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 Live-cell single-molecule imaging reveals clathrin and caveolin-1 dependent docking of SMAD4 at the cell membrane. Live-cell single-molecule imaging reveals clathrin and caveolin-1 dependent docking of SMAD4 at the cell membrane. FEBS letters 2013 imex curation Yong Yang1*, Joy Wolfram1,2, Jianliang Shen1, Yuliang Zhao2,3, Xiaohong Fang4, Haifa Shen1,5 & Mauro Ferrari, Yang Y., Wolfram J., Shen J., Zhao Y., Fang X., Shen H., Ferrari M. yyang@tmhs.org 22-Nov-2013: Contacted by IntAct-Help. Only protein-protein interactions human-mda_mb_231 Homo sapiens Caucasian breast adenocarcinoma mda_mb_231 Human Caucasian breast adenocarcinoma fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Yong Yang1*, Joy Wolfram1,2, Jianliang Shen1, Yuliang Zhao2,3, Xiaohong Fang4, Haifa Shen1,5 & Mauro Ferrari yyang@tmhs.org Accepted 2013-OCT-30 by LUANA 22-Nov-2013: Contacted by IntAct-Help. 2013 Only protein-protein interactions imex curation smad4_human Mothers against decapentaplegic homolog 4 SMAD4 DPC4 MADH4 SMAD family member 4 Deletion target in pancreatic carcinoma 4 protein protein human Homo sapiens Human MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD DIP protein Q13485 original sequence version: 149 DIP protein Q13485 original sequence version: 177 7EE3C4647712DA90 cav1_human Caveolin-1 CAV1 CAV protein protein human Homo sapiens Human MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI DIP protein Q03135 original sequence version: 164 DIP protein Q03135 original sequence version: 119 DIP protein Q03135 original sequence version: 122 DIP protein Q03135-1 original sequence version: 122 DIP protein Q03135 original sequence version: 133 DIP protein Q03135 original sequence version: 155 DIP protein Q03135 original sequence version: 147 2424DE9B5E6521D5 cav1-smad4 1 caveolin-1 3 immunostaining immunostaining immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell SMAD4 2 immunostaining immunostaining immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization f2a Using immunofluorescence imaging of fixed cells, we studied the potential colocalization between SMAD4 and clathrin or caveolin-1. Indeed, there were regions on the cell membrane were the proteins co-localized (Fig. 2A). The partition coefficient for co-localization of SMAD4 with clathrin or caveolin-1 was approximately 29% and 44%, respectively.