mbinfo MBInfo http://www.mechanobio.info/ http://www.mechanobio.info/ suetsugu-2006-1 The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Suetsugu S., Murayama K., Sakamoto A., Hanawa-Suetsugu K., Seto A., Oikawa T., Mishima C., Shirouzu M., Takenawa T., Yokoyama S. Interaction detection: GST pull down. Participant detection: western blot results were quantitated by densitometry. The source of Rac1 traced from references [PMID: 7476445] and the source of IRSp53 specified by the author. yokoyama@biochem.s.u-tokyo.ac.jp J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation suetsugu-2006-2 The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. in vitro In vitro biosensor biosensor predetermined predetermined participant predetermined Suetsugu S., Murayama K., Sakamoto A., Hanawa-Suetsugu K., Seto A., Oikawa T., Mishima C., Shirouzu M., Takenawa T., Yokoyama S. Interaction detection: GST pull down. Participant detection: western blot results were quantitated by densitometry. The source of Rac1 traced from references [PMID: 7476445] and the source of IRSp53 specified by the author. yokoyama@biochem.s.u-tokyo.ac.jp J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation baip2_human Brain-specific angiogenesis inhibitor 1-associated protein 2 Insulin receptor substrate protein of 53 kDa Insulin receptor substrate p53/p58 Fas ligand-associated factor 3 BAIAP2 protein protein human Homo sapiens Human MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR rac1_human Ras-related C3 botulinum toxin substrate 1 RAC1 MIG5 p21-Rac1 Ras-like protein TC25 Cell migration-inducing gene 5 protein TC25 protein protein human Homo sapiens Human MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL baiap2-rac1-2 1317100 n/a 1317102 unspecified role unspecified role bait bait Q9UQB8:p.Lys143Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false Q9UQB8:p.[Arg11Glu;Gln23Glu] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false Q9UQB8:p.[Lys143Glu;Lys147Glu] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false Q9UQB8:p.Gln23Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false n-terminal region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false Q9UQB8:p.[Lys142Ala;Lys143Ala;Arg145Ala;Lys146Ala;Lys147Ala] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) n/a 1317103 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association false false false Fig 2E. Rac1 was GTPgammaS-loaded. baiap2-rac1-3 1317101 n/a 1317102 unspecified role unspecified role bait bait rcb domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false n-terminal region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecoli Escherichia coli (strain K12) n/a 1317103 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association false false false 1317101 Fig 3B. IRSp53-RCB bound strongly only to the GTPgammaS-loaded Rac1. The interaction was greatly decreased with GDP-loaded Rac1.