IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1). Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1). Plant Cell (1040-4651) 2004 Russinova E., Borst JW., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries SC. In some instances FM4-64 a lipophillic dye was used , which labels membranes and is commonly used in vesicle trafficking studies in in plant cells. sacco.devries@wur.nl 16-Oct-2008: Contacted by JYOTI. orchard vigun Vigna unguiculata (Cowpea) confocal microscopy confocal microscopy tag fluorescence tag visualisation by fluorescence tag fluorescence Russinova E., Borst JW., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries SC. In some instances FM4-64 a lipophillic dye was used , which labels membranes and is commonly used in vesicle trafficking studies in in plant cells. sacco.devries@wur.nl Accepted 2008-SEP-26 by ORCHARD. 16-Oct-2008: Contacted by JYOTI. Plant Cell (1040-4651) 2004 orchard Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1). Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1). Plant Cell (1040-4651) 2004 Russinova E., Borst JW., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries SC. In some instances FM4-64 a lipophillic dye was used , which labels membranes and is commonly used in vesicle trafficking studies in in plant cells. sacco.devries@wur.nl 16-Oct-2008: Contacted by JYOTI. orchard vigun Vigna unguiculata (Cowpea) fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret tag fluorescence tag visualisation by fluorescence tag fluorescence Russinova E., Borst JW., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries SC. In some instances FM4-64 a lipophillic dye was used , which labels membranes and is commonly used in vesicle trafficking studies in in plant cells. sacco.devries@wur.nl Accepted 2008-SEP-26 by ORCHARD. 16-Oct-2008: Contacted by JYOTI. Plant Cell (1040-4651) 2004 orchard bak1_arath BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 BAK1 SERK3 At4g33430 F17M5.190 Somatic embryogenesis receptor-like kinase 3 ELG Somatic embryogenesis receptor kinase 3 Protein ELONGATED protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR DIP protein Q94F62 original sequence version: 119 DIP protein Q94F62 original sequence version: 129 DIP protein Q94F62 original sequence version: 94 DIP protein Q94F62 original sequence version: 100 DIP protein Q94F62 original sequence version: 139 DIP protein Q94F62 original sequence version: 121 DIP protein Q94F62 original sequence version: 141 DIP protein Q94F62 original sequence version: 113 547B3F38FB46E1DD brl1_arath Serine/threonine-protein kinase BRI1-like 1 BRL1 At1g55610 F20N2.4 BRASSINOSTEROID INSENSITIVE 1-like protein 1 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MKQRWLLVLILCFFTTSLVMGIHGKHLINDDFNETALLLAFKQNSVKSDPNNVLGNWKYESGRGSCSWRGVSCSDDGRIVGLDLRNSGLTGTLNLVNLTALPNLQNLYLQGNYFSSGGDSSGSDCYLQVLDLSSNSISDYSMVDYVFSKCSNLVSVNISNNKLVGKLGFAPSSLQSLTTVDLSYNILSDKIPESFISDFPASLKYLDLTHNNLSGDFSDLSFGICGNLTFFSLSQNNLSGDKFPITLPNCKFLETLNISRNNLAGKIPNGEYWGSFQNLKQLSLAHNRLSGEIPPELSLLCKTLVILDLSGNTFSGELPSQFTACVWLQNLNLGNNYLSGDFLNTVVSKITGITYLYVAYNNISGSVPISLTNCSNLRVLDLSSNGFTGNVPSGFCSLQSSPVLEKILIANNYLSGTVPMELGKCKSLKTIDLSFNELTGPIPKEIWMLPNLSDLVMWANNLTGTIPEGVCVKGGNLETLILNNNLLTGSIPESISRCTNMIWISLSSNRLTGKIPSGIGNLSKLAILQLGNNSLSGNVPRQLGNCKSLIWLDLNSNNLTGDLPGELASQAGLVMPGSVSGKQFAFVRNEGGTDCRGAGGLVEFEGIRAERLERLPMVHSCPATRIYSGMTMYTFSANGSMIYFDISYNAVSGFIPPGYGNMGYLQVLNLGHNRITGTIPDSFGGLKAIGVLDLSHNNLQGYLPGSLGSLSFLSDLDVSNNNLTGPIPFGGQLTTFPVSRYANNSGLCGVPLRPCGSAPRRPITSRIHAKKQTVATAVIAGIAFSFMCFVMLVMALYRVRKVQKKEQKREKYIESLPTSGSCSWKLSSVPEPLSINVATFEKPLRKLTFAHLLEATNGFSAETMVGSGGFGEVYKAQLRDGSVVAIKKLIRITGQGDREFMAEMETIGKIKHRNLVPLLGYCKVGEERLLVYEYMKWGSLETVLHEKSSKKGGIYLNWAARKKIAIGAARGLAFLHHSCIPHIIHRDMKSSNVLLDEDFEARVSDFGMARLVSALDTHLSVSTLAGTPGYVPPEYYQSFRCTAKGDVYSYGVILLELLSGKKPIDPGEFGEDNNLVGWAKQLYREKRGAEILDPELVTDKSGDVELFHYLKIASQCLDDRPFKRPTMIQLMAMFKEMKADTEEDESLDEFSLKETPLVEESRDKEP 8C4DD9231A466AF7 brl1-bak1-3 1 4 unspecified role unspecified role neutral component neutral component c-terminal yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 3 unspecified role unspecified role neutral component neutral component c-terminal cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range colocalization colocalization Figure 1U Figure 1W Figure 3 An interesting observation in the BRI1/AtSERK3 coexpression experiments was the lack of complete colocalization between the two fluorescently tagged proteins in the endosomes The authors noted the existence of "three different types of vesicle-like compartments, compartments that contained BRI1 and AtSERK3 together and compartments that contained either AtSERK3". The authors also noted that "most of the BRI1- and AtSERK3-containing vesicles are stained with FM4-64, suggesting that BRI1 and AtSERK3 proteins are indeed recycled and internalized via an endocytic mechanism". brl1-bak1-4 2 3 unspecified role unspecified role fluorescence donor fluorescence donor c-terminal cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 4 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept c-terminal yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range direct interaction direct interaction Figure 4I Figure 4J Figure H We conclude that BRI1-AtSERK3 heterodimerization is nonuniformly distributed in the plasma membrane and appears to coincide with developing endocytic compartments that contain both receptors. The authors concluded "BRI1-AtSERK3 heterodimerization is nonuniformly distributed in the plasma membrane and appears to coincide with developing endocytic compartments that contain both receptors". brl1-1 2 4 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept c-terminal yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 4 unspecified role unspecified role fluorescence donor fluorescence donor c-terminal cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range direct interaction direct interaction Figure 4D The areas where BRI1/BRI1 homodimers in the plasma membrane occur do not appear to be organized but are fairly frequent (note the dark orange areas indicated by arrowheads in Figure 4D). The authors concluded "where BRI1/BRI1 homodimers in the plasma membrane occur do not appear to be organized but are fairly frequent".