MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Advanced glycation end-products induce calpain-mediated degradation of ezrin. Advanced glycation end-products induce calpain-mediated degradation of ezrin. FEBS J. (1742-464X) 2012 McRobert EA., Young AN., Bach LA. Anne.McRobert@monash.edu in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined McRobert EA., Young AN., Bach LA. Anne.McRobert@monash.edu FEBS J. (1742-464X) 2012 can1_human Calpain-1 catalytic subunit CAPN1 CANPL1 Calpain-1 large subunit Calcium-activated neutral proteinase 1 Calpain mu-type Micromolar-calpain Cell proliferation-inducing gene 30 protein PIG30 protein protein human Homo sapiens Human MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA 1CB6D7C56D063498 ezri_human Ezrin EZR VIL2 p81 Cytovillin Villin-2 protein protein human Homo sapiens Human MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL DIP protein P15311 original sequence version: 170 DIP protein P15311 original sequence version: 142 F1B592CF49A7CC46 capn1-ezr 1 Ezrin 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified Calpain-1 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified cleavage cleavage reaction cleavage homomint mint Calpain cleavage of ezrin resulted in a rapid loss of the C-terminus as observed by the immediate loss of a C-terminal monoclonal antibody epitope (aa 391-515) (Figure 5B). The main breakdown product (~43 kDa) was recognized by a specific N-terminal antibody (Figure 5C) but not by the C-terminal ezrin antibody (Figure 5B). Inclusion of PIP2 to the ezrin: calpain reaction mixture reduced the susceptibility of ezrin to calpain cleavage (Figure 7). Cleavage was inhibited by EGTA (a calcium chelator), leupeptin (a trypsin-like and cysteine protease inhibitor), and calpastatin peptide (a calpain 1 and 2 inhibitor), but not by aprotonin (a serine protease inhibitor, Supplementary Figure 3). f5 f7 sf3 capn1-ezr-1 1 Ezrin 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified P15311:p.Thr567Asp mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain T D Tue Jul 12 10:56:44 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 15:30:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr567asp' Tue Jun 30 16:07:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr567Asp' gst tag 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 Calpain-1 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified cleavage cleavage reaction cleavage f6b homomint mint To determine whether Thr567 phosphorylation is linked to the susceptibility of ezrin to calpain cleavage, ezrin was mutated at Thr567 to be constitutively active (T567D, EmD) or to be unphosphorylatable and inactive (T567A, EmA)After 5 min incubation with calpain 1, considerable cleavage of wild-type ezrin and EmA was observed whereas EmD was still resistant to cleavage after 20 min (Figure 6B, C)