Database accession: MF7000703
Name: CDC15 F-BAR Domain (Schizosaccharomyces pombe)
PDB ID: 6xj1
Experimental method: X-ray (3.52 Å)
Assembly: Homodimer
Source organism: Schizosaccharomyces pombe
Primary publication of the structure:
Snider CE, Chandra M, McDonald NA, Willet AH, Collier SE, Ohi MD, Jackson LP, Gould KL
Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.
(2020) Cell Rep 33: 108526
PMID: 33357436
Abstract:
Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
cytoskeletal protein-membrane anchor activity cytoskeletal protein-membrane anchor activity
phospholipid binding phospholipid binding
Biological process:
clathrin-dependent endocytosis clathrin-dependent endocytosis
cytoskeleton organization cytoskeleton organization
establishment of bipolar cell polarity establishment of bipolar cell polarity
mitotic actomyosin contractile ring assembly mitotic actomyosin contractile ring assembly
Cellular component:
actin cortical patch actin cortical patch
cell division site cell division site
cell tip cell tip
cytoplasm cytoplasm
cytoplasmic side of plasma membrane cytoplasmic side of plasma membrane
mating projection tip mating projection tip
medial cortical node medial cortical node
medial membrane band medial membrane band
mitotic actomyosin contractile ring mitotic actomyosin contractile ring
mitotic actomyosin contractile ring, proximal layer mitotic actomyosin contractile ring, proximal layer
plasma membrane plasma membrane
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Cell division control protein 15
Source organism: Schizosaccharomyces pombe
Length: 927 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV
UniProtKB AC: Q09822 (positions: 35-300)
Coverage: 28%
Name: Cell division control protein 15
Source organism: Schizosaccharomyces pombe
Length: 927 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV
UniProtKB AC: Q09822 (positions: 22-298)
Coverage: 29%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: F-BAR domain
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
