bhf-ucl markandeya-2011-1 Caveolin-3 regulates protein kinase A modulation of the Ca(V)3.2 (alpha1H) T-type Ca2+ channels. mouse-ventricular myocyte_neo Mus musculus neonatal_ventricular_myocyte neonatal ventricular myocyte A heart muscle cell. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Markandeya Y.S., Fahey J.M., Pluteanu F., Cribbs L.L., Balijepalli R.C. Cardiac - Interactions involving cardiac related proteins rcb@medicine.wisc.edu J. Biol. Chem. (0021-9258) 2011 imex curation Only protein-protein interactions markandeya-2011-2 Caveolin-3 regulates protein kinase A modulation of the Ca(V)3.2 (alpha1H) T-type Ca2+ channels. human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Markandeya Y.S., Fahey J.M., Pluteanu F., Cribbs L.L., Balijepalli R.C. Cardiac - Interactions involving cardiac related proteins rcb@medicine.wisc.edu J. Biol. Chem. (0021-9258) 2011 imex curation Only protein-protein interactions markandeya-2011-3 Caveolin-3 regulates protein kinase A modulation of the Ca(V)3.2 (alpha1H) T-type Ca2+ channels. mouse-ventricular myocyte_neo Mus musculus neonatal_ventricular_myocyte neonatal ventricular myocyte A heart muscle cell. electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy immunostaining immunostaining Markandeya Y.S., Fahey J.M., Pluteanu F., Cribbs L.L., Balijepalli R.C. Cardiac - Interactions involving cardiac related proteins rcb@medicine.wisc.edu J. Biol. Chem. (0021-9258) 2011 imex curation Only protein-protein interactions markandeya-2011-4 Caveolin-3 regulates protein kinase A modulation of the Ca(V)3.2 (alpha1H) T-type Ca2+ channels. in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Markandeya Y.S., Fahey J.M., Pluteanu F., Cribbs L.L., Balijepalli R.C. Cardiac - Interactions involving cardiac related proteins rcb@medicine.wisc.edu J. Biol. Chem. (0021-9258) 2011 imex curation Only protein-protein interactions q6pe92_mouse Cacna1h protein protein mouse Mus musculus Mouse MTEGTLAADEVRVPLGASPSAPAAPVRASPASPGVPGREEQRGSGSSVLAPESPGTECGADLGADEEQPVPYPALAATVFFCLGQTTRPRSWCLRLVCNPWFEHISMLVIMLNCVTLGMFRPCEDVECRSERCSILEAFDDFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVMAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPSRRELRVQCTLGWEAYGQPQAEDGGAGRNACINWNQYYNVCRSGEFNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRENQLMREQRARYLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSSTLHGQGPRRRPRRAGRRTASVHHLVHHHHHHQKKKKKKKKKKKKKKK cav3_mouse Caveolin-3 Cav3 M-caveolin protein protein mouse Mus musculus Mouse MMTEEHTDLEARIIKDIHCKEIDLVNRDPKNINEDIVKVDFEDVIAEPEGTYSFDGVWKVSFTTFTVSKYWCYRLLSTLLGVPLALLWGFLFACISFCHIWAVVPCIKSYLIEIQCISHIYSLCIRTFCNPLFAALGQVCSNIKVVLRREG q5sug4_mouse Voltage-dependent T-type calcium channel subunit alpha Cacna1g protein protein mouse Mus musculus Mouse MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAVGVRAGLLSSPVARGGQEPQPSGSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRWLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPEMLKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHEMPDSDSEAVYEFTQDAQHSDLRDPHRRRRPSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEEIGKREDTSGQLSCIQLPVNSQGGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHSELRKSLLPPLIIHTAATPMSLPKSSSTGVGEALGSGSRRTSSSGSAEPGTAHHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRADDPPLDGDDGDDEGNLSKGERLRAWVRARLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLKRLEKKRRSKEKQMADLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSPDSPKPGAPHTTAHIGAASSGFSLEHPTMVPHTEEGPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDAHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGSQSKVSKHIRLPAPCPGLEPSWAKDPQETRSSLELDTELSWISGDLLPSSQEEPLSPRDLKKCYSVEAQSCRRRPGSWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGPRPPCSPGVCLRRRAPASDSKDPSASSPLDSTAASPSPKKDALSLSGLSSDPTDLDP cav3-cacna1h-3 1431506 n/a 1431510 unspecified role unspecified role prey prey n/a 1431511 unspecified role unspecified role bait bait physical association physical association false false false Fig. 1B cacna1h-cav3 1431506 n/a 1431511 unspecified role unspecified role prey prey n/a 1431510 unspecified role unspecified role bait bait physical association physical association false false false Fig. 1B cav3-cacna1g 1431506 n/a 1431512 unspecified role unspecified role prey prey n/a 1431511 unspecified role unspecified role bait bait physical association physical association false false false Fig. 1A cacna1g-cav3 1431506 n/a 1431512 unspecified role unspecified role bait bait n/a 1431511 unspecified role unspecified role prey prey physical association physical association false false false Fig. 1A cav3-cacna1h-4 1431507 n/a 1431510 unspecified role unspecified role prey prey n/a 1431511 unspecified role unspecified role bait bait physical association physical association false false false Fig. 1c cav3-cacna1g-1 1431507 n/a 1431512 unspecified role unspecified role prey prey n/a 1431511 unspecified role unspecified role bait bait physical association physical association false false false Fig. 1c cacna1h-cav3-2 1431508 n/a 1431510 unspecified role unspecified role neutral component neutral component n/a 1431511 unspecified role unspecified role neutral component neutral component colocalization colocalization false false false Fig. 2 cav3-cacna1h-6 1431509 n/a 1431510 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. n/a 1431511 unspecified role unspecified role bait bait n-terminal 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 n-terminal required to bind necessary binding region required to bind western blot western blot Immuno blot Immuno blot certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) physical association physical association false false false Fig. 4B (and A) The authors discuss that: although it is clear from our GST-Cav-3 pulldown experiments that the N terminus region of Cav-3 interacts with the Cav3.2 channel and modulates the ICav3.2, there exists a likely possibility of direct interaction between the Cav3.2 channel and Cav-3. The intracellular linker region between domains II and III for the Cav3.2 channel contains clusters of serine and threonine residues and has been identified as an important region for interaction and regulation of the channel by serine/threonine kinases and G-protein signaling pathway proteins (3). In this context, it may not be unreasonable to hypothesize an interaction between the N terminus region of Cav-3 and the intracellular loop between domains II and III of the Cav3.2 channel. Further studies are needed to identify the site of Cav3.2 channel involved in the interaction with Cav-3, which may also help us understand dynamic regulation of the Cav3.2 channels.