[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND MUTANTS BRI1-101; BRI1-104; BRI1-113 AND BRI1-115.
STRAIN=cv. Columbia;
DOI=10.1016/S0092-8674(00)80357-8; PubMed=9298904 [NCBI, ExPASy, EBI, Israel, Japan]
Li J.,
Chory J.;
"A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction.";
Cell 90:929-938(1997).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTANTS BRI1-5/DWF2-W41; BRI1-6/BRI1-119/DWF2-399; BRI1-7/DWF2-WM3-2; BRI1-8/DWF2-WM6-2 AND BRI1-9/DWF2-WMB19.
STRAIN=cv. En-2, and cv. Wassilewskija-2;
DOI=10.1104/pp.121.3.743; PubMed=10557222 [NCBI, ExPASy, EBI, Israel, Japan]
Noguchi T.,
Fujioka S.,
Choe S.,
Takatsuto S.,
Yoshida S.,
Yuan H.,
Feldmann K.A.,
Tax F.E.;
"Brassinosteroid-insensitive dwarf mutants of Arabidopsis accumulate brassinosteroids.";
Plant Physiol. 121:743-752(1999).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTANTS BRI1-1; BRI1-108; BRI1-117 AND BRI1-102.
STRAIN=cv. Columbia;
DOI=10.1104/pp.123.4.1247; PubMed=10938344 [NCBI, ExPASy, EBI, Israel, Japan]
Friedrichsen D.M.,
Joazeiro C.A.P.,
Li J.,
Hunter T.,
Chory J.;
"BRASSINOSTEROID-INSENSITIVE-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase.";
Plant Physiol. 123:1247-1256(2000).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X.,
Schueller C.,
Wambutt R.,
Murphy G.,
Volckaert G.,
Pohl T.,
Duesterhoeft A.,
Stiekema W.,
Entian K.-D.,
Terryn N.,
Harris B.,
Ansorge W.,
Brandt P.,
Grivell L.A.,
Rieger M.,
Weichselgartner M.,
de Simone V.,
Obermaier B.,
Mache R.,
Mueller M.,
Kreis M.,
Delseny M.,
Puigdomenech P.,
Watson M.,
Schmidtheini T.,
Reichert B.,
Portetelle D.,
Perez-Alonso M.,
Boutry M.,
Bancroft I.,
Vos P.,
Hoheisel J.,
Zimmermann W.,
Wedler H.,
Ridley P.,
Langham S.-A.,
McCullagh B.,
Bilham L.,
Robben J.,
van der Schueren J.,
Grymonprez B.,
Chuang Y.-J.,
Vandenbussche F.,
Braeken M.,
Weltjens I.,
Voet M.,
Bastiaens I.,
Aert R.,
Defoor E.,
Weitzenegger T.,
Bothe G.,
Ramsperger U.,
Hilbert H.,
Braun M.,
Holzer E.,
Brandt A.,
Peters S.,
van Staveren M.,
Dirkse W.,
Mooijman P.,
Klein Lankhorst R.,
Rose M.,
Hauf J.,
Koetter P.,
Berneiser S.,
Hempel S.,
Feldpausch M.,
Lamberth S.,
Van den Daele H.,
De Keyser A.,
Buysshaert C.,
Gielen J.,
Villarroel R.,
De Clercq R.,
van Montagu M.,
Rogers J.,
Cronin A.,
Quail M.A.,
Bray-Allen S.,
Clark L.,
Doggett J.,
Hall S.,
Kay M.,
Lennard N.,
McLay K.,
Mayes R.,
Pettett A.,
Rajandream M.A.,
Lyne M.,
Benes V.,
Rechmann S.,
Borkova D.,
Bloecker H.,
Scharfe M.,
Grimm M.,
Loehnert T.-H.,
Dose S.,
de Haan M.,
Maarse A.C.,
Schaefer M.,
Mueller-Auer S.,
Gabel C.,
Fuchs M.,
Fartmann B.,
Granderath K.,
Dauner D.,
Herzl A.,
Neumann S.,
Argiriou A.,
Vitale D.,
Liguori R.,
Piravandi E.,
Massenet O.,
Quigley F.,
Clabauld G.,
Muendlein A.,
Felber R.,
Schnabl S.,
Hiller R.,
Schmidt W.,
Lecharny A.,
Aubourg S.,
Chefdor F.,
Cooke R.,
Berger C.,
Monfort A.,
Casacuberta E.,
Gibbons T.,
Weber N.,
Vandenbol M.,
Bargues M.,
Terol J.,
Torres A.,
Perez-Perez A.,
Purnelle B.,
Bent E.,
Johnson S.,
Tacon D.,
Jesse T.,
Heijnen L.,
Schwarz S.,
Scholler P.,
Heber S.,
Francs P.,
Bielke C.,
Frishman D.,
Haase D.,
Lemcke K.,
Mewes H.-W.,
Stocker S.,
Zaccaria P.,
Bevan M.,
Wilson R.K.,
de la Bastide M.,
Habermann K.,
Parnell L.,
Dedhia N.,
Gnoj L.,
Schutz K.,
Huang E.,
Spiegel L.,
Sekhon M.,
Murray J.,
Sheet P.,
Cordes M.,
Abu-Threideh J.,
Stoneking T.,
Kalicki J.,
Graves T.,
Harmon G.,
Edwards J.,
Latreille P.,
Courtney L.,
Cloud J.,
Abbott A.,
Scott K.,
Johnson D.,
Minx P.,
Bentley D.,
Fulton B.,
Miller N.,
Greco T.,
Kemp K.,
Kramer J.,
Fulton L.,
Mardis E.,
Dante M.,
Pepin K.,
Hillier L.W.,
Nelson J.,
Spieth J.,
Ryan E.,
Andrews S.,
Geisel C.,
Layman D.,
Du H.,
Ali J.,
Berghoff A.,
Jones K.,
Drone K.,
Cotton M.,
Joshu C.,
Antonoiu B.,
Zidanic M.,
Strong C.,
Sun H.,
Lamar B.,
Yordan C.,
Ma P.,
Zhong J.,
Preston R.,
Vil D.,
Shekher M.,
Matero A.,
Shah R.,
Swaby I.K.,
O'Shaughnessy A.,
Rodriguez M.,
Hoffman J.,
Till S.,
Granat S.,
Shohdy N.,
Hasegawa A.,
Hameed A.,
Lodhi M.,
Johnson A.,
Chen E.,
Marra M.A.,
Martienssen R.,
McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
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[5]
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PHOSPHORYLATION, AND MUTAGENESIS OF LYS-911.
DOI=10.1104/pp.124.2.751; PubMed=11027724 [NCBI, ExPASy, EBI, Israel, Japan]
Oh M.-H.,
Ray W.K.,
Huber S.C.,
Asara J.M.,
Gage D.A.,
Clouse S.D.;
"Recombinant BRASSINOSTEROID INSENSITIVE 1 receptor-like kinase autophosphorylates on serine and threonine residues and phosphorylates a conserved peptide motif in vitro.";
Plant Physiol. 124:751-766(2000).
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[6]
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STEROID-BINDING.
DOI=10.1126/science.288.5475.2360; PubMed=10875920 [NCBI, ExPASy, EBI, Israel, Japan]
He Z.,
Wang Z.-Y.,
Li J.,
Zhu Q.,
Lamb C.,
Ronald P.,
Chory J.;
"Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1.";
Science 288:2360-2363(2000).
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[7]
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SUBCELLULAR LOCATION, STEROID-BINDING, AND AUTOPHOSPHORYLATION.
DOI=10.1038/35066597; PubMed=11268216 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Z.-Y.,
Seto H.,
Fujioka S.,
Yoshida S.,
Chory J.;
"BRI1 is a critical component of a plasma-membrane receptor for plant steroids.";
Nature 410:380-383(2001).
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[8]
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SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BAK1.
DOI=10.1016/S0092-8674(02)00814-0; PubMed=12150928 [NCBI, ExPASy, EBI, Israel, Japan]
Nam K.H.,
Li J.;
"BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.";
Cell 110:203-212(2002).
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[9]
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PHOSPHORYLATION, AND INTERACTION WITH BAK1.
DOI=10.1016/S0092-8674(02)00812-7; PubMed=12150929 [NCBI, ExPASy, EBI, Israel, Japan]
Li J.,
Wen J.,
Lease K.A.,
Doke J.T.,
Tax F.E.,
Walker J.C.;
"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.";
Cell 110:213-222(2002).
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[10]
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SUBCELLULAR LOCATION, AND INTERACTION WITH BAK1.
DOI=10.1105/tpc.104.025387; PubMed=15548744 [NCBI, ExPASy, EBI, Israel, Japan]
Russinova E.,
Borst J.-W.,
Kwaaitaal M.,
Cano-Delgado A.,
Yin Y.,
Chory J.,
de Vries S.C.;
"Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1).";
Plant Cell 16:3216-3229(2004).
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[11]
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INTERACTION WITH TTL.
DOI=10.1105/tpc.104.023903; PubMed=15319482 [NCBI, ExPASy, EBI, Israel, Japan]
Nam K.H.,
Li J.;
"The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1.";
Plant Cell 16:2406-2417(2004).
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[12]
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PHOSPHORYLATION, INTERACTION WITH BAK1, AND MUTAGENESIS OF SER-838; THR-842; THR-846; SER-858; THR-872; THR-1039; SER-1044; THR-1045; THR-1049; SER-1168; SER-1172; 1179-SER-THR-1180 AND SER-1187.
DOI=10.1105/tpc.105.031393; PubMed=15894717 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X.,
Goshe M.B.,
Soderblom E.J.,
Phinney B.S.,
Kuchar J.A.,
Li J.,
Asami T.,
Yoshida S.,
Huber S.C.,
Clouse S.D.;
"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.";
Plant Cell 17:1685-1703(2005).
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