The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

BRI1  -  protein brassinosteroid insensitive 1

Arabidopsis thaliana

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of BRI1

  • Removal of BRI1's C terminus leads to a hypersensitive receptor, indicated by suppression of dwarfism of BR-deficient and BR-perception mutants and by enhanced BR signaling as a result of elevated phosphorylation of BRI1 [1].
  • The bri1 mutant showed multiple deficiencies in developmental pathways that could not be rescued by brassinosteroid treatment including a severely dwarfed stature; dark green, thickened leaves; males sterility; reduced apical dominance; and de-etiolation of dark-grown seedlings [2].

High impact information on BRI1


Biological context of BRI1

  • The SERK1 mutant allele serk1-1 enhances the phenotype of the weak BRI1 allele bri1-119 [4].
  • These findings support a role for TRIP-1 in the molecular mechanisms of BR-regulated plant growth and development, possibly as a cytoplasmic substrate of the BRI1 receptor kinase [5].
  • Coexpression of BRI1 and AtSERK3 results in a change of the steady state distribution of both receptors because of accelerated endocytosis [6].
  • In Arabidopsis thaliana brassinosteroid (BR), perception is mediated by two Leu-rich repeat receptor-like kinases, BRASSINOSTEROID INSENSITIVE1 (BRI1) and BRI1-ASSOCIATED RECEPTOR KINASE1 (BAK1) (Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-like KINASE3 [AtSERK3]) [6].
  • The extracellular leucine-rich repeat (LRR) and transmembrane domains of the Arabidopsis receptor kinase BRI1, which is implicated in brassinosteroid signaling, were fused to the serine/threonine kinase domain of XA21, the rice disease resistance receptor [7].

Anatomical context of BRI1


Associations of BRI1 with chemical compounds


Physical interactions of BRI1

  • TTL interacts with BRI1 in a kinase-dependent manner in yeast and is phosphorylated by BRI1 in vitro [8].
  • Three clones, Y-1, 2 and 3, were found to interact commonly with the kinase domain of RLK902 and RKL1 and not to interact with the kinase domain of BRI1, a member of LRR-RLKs [13].

Enzymatic interactions of BRI1


Regulatory relationships of BRI1

  • It is believed that BRI1 becomes activated through heterodimerization with BAK1, a similar LRR receptor kinase, in response to BR signal [8].
  • Moreover, a weak response in the mutant suggests that DWF4 alone is likely to be regulated in other way(s) in addition to BRI1 mediation [14].

Other interactions of BRI1

  • Using blue native gel electrophoresis, we show that SERK1 and SERK3 are part of BRI1-containing multiple protein complexes with relative masses between 300 and 500 kD [4].
  • The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1 [8].
  • Based on sequence similarity, we have identified three members of the BRI1 family, named BRL1, BRL2 and BRL3 [15].
  • However, their response to fluctuation of BR levels was highly reduced (DWF4) or nullified (the other eight genes) in a bri1 mutant [14].
  • It was proposed that BR signals, perceived by a membrane BR receptor complex that contains the leucine (Leu)-rich repeat receptor-like kinase BRI1, inactivate BIN2 to relieve its inhibitory effect on unknown downstream BR-signaling components [16].

Analytical, diagnostic and therapeutic context of BRI1


  1. Autoregulation and homodimerization are involved in the activation of the plant steroid receptor BRI1. Wang, X., Li, X., Meisenhelder, J., Hunter, T., Yoshida, S., Asami, T., Chory, J. Dev. Cell (2005) [Pubmed]
  2. A brassinosteroid-insensitive mutant in Arabidopsis thaliana exhibits multiple defects in growth and development. Clouse, S.D., Langford, M., McMorris, T.C. Plant Physiol. (1996) [Pubmed]
  3. BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling. Nam, K.H., Li, J. Cell (2002) [Pubmed]
  4. The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein complex includes BRASSINOSTEROID-INSENSITIVE1. Karlova, R., Boeren, S., Russinova, E., Aker, J., Vervoort, J., de Vries, S. Plant Cell (2006) [Pubmed]
  5. Interaction of Arabidopsis BRASSINOSTEROID-INSENSITIVE 1 receptor kinase with a homolog of mammalian TGF-beta receptor interacting protein. Ehsan, H., Ray, W.K., Phinney, B., Wang, X., Huber, S.C., Clouse, S.D. Plant J. (2005) [Pubmed]
  6. Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1). Russinova, E., Borst, J.W., Kwaaitaal, M., Caño-Delgado, A., Yin, Y., Chory, J., de Vries, S.C. Plant Cell (2004) [Pubmed]
  7. Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1. He, Z., Wang, Z.Y., Li, J., Zhu, Q., Lamb, C., Ronald, P., Chory, J. Science (2000) [Pubmed]
  8. The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1. Nam, K.H., Li, J. Plant Cell (2004) [Pubmed]
  9. BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling. Li, J., Wen, J., Lease, K.A., Doke, J.T., Tax, F.E., Walker, J.C. Cell (2002) [Pubmed]
  10. BRL1, a leucine-rich repeat receptor-like protein kinase, is functionally redundant with BRI1 in regulating Arabidopsis brassinosteroid signaling. Zhou, A., Wang, H., Walker, J.C., Li, J. Plant J. (2004) [Pubmed]
  11. Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. 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. Plant Cell (2005) [Pubmed]
  12. Transcriptional and posttranscriptional regulation of Arabidopsis TCH4 expression by diverse stimuli. Roles of cis regions and brassinosteroids. Iliev, E.A., Xu, W., Polisensky, D.H., Oh, M.H., Torisky, R.S., Clouse, S.D., Braam, J. Plant Physiol. (2002) [Pubmed]
  13. Identification of three clones which commonly interact with the kinase domains of highly homologous two receptor-like kinases, RLK902 and RKL1. Tarutani, Y., Sasaki, A., Yasuda, M., Nakashita, H., Yoshida, S., Yamaguchi, I., Suzuki, Y. Biosci. Biotechnol. Biochem. (2004) [Pubmed]
  14. Brassinosteroid homeostasis in Arabidopsis is ensured by feedback expressions of multiple genes involved in its metabolism. Tanaka, K., Asami, T., Yoshida, S., Nakamura, Y., Matsuo, T., Okamoto, S. Plant Physiol. (2005) [Pubmed]
  15. BRL1 and BRL3 are novel brassinosteroid receptors that function in vascular differentiation in Arabidopsis. Caño-Delgado, A., Yin, Y., Yu, C., Vafeados, D., Mora-García, S., Cheng, J.C., Nam, K.H., Li, J., Chory, J. Development (2004) [Pubmed]
  16. Two putative BIN2 substrates are nuclear components of brassinosteroid signaling. Zhao, J., Peng, P., Schmitz, R.J., Decker, A.D., Tax, F.E., Li, J. Plant Physiol. (2002) [Pubmed]
  17. Recombinant brassinosteroid insensitive 1 receptor-like kinase autophosphorylates on serine and threonine residues and phosphorylates a conserved peptide motif in vitro. Oh, M.H., Ray, W.K., Huber, S.C., Asara, J.M., Gage, D.A., Clouse, S.D. Plant Physiol. (2000) [Pubmed]
  18. Brassinosteroid-insensitive-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase. Friedrichsen, D.M., Joazeiro, C.A., Li, J., Hunter, T., Chory, J. Plant Physiol. (2000) [Pubmed]
WikiGenes - Universities