mbinfo MBInfo http://www.mechanobio.info/ Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. (1465-7392) 1999 imex curation Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions human-kidney Human kidney kidney kidney [Renal] anti bait coip anti bait coimmunoprecipitation anti bait coip anti tag western anti tag western blot anti tag western Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu Accepted 2012-SEP-18 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. Nat. Cell Biol. (1465-7392) 1999 Only protein-protein interactions imex curation Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. (1465-7392) 1999 imex curation Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions human-a_431 Homo sapiens epidermoid carcinoma a_431 Human epidermoid carcinoma anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu Accepted 2012-SEP-18 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. Nat. Cell Biol. (1465-7392) 1999 Only protein-protein interactions imex curation Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. (1465-7392) 1999 imex curation Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down autoradiography autoradiography Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu Accepted 2012-SEP-18 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. Nat. Cell Biol. (1465-7392) 1999 Only protein-protein interactions imex curation Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. (1465-7392) 1999 imex curation Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay autoradiography autoradiography Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu Accepted 2012-SEP-18 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. Nat. Cell Biol. (1465-7392) 1999 Only protein-protein interactions imex curation Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. (1465-7392) 1999 imex curation Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. To test the activation effect of Pak1 on LIMK1, the rate of cofilin phosphorylation by LIMK1 was calculated by measuring the incorporation of radiolabelled-P into Ser3 of cofilin. Inferred from the paper, all human LIMK1 proteins were purified from HEK293 cells in Fig.1a, b & Fig. 2Ab; whereas the kinase domains of the human LIMK1 in Fig. 1c & Fig. 2Aa, B were purified from the baculovirus-infected SF-21 cells. Inferred from the reference paper (PMID: 7618083), all PAK1 proteins were purified from E.coli cells. bokoch@scripps.edu;ggill@ucsd.edu Accepted 2012-SEP-18 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. Nat. Cell Biol. (1465-7392) 1999 Only protein-protein interactions imex curation limk1_human LIM domain kinase 1 LIMK1 LIMK protein protein human Homo sapiens Human MRLTLLCCTWREERMGEEGSELPVCASCGQRIYDGQYLQALNADWHADCFRCCDCSASLSHQYYEKDGQLFCKKDYWARYGESCHGCSEQITKGLVMVAGELKYHPECFICLTCGTFIGDGDTYTLVEHSKLYCGHCYYQTVVTPVIEQILPDSPGSHLPHTVTLVSIPASSHGKRGLSVSIDPPHGPPGCGTEHSHTVRVQGVDPGCMSPDVKNSIHVGDRILEINGTPIRNVPLDEIDLLIQETSRLLQLTLEHDPHDTLGHGLGPETSPLSSPAYTPSGEAGSSARQKPVLRSCSIDRSPGAGSLGSPASQRKDLGRSESLRVVCRPHRIFRPSDLIHGEVLGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSQYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKNVVVADFGLARLMVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPSFFPITVRCCDLDPEKRPSFVKLEHWLETLRMHLAGHLPLGPQLEQLDRGFWETYRRGESGLPAHPEVPD DIP protein P53667 original sequence version: 113 9838BEFBE7006447 pak1_human Serine/threonine-protein kinase PAK 1 PAK1 p21-activated kinase 1 p65-PAK Alpha-PAK protein protein human Homo sapiens Human MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH DIP protein Q13153 original sequence version: 161 DIP protein Q13153 original sequence version: 122 DIP protein Q13153 original sequence version: 134 DIP protein Q13153 original sequence version: 165 1A95CD5F2195CD7B limk1-pak1 4 6 enzyme target enzyme target substrate substrate unspecified role unspecified role kinase domain activation domain activation domain tag activation domain certain certain sequence position certain certain certain sequence position certain spofr-sf_21 Spodoptera frugiperda insect cells sf_21 Insect cells derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae. full name: IPLB-SF-21-AE cells are susceptible to Baculovirus infection. Pak1 7 enzyme enzyme unspecified role unspecified role Q13153:p.Thr423Glu mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain T E Wed May 02 19:01:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr423glu' Tue Jun 30 20:25:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr423Glu' The mutation for the constitutively activated form of Pak1 protein is inferred from the reference paper. (PMID: 10551809) region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation Fig1. c pak1-limk1 2 7 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey physical association physical association Fig. 3a limk1-pak1 1 7 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Fig. 3b Constitutively activated Rac(Q61L) enhanced complex formation between Pak and LIMK1, compared with the complex formation induced by inactive Rac(T17N). pak1-limk1 3 7 unspecified role unspecified role bait bait region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain LIMK1 binds to the region between amino acids 67 to 150 in the Pak1 N terminus, which contains the p21-binding domain (amino acids 67-86) and the autoinhibitory regulatory domain (amino acids 83-149). ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 autoradiography autoradiography undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association Fig. 3c LIMK1 binds to a region of Pak1 that includes its autoinhibitory domain, and this interaction is increased by Rac or Cdc42 binding to the p21-binding domain of Pak1. limk1-limk1 4 6 putative self putative self putative self putative self human-kidney Human kidney kidney kidney [Renal] phosphorylation phosphorylation reaction phosphorylation true Fig. 2Ab pak1-pak1 4 7 putative self putative self putative self putative self ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation true Fig. 2Ab limk1-pak1-1 5 7 unspecified role unspecified role neutral component neutral component nucl transfection nucleic acid transfection nucl transfection region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 unspecified role unspecified role neutral component neutral component nucl transfection nucleic acid transfection nucl transfection colocalization colocalization Fig. 7