BARELY ANY MERISTEM 1 (BAM1) is a plasma membrane leucine-rich repeat receptor-like Ser/Thr kinase of the CLAVATA1 clade. Its extracellular LRR domain binds CLV3 and a broad range of other CLE peptides, with wider ligand specificity than CLV1, and its cytoplasmic kinase phosphorylates CIK co-receptor kinases and the receptor-like cytoplasmic kinases PBL34/35/36. BAM1 forms homomers and heteromers with BAM2 and CLV1. In the shoot meristem it acts redundantly with CLV1 as a direct CLV3 receptor that restricts WUSCHEL expression. BAM1 is normally expressed in the meristem periphery and is up-regulated in the centre when CLV1 is lost, which compensates for clv1 loss. Outside the meristem, BAM1 acts with BAM2 and BAM3 in early anther cell-layer specification, male gametophyte and ovule development, leaf vascular patterning, and CLE25/26/45-triggered suppression of root protophloem differentiation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: This IEA comes from the protein kinase domain signature. BAM1 has an active Ser/Thr kinase domain that phosphorylates CIKs and PBL34/35/36. Reason: It is correct but less specific than the experimentally supported transmembrane receptor Ser/Thr kinase activity, consistent with the MODIFY of the GO:0004674 rows. Proposed replacements: transmembrane receptor protein serine/threonine kinase activity Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:34651321 A CLE-BAM-CIK signalling module controls root protophloem di... | MODIFY | Summary: BAM1 phosphorylates downstream partners: PBL34/35/36 in vitro, and CLE-induced CIK phosphorylation depends on CLV1/BAM1/BAM3. BAM1 also binds the CLV3 peptide directly (photoaffinity labelling; radioligand Kd about 26 nM), so it combines ligand binding and Ser/Thr kinase catalysis in a single transmembrane receptor. Reason: Ser/Thr kinase activity is the catalytic core of BAM1 receptor function. Because the kinase is the cytoplasmic domain of a ligand-binding single-pass LRR receptor, the more precise term is transmembrane receptor protein serine/threonine kinase activity, a direct child of GO:0004674. Proposed replacements: transmembrane receptor protein serine/threonine kinase activity Supporting Evidence: PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. 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:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. PMID:34651321 CLE25/26/45 enhanced the phosphorylation levels of CIKs, which were greatly impaired in clv1 bam1 3 mutant |
| GO:0004674 protein serine/threonine kinase activity | IEA GO_REF:0000003 | MODIFY | Summary: BAM1 phosphorylates downstream partners: PBL34/35/36 in vitro, and CLE-induced CIK phosphorylation depends on CLV1/BAM1/BAM3. Reason: Ser/Thr kinase activity is the catalytic core of BAM1 receptor function; as for the IDA row, the more precise term for this ligand-binding receptor is transmembrane receptor protein serine/threonine kinase activity, a direct child of GO:0004674. Proposed replacements: transmembrane receptor protein serine/threonine kinase activity Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. PMID:34651321 CLE25/26/45 enhanced the phosphorylation levels of CIKs, which were greatly impaired in clv1 bam1 3 mutant |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | MODIFY | Summary: In radioligand competition assays, BAM1 binds the CLV3 CLE peptide (Kd about 26 nM) and is competed by most other CLE peptides tested. The interaction partners here are CLE peptide ligands. Photoaffinity labelling independently confirmed direct CLV3 binding by BAM1. Reason: A ligand-receptor peptide interaction is better represented as peptide binding than as generic protein binding. 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 This suggests that BAM receptors have a wider range of specificity for CLE binding than either CLV1 or CLV2, perhaps related to their broad developmental roles. PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: This ectodomain interaction comes from a sensitized high-throughput LRR-RK screen (CSI-LRR). The partners (ERL1, BRL3 and uncharacterized LRR-RKs) have no established functional link to BAM1. Reason: A bare protein binding row from a high-throughput ectodomain screen carries no functional information, and the screen does not support a more informative term. Removal does not mean the interaction is false. Supporting Evidence: PMID:29320478 produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: This ectodomain interaction comes from a sensitized high-throughput LRR-RK screen (CSI-LRR). The partners (ERL1, BRL3 and uncharacterized LRR-RKs) have no established functional link to BAM1. Reason: A bare protein binding row from a high-throughput ectodomain screen carries no functional information, and the screen does not support a more informative term. Removal does not mean the interaction is false. Supporting Evidence: PMID:29320478 produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: This ectodomain interaction comes from a sensitized high-throughput LRR-RK screen (CSI-LRR). The partners (ERL1, BRL3 and uncharacterized LRR-RKs) have no established functional link to BAM1. Reason: A bare protein binding row from a high-throughput ectodomain screen carries no functional information, and the screen does not support a more informative term. Removal does not mean the interaction is false. Supporting Evidence: PMID:29320478 produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: This ectodomain interaction comes from a sensitized high-throughput LRR-RK screen (CSI-LRR). The partners (ERL1, BRL3 and uncharacterized LRR-RKs) have no established functional link to BAM1. Reason: A bare protein binding row from a high-throughput ectodomain screen carries no functional information, and the screen does not support a more informative term. Removal does not mean the interaction is false. Supporting Evidence: PMID:29320478 produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: This ectodomain interaction comes from a sensitized high-throughput LRR-RK screen (CSI-LRR). The partners (ERL1, BRL3 and uncharacterized LRR-RKs) have no established functional link to BAM1. Reason: A bare protein binding row from a high-throughput ectodomain screen carries no functional information, and the screen does not support a more informative term. Removal does not mean the interaction is false. Supporting Evidence: PMID:29320478 produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions |
| GO:0005515 protein binding | IPI PMID:33909893 Receptor-like cytoplasmic kinase MAZZA mediates developmenta... | MODIFY | Summary: The membrane-associated RLCK MAZZA (CARK5) interacts in vivo with CLV1-family receptors, including BAM1. Reason: The partner is a protein kinase, so protein kinase binding is the informative term. Proposed replacements: protein kinase binding Supporting Evidence: PMID:33909893 the membrane-associated receptor-like cytoplasmic kinase (RLCK) MAZZA (MAZ) and additional members of the Pti1-like protein family interact in vivo with CLV1f receptors. |
| GO:0005515 protein binding | IPI PMID:34935965 Receptor-like cytoplasmic kinases PBL34/35/36 are required f... | MODIFY | Summary: BAM1 interacts with the RLCKs PBL34/35/36 at the plasma membrane and phosphorylates them. These are downstream components of CLE signalling. Reason: The partners are protein kinases and substrates, so protein kinase binding is more informative than protein binding. Proposed replacements: protein kinase binding Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005515 protein binding | IPI PMID:34935965 Receptor-like cytoplasmic kinases PBL34/35/36 are required f... | MODIFY | Summary: BAM1 interacts with the RLCKs PBL34/35/36 at the plasma membrane and phosphorylates them. These are downstream components of CLE signalling. Reason: The partners are protein kinases and substrates, so protein kinase binding is more informative than protein binding. Proposed replacements: protein kinase binding Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005515 protein binding | IPI PMID:34935965 Receptor-like cytoplasmic kinases PBL34/35/36 are required f... | MODIFY | Summary: BAM1 interacts with the RLCKs PBL34/35/36 at the plasma membrane and phosphorylates them. These are downstream components of CLE signalling. Reason: The partners are protein kinases and substrates, so protein kinase binding is more informative than protein binding. Proposed replacements: protein kinase binding Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: BAM1 has a catalytically active kinase domain, which requires ATP binding. Reason: This is consistent with the demonstrated kinase activity. Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005886 plasma membrane | EXP PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | ACCEPT | Summary: BAM1 is a plasma membrane receptor kinase. CLE-binding activity is detected in membrane fractions, and BAM1 interacts with PBLs at the plasma membrane. Reason: This is the functional location. 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:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005886 plasma membrane | HDA PMID:14506206 Large-scale analysis of in vivo phosphorylated membrane prot... | ACCEPT | Summary: BAM1 is a plasma membrane receptor kinase. CLE-binding activity is detected in membrane fractions, and BAM1 interacts with PBLs at the plasma membrane. Reason: This is the functional location. 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:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: BAM1 is a plasma membrane receptor kinase. CLE-binding activity is detected in membrane fractions, and BAM1 interacts with PBLs at the plasma membrane. Reason: This is the functional location. 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:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: BAM1 is a plasma membrane receptor kinase. CLE-binding activity is detected in membrane fractions, and BAM1 interacts with PBLs at the plasma membrane. Reason: This is the functional location. 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:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0005886 plasma membrane | ISM GO_REF:0000122 | ACCEPT | Summary: BAM1 is a plasma membrane receptor kinase. CLE-binding activity is detected in membrane fractions, and BAM1 interacts with PBLs at the plasma membrane. Reason: This is the functional location. 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:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0009755 hormone-mediated signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: This IBA comes from a PANTHER node seeded by brassinosteroid receptors (BRI1, BRL2, OsBRI1). BAM1 sits inside that LRR-RK clade, and it does mediate hormone signalling: it is a receptor for CLE peptide hormones. The transfer is therefore technically valid, but the generic term says little about BAM1. Reason: The inherited term is broadly true for a peptide-hormone receptor kinase. The specific receptor activity and meristem processes are the core annotations. Supporting Evidence: PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0009934 regulation of meristem structural organization | IEA GO_REF:0000117 | ACCEPT | Summary: bam1 bam2 clv1 combinations show severe stem cell specification defects, and bam mutants modify clv meristem phenotypes. BAM1 regulates meristem organization redundantly with CLV1. Reason: This core meristem role is supported by genetic interaction data and matches the CLV1 annotation. Supporting Evidence: PMID:18780746 We have identified two such parallel receptors, BAM1 and BAM2. PMID:18780746 with bam clv mutants exhibiting severe defects in stem cell specification |
| GO:0009934 regulation of meristem structural organization | IGI PMID:18780746 BAM receptors regulate stem cell specification and organ dev... | ACCEPT | Summary: bam1 bam2 clv1 combinations show severe stem cell specification defects, and bam mutants modify clv meristem phenotypes. BAM1 regulates meristem organization redundantly with CLV1. Reason: This core meristem role is supported by genetic interaction data and matches the CLV1 annotation. Supporting Evidence: PMID:18780746 We have identified two such parallel receptors, BAM1 and BAM2. PMID:18780746 with bam clv mutants exhibiting severe defects in stem cell specification |
| GO:0010075 regulation of meristem growth | IEA GO_REF:0000117 | ACCEPT | Summary: bam1 bam2 (and bam3) mutants show loss of stem cells at the shoot and flower meristems, and clv1 bam1 double mutants have greatly enlarged meristems with expanded WUS expression. Reason: This is the central meristem output of BAM1 CLE signalling. Supporting Evidence: PMID:16367950 Loss-of-function alleles of these receptors lead to phenotypes consistent with the loss of stem cells at the shoot and flower meristem PMID:25754504 WUS gene transcripts were up-regulated, and the region of WUS expression was enlarged at the SAM in the clv1 bam1 double mutant. |
| GO:0010075 regulation of meristem growth | IGI PMID:16367950 The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-lik... | ACCEPT | Summary: bam1 bam2 (and bam3) mutants show loss of stem cells at the shoot and flower meristems, and clv1 bam1 double mutants have greatly enlarged meristems with expanded WUS expression. Reason: This is the central meristem output of BAM1 CLE signalling. Supporting Evidence: PMID:16367950 Loss-of-function alleles of these receptors lead to phenotypes consistent with the loss of stem cells at the shoot and flower meristem PMID:25754504 WUS gene transcripts were up-regulated, and the region of WUS expression was enlarged at the SAM in the clv1 bam1 double mutant. |
| GO:0033612 receptor serine/threonine kinase binding | IEA GO_REF:0000117 | ACCEPT | Summary: BAM1 forms robust co-immunoprecipitating multimers with CLV1 (and BAM2), which are receptor Ser/Thr kinases. Reason: This is a well-supported receptor-receptor association within the CLV1/BAM complex. Supporting Evidence: PMID:20626648 We observed robust co-IP between CLV1-CLV1, CLV1-BAM1, CLV1-BAM2, BAM1-BAM1, and BAM1-BAM2 |
| GO:0033612 receptor serine/threonine kinase binding | IPI PMID:20626648 CLAVATA2 forms a distinct CLE-binding receptor complex regul... | ACCEPT | Summary: BAM1 forms robust co-immunoprecipitating multimers with CLV1 (and BAM2), which are receptor Ser/Thr kinases. Reason: This is a well-supported receptor-receptor association within the CLV1/BAM complex. Supporting Evidence: PMID:20626648 We observed robust co-IP between CLV1-CLV1, CLV1-BAM1, CLV1-BAM2, BAM1-BAM1, and BAM1-BAM2 |
| GO:0035556 intracellular signal transduction | IDA PMID:34651321 A CLE-BAM-CIK signalling module controls root protophloem di... | KEEP AS NON CORE | Summary: BAM1 kinase signalling leads to phosphorylation of CIKs and PBL34/35/36 and to CLV3-activated MPK3/MPK6 phosphorylation. Reason: This is correct as a description of downstream relay, but the receptor-level process is cell surface receptor signalling. Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. PMID:34935965 The CLV3-activated phosphorylation of MPK3 and MPK6 is dependent on CLV1 and BAM1. |
| GO:0038023 signaling receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: This PAINT IBA for signalling receptor activity is consistent with BAM1 acting as a direct CLE peptide receptor kinase. Reason: This is correct, and transmembrane receptor Ser/Thr kinase activity is the more specific core term. Supporting Evidence: PMID:25754504 Further analysis showed that the receptor kinase BAM1 directly binds the CLV3 peptide. 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 |
| GO:0042802 identical protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | KEEP AS NON CORE | Summary: BAM1 forms homomers, detected by co-IP and in the CSI-LRR ectodomain screen. Reason: Receptor homomerization is real but is not a distinct function. Supporting Evidence: PMID:20626648 We observed robust co-IP between CLV1-CLV1, CLV1-BAM1, CLV1-BAM2, BAM1-BAM1, and BAM1-BAM2 PMID:29320478 produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions |
| GO:0048229 gametophyte development | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: bam1 bam2 mutants are defective in early anther cell-layer specification, and BAM1/2/3 are needed for male gametophyte development and ovule function. Reason: This is a genuine developmental role, separate from the shoot meristem CLV3 receptor role. Supporting Evidence: PMID:16751349 bam1 bam2 anthers appear to be abnormal at a very early stage and lack the endothecium, middle, and tapetum layers. PMID:16367950 BAM1, BAM2 and BAM3 are required for male gametophyte development, as well as ovule specification and function. |
| GO:0048229 gametophyte development | IGI PMID:16367950 The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-lik... | KEEP AS NON CORE | Summary: bam1 bam2 mutants are defective in early anther cell-layer specification, and BAM1/2/3 are needed for male gametophyte development and ovule function. Reason: This is a genuine developmental role, separate from the shoot meristem CLV3 receptor role. Supporting Evidence: PMID:16751349 bam1 bam2 anthers appear to be abnormal at a very early stage and lack the endothecium, middle, and tapetum layers. PMID:16367950 BAM1, BAM2 and BAM3 are required for male gametophyte development, as well as ovule specification and function. |
| GO:0048437 floral organ development | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: BAM receptors are needed for normal flower organ development, including anther development. Reason: This is a pleiotropic developmental role. Supporting Evidence: PMID:16751349 bam1 bam2 anthers appear to be abnormal at a very early stage and lack the endothecium, middle, and tapetum layers. PMID:16367950 Loss-of-function alleles of these receptors lead to phenotypes consistent with the loss of stem cells at the shoot and flower meristem |
| GO:0048437 floral organ development | IGI PMID:16367950 The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-lik... | KEEP AS NON CORE | Summary: BAM receptors are needed for normal flower organ development, including anther development. Reason: This is a pleiotropic developmental role. Supporting Evidence: PMID:16751349 bam1 bam2 anthers appear to be abnormal at a very early stage and lack the endothecium, middle, and tapetum layers. PMID:16367950 Loss-of-function alleles of these receptors lead to phenotypes consistent with the loss of stem cells at the shoot and flower meristem |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | ACCEPT | Summary: BAM1 is a Ser/Thr receptor kinase, and phosphorylation of serine residues on substrates is expected. The annotation is based on similarity and Rhea mapping. Reason: This is consistent with the demonstrated Ser/Thr kinase activity. Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0106310 protein serine kinase activity | ISS GO_REF:0000024 | ACCEPT | Summary: BAM1 is a Ser/Thr receptor kinase, and phosphorylation of serine residues on substrates is expected. The annotation is based on similarity and Rhea mapping. Reason: This is consistent with the demonstrated Ser/Thr kinase activity. Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. |
| GO:0007178 cell surface receptor protein serine/threonine kinase signaling pathway | IDA PMID:34935965 Receptor-like cytoplasmic kinases PBL34/35/36 are required f... | NEW | Summary: CLE perception by BAM1 leads to phosphorylation of CIK co-receptors and PBL34/35/36 and to CLV3-induced MPK3/6 activation, which is a receptor Ser/Thr kinase signalling cascade. Reason: This is the receptor-level process, in place of the generic intracellular signal transduction and hormone-mediated signaling terms. Supporting Evidence: PMID:34935965 Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. PMID:34935965 The CLV3-activated phosphorylation of MPK3 and MPK6 is dependent on CLV1 and BAM1. PMID:34651321 CLE25/26/45 enhanced the phosphorylation levels of CIKs, which were greatly impaired in clv1 bam1 3 mutant |
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Download this section (compressed HTML)Q: Is BAM1 in the meristem periphery mainly a signalling receptor or a ligand sink that sequesters CLV3/CLE peptides, as suggested by suppression of clv3 by bam1 bam2?
Q: Which CLE ligands activate BAM1 in anther and ovule development?
Experiment: Express kinase-dead BAM1 (or BAM1 lacking its kinase domain) from the BAM1 promoter in clv1 bam1 and clv3 bam1 bam2 backgrounds, and compare rescue of WUS expression and meristem size.
Hypothesis: BAM1 restricts the stem cell niche through kinase-dependent signalling at the centre and acts as a kinase-independent ligand sink at the periphery.
Type: genetic complementation
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