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A GAIN in understanding autoproteolytic G protein‐coupled receptors and polycystic kidney disease proteins
dc.contributor.authorTesmer, John J Gen_US
dc.date.accessioned2014-01-08T20:34:48Z
dc.date.available2014-01-08T20:34:48Z
dc.date.issued2012-03-21en_US
dc.identifier.citationTesmer, John J G (2012). "A GAIN in understanding autoproteolytic G protein‐coupled receptors and polycystic kidney disease proteins." The EMBO Journal 31(6): 1334-1335. <http://hdl.handle.net/2027.42/102153>en_US
dc.identifier.issn0261-4189en_US
dc.identifier.issn1460-2075en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/102153
dc.publisherJohn Wiley & Sons, Ltden_US
dc.titleA GAIN in understanding autoproteolytic G protein‐coupled receptors and polycystic kidney disease proteinsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.identifier.pmid22388517en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/102153/1/embj201251.pdf
dc.identifier.doi10.1038/emboj.2012.51en_US
dc.identifier.sourceThe EMBO Journalen_US
dc.identifier.citedreferenceAraç D, Boucard AA, Bolliger MF, Nguyen J, Soltis SM, Südhof TC, Brunger AT ( 2012 ) A novel evolutionarily conserved domain of cell‐adhesion GPCRs mediates autoproteolysis. EMBO J 31: 1364 – 1378en_US
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dc.identifier.citedreferenceIchtchenko K, Bittner MA, Krasnoperov V, Little AR, Chepurny O, Holz RW, Petrenko AG ( 1999 ) A novel ubiquitously expressed α‐latrotoxin receptor is a member of the CIRL family of G‐protein‐coupled receptors. J Biol Chem 274: 5491 – 5498en_US
dc.identifier.citedreferenceKrasnoperov V, Lu Y, Buryanovsky L, Neubert TA, Ichtchenko K, Petrenko AG ( 2002 ) Post‐translational proteolytic processing of the calcium‐independent receptor of α‐latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein‐coupled receptor. Role of the G protein‐coupled receptor proteolysis site (GPS) motif. J Biol Chem 277: 46518 – 46526en_US
dc.identifier.citedreferenceLin HH, Chang GW, Davies JQ, Stacey M, Harris J, Gordon S ( 2004 ) Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein‐coupled receptor proteolytic site motif. J Biol Chem 279: 31823 – 31832en_US
dc.identifier.citedreferencePaavola KJ, Stephenson JR, Ritter SL, Alter SP, Hall RA ( 2011 ) The N terminus of the adhesion G protein‐coupled receptor GPR56 controls receptor signaling activity. J Biol Chem 286: 28914 – 28921en_US
dc.identifier.citedreferenceQian F, Boletta A, Bhunia AK, Xu H, Liu L, Ahrabi AK, Watnick TJ, Zhou F, Germino GG ( 2002 ) Cleavage of polycystin‐1 requires the receptor for egg jelly domain and is disrupted by human autosomal‐dominant polycystic kidney disease 1‐associated mutations. Proc Natl Acad Sci USA 99: 16981 – 16986en_US
dc.identifier.citedreferenceSilva JP, Ushkaryov YA ( 2010 ) The latrophilins, ‘split‐personality’ receptors. Adv Exp Med Biol 706: 59 – 75en_US
dc.identifier.citedreferenceYona S, Lin HH, Siu WO, Gordon S, Stacey M ( 2008 ) Adhesion‐GPCRs: emerging roles for novel receptors. Trends Biochem Sci 33: 491 – 500en_US
dc.identifier.citedreferenceYu S, Hackmann K, Gao J, He X, Piontek K, Garcia‐Gonzalez MA, Menezes LF, Xu H, Germino GG, Zuo J, Qian F ( 2007 ) Essential role of cleavage of polycystin‐1 at G protein‐coupled receptor proteolytic site for kidney tubular structure. Proc Natl Acad Sci USA 104: 18688 – 18693en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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