 CLV2 can directly interact with CRN in the absence of CLV3 PMID:20626648 Transgenic Arabidopsis plants stably expressing CLV2-MYC and CRN-GFP were used to assess interactions in vivo. Here we also observed robust co-IP between the two proteins PMID:19933383 CRN readily forms homomers and interacts with CLV2 through the transmembrane domain and adjacent juxtamembrane sequences.
GO:0005515 protein binding	IPI PMID:28586647 Phosphate Starvation-Dependent Iron Mobilization Induces CLE...	MODIFY	Summary: CLE14 is perceived through CLV2 (with PEPR2) to trigger root meristem differentiation under low phosphate. The interaction partner is a CLE peptide ligand. Reason: A ligand-receptor peptide interaction is better captured by peptide binding than by generic protein binding. Proposed replacements: peptide hormone binding Supporting Evidence: PMID:28586647 CLV2 and PEPR2 receptors perceive CLE14 and trigger RAM differentiation
GO:0005789 endoplasmic reticulum membrane	IDA PMID:21051944 Membrane distributions of two ligand-binding receptor comple...	KEEP AS NON CORE	Summary: CLV2 is detected in the endoplasmic reticulum, especially when CRN is absent or limiting, because the CLV2/CRN complex must form before it can leave the ER. The ER is a transit compartment, not the site of signalling. Reason: The localization is real, but it is a biosynthetic and quality-control location rather than the functional one. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 CLV2 shows greater co-localization with an endoplasmic reticulum (ER) marker.
GO:0005789 endoplasmic reticulum membrane	IDA PMID:27229734 Shared and distinct functions of the pseudokinase CORYNE (CR...	KEEP AS NON CORE	Summary: CLV2 is detected in the endoplasmic reticulum, especially when CRN is absent or limiting, because the CLV2/CRN complex must form before it can leave the ER. The ER is a transit compartment, not the site of signalling. Reason: The localization is real, but it is a biosynthetic and quality-control location rather than the functional one. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 CLV2 shows greater co-localization with an endoplasmic reticulum (ER) marker.
GO:0005789 endoplasmic reticulum membrane	IDA PMID:28607033 Perception of root-active CLE peptides requires CORYNE funct...	KEEP AS NON CORE	Summary: CLV2 is detected in the endoplasmic reticulum, especially when CRN is absent or limiting, because the CLV2/CRN complex must form before it can leave the ER. The ER is a transit compartment, not the site of signalling. Reason: The localization is real, but it is a biosynthetic and quality-control location rather than the functional one. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 CLV2 shows greater co-localization with an endoplasmic reticulum (ER) marker.
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: CLV2 is detected in the endoplasmic reticulum, especially when CRN is absent or limiting, because the CLV2/CRN complex must form before it can leave the ER. The ER is a transit compartment, not the site of signalling. Reason: The localization is real, but it is a biosynthetic and quality-control location rather than the functional one. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 CLV2 shows greater co-localization with an endoplasmic reticulum (ER) marker.
GO:0005886 plasma membrane	EXP PMID:19933383 Stem cell signaling in Arabidopsis requires CRN to localize ...	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0005886 plasma membrane	IBA GO_REF:0000033	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0005886 plasma membrane	IDA PMID:21051944 Membrane distributions of two ligand-binding receptor comple...	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0005886 plasma membrane	IDA PMID:27229734 Shared and distinct functions of the pseudokinase CORYNE (CR...	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0005886 plasma membrane	IDA PMID:28607033 Perception of root-active CLE peptides requires CORYNE funct...	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0005886 plasma membrane	IEA GO_REF:0000044	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0005886 plasma membrane	ISM GO_REF:0000122	ACCEPT	Summary: CLV2 accumulates at the plasma membrane in a CRN-dependent way. The plasma membrane is where the CLV2/CRN complex perceives CLE peptides. Reason: This location is supported by several experimental studies and is consistent with the receptor function. Supporting Evidence: PMID:19933383 We found that CLV2 and CRN require each other for export from the endoplasmic reticulum and localization to the plasma membrane (PM). PMID:21051944 All tested proteins measurably accumulate at the plasma membrane.
GO:0007165 signal transduction	IEA GO_REF:0000117	MODIFY	Summary: CLV2 takes part in CLE peptide signalling at the cell surface. Signal transduction is correct but very broad. Reason: Use the more informative parent for cell-surface receptor signalling. No CLE-specific GO process term exists. Proposed replacements: cell surface receptor signaling pathway Supporting Evidence: PMID:18381924 We show here that the novel receptor kinase CORYNE (CRN) and CLV2 act together, and in parallel with CLV1, to perceive the CLV3 signal. PMID:16055633 Interestingly, clv2 failed to respond to the peptide treatment, suggesting that CLV2 is involved in the CLE peptide signaling.
GO:0007165 signal transduction	TAS PMID:10521522 The Arabidopsis CLAVATA2 gene encodes a receptor-like protei...	MODIFY	Summary: CLV2 takes part in CLE peptide signalling at the cell surface. Signal transduction is correct but very broad. Reason: Use the more informative parent for cell-surface receptor signalling. No CLE-specific GO process term exists. Proposed replacements: cell surface receptor signaling pathway Supporting Evidence: PMID:18381924 We show here that the novel receptor kinase CORYNE (CRN) and CLV2 act together, and in parallel with CLV1, to perceive the CLV3 signal. PMID:16055633 Interestingly, clv2 failed to respond to the peptide treatment, suggesting that CLV2 is involved in the CLE peptide signaling.
GO:0009653 anatomical structure morphogenesis	IMP PMID:9729492 CLAVATA2, a regulator of meristem and organ development in A...	KEEP AS NON CORE	Summary: clv2 mutants have defects in gynoecium, pedicel and stamen development in addition to enlarged meristems. Anatomical structure morphogenesis is a broad, downstream phenotype term. Reason: This is a pleiotropic developmental phenotype downstream of CLE signalling. Supporting Evidence: PMID:9729492 Mutations at the CLAVATA2 (CLV2) locus of Arabidopsis result in enlarged shoot and flower meristems, as well as alterations in the development of the gynoecia, flower pedicels, and stamens.
GO:0009909 regulation of flower development	IMP PMID:9729492 CLAVATA2, a regulator of meristem and organ development in A...	KEEP AS NON CORE	Summary: clv2 flower phenotypes change with photoperiod and include flower-to-shoot transformations under short days. This reflects the meristem and organ roles of CLV2 rather than a dedicated role in flowering. Reason: This is a downstream developmental consequence of loss of CLE signalling. Supporting Evidence: PMID:9729492 Mutations at the CLAVATA2 (CLV2) locus of Arabidopsis result in enlarged shoot and flower meristems, as well as alterations in the development of the gynoecia, flower pedicels, and stamens.
GO:0010075 regulation of meristem growth	IDA PMID:28586647 Phosphate Starvation-Dependent Iron Mobilization Induces CLE...	ACCEPT	Summary: CLV2, with CRN, restricts WUS expression and meristem size in the shoot, and mediates CLE14-triggered differentiation of the root apical meristem. Reason: This is the central physiological output of CLV2-dependent CLE signalling. Supporting Evidence: PMID:21705761 The CLAVATA1 (CLV1), CLV2, and CORYNE (CRN) receptors in Arabidopsis thaliana maintain cell proliferation in shoot apical meristems by restricting expression of the transcription factor WUSCHEL (WUS). PMID:28586647 CLV2 and PEPR2 receptors perceive CLE14 and trigger RAM differentiation PMID:9729492 Mutations at the CLAVATA2 (CLV2) locus of Arabidopsis result in enlarged shoot and flower meristems, as well as alterations in the development of the gynoecia, flower pedicels, and stamens.
GO:0010075 regulation of meristem growth	IMP PMID:21705761 CLAVATA signaling pathway receptors of Arabidopsis regulate ...	ACCEPT	Summary: CLV2, with CRN, restricts WUS expression and meristem size in the shoot, and mediates CLE14-triggered differentiation of the root apical meristem. Reason: This is the central physiological output of CLV2-dependent CLE signalling. Supporting Evidence: PMID:21705761 The CLAVATA1 (CLV1), CLV2, and CORYNE (CRN) receptors in Arabidopsis thaliana maintain cell proliferation in shoot apical meristems by restricting expression of the transcription factor WUSCHEL (WUS). PMID:28586647 CLV2 and PEPR2 receptors perceive CLE14 and trigger RAM differentiation PMID:9729492 Mutations at the CLAVATA2 (CLV2) locus of Arabidopsis result in enlarged shoot and flower meristems, as well as alterations in the development of the gynoecia, flower pedicels, and stamens.
GO:0010078 maintenance of root meristem identity	IMP PMID:28607033 Perception of root-active CLE peptides requires CORYNE funct...	KEEP AS NON CORE	Summary: CLV2/CRN are needed to fully sense root-active CLE peptides that act in the protophloem and proximal root meristem. The IMP is based on resistance to added CLE peptides. Reason: This is a root-context output of CLE perception, supported mainly by peptide-resistance assays. Supporting Evidence: PMID:28607033 the receptor-like protein CLAVATA 2 (CLV2) and the pseudokinase CORYNE (CRN) are necessary to fully sense root-active CLE peptides
GO:0010088 phloem development	IMP PMID:28607033 Perception of root-active CLE peptides requires CORYNE funct...	KEEP AS NON CORE	Summary: Root-active CLE peptides act mainly in the protophloem, and CLV2/CRN are needed for this response. Reason: This is a context-specific developmental output of CLE perception. Supporting Evidence: PMID:28607033 the receptor-like protein CLAVATA 2 (CLV2) and the pseudokinase CORYNE (CRN) are necessary to fully sense root-active CLE peptides PMID:28607033 protophloem-specific CRN expression complements resistance of the crn mutant to root-active CLE peptides
GO:0016020 membrane	ISS PMID:10521522 The Arabidopsis CLAVATA2 gene encodes a receptor-like protei...	KEEP AS NON CORE	Summary: CLV2 is a single-pass transmembrane protein. Membrane is correct but uninformative compared with plasma membrane. Reason: This is correct but redundant with the more specific plasma membrane annotations. Supporting Evidence: PMID:10521522 We isolated the CLV2 gene and found that it encodes a receptor-like protein (RLP), with a presumed extracellular domain composed of leucine-rich repeats
GO:0038023 signaling receptor activity	IBA GO_REF:0000033	ACCEPT	Summary: This PAINT IBA places CLV2 in a receptor-like protein clade with signalling receptor activity. It is consistent with the role of CLV2 as a CLE co-receptor. Reason: This general receptor activity is correct, and coreceptor activity is its more specific child. Supporting Evidence: PMID:18381924 We show here that the novel receptor kinase CORYNE (CRN) and CLV2 act together, and in parallel with CLV1, to perceive the CLV3 signal. PMID:25754504 In contrast, the CLV2/CRN complex and RPK2 are not involved in direct ligand interactions but may act as co-receptors.
GO:0040008 regulation of growth	IMP PMID:9729492 CLAVATA2, a regulator of meristem and organ development in A...	KEEP AS NON CORE	Summary: clv2 mutants show growth-related phenotypes, including altered organ development and photoperiod-dependent changes. Regulation of growth is a broad downstream term. Reason: This is a broad pleiotropic phenotype. Supporting Evidence: PMID:9729492 Mutations at the CLAVATA2 (CLV2) locus of Arabidopsis result in enlarged shoot and flower meristems, as well as alterations in the development of the gynoecia, flower pedicels, and stamens.
GO:0045595 regulation of cell differentiation	IMP PMID:28607033 Perception of root-active CLE peptides requires CORYNE funct...	KEEP AS NON CORE	Summary: CLE signalling through CLV2/CRN suppresses protophloem differentiation and promotes root meristem differentiation, depending on the ligand. Reason: This is a downstream developmental output of CLE perception. Supporting Evidence: PMID:28607033 the receptor-like protein CLAVATA 2 (CLV2) and the pseudokinase CORYNE (CRN) are necessary to fully sense root-active CLE peptides
GO:0048507 meristem development	IMP PMID:18434605 A genome-wide functional investigation into the roles of rec...	ACCEPT	Summary: A genome-wide RLP T-DNA collection revealed new developmental phenotypes for clv2 insertion mutants, consistent with a role in meristem development. Reason: This is consistent with the established role of CLV2 in meristem maintenance. Supporting Evidence: PMID:18434605 A number of novel developmental phenotypes were revealed for our CLV2 and TMM insertion mutants. PMID:9729492 Mutations at the CLAVATA2 (CLV2) locus of Arabidopsis result in enlarged shoot and flower meristems, as well as alterations in the development of the gynoecia, flower pedicels, and stamens.

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