Negative Regulation of the Ethylene Response by Differential Cooperations of the Ethylene Receptor Family Members and the Raf-Like Protein CTR1

2013 ◽  
Vol 43 (12) ◽  
pp. 1054-1064
Author(s):  
Fang XIE ◽  
Qian LIU ◽  
ChiKuang WEN ◽  
LiPing QIU
Keyword(s):  
Family Members ◽  
Negative Regulation ◽  
Ethylene Receptor ◽  
Ethylene Response ◽  
Receptor Family

Ethylene-binding activity, gene expression levels, and receptor system output for ethylene receptor family members from Arabidopsis and tomato†

2005 ◽  
Vol 41 (5) ◽  
pp. 651-659 ◽  
Author(s):  
Ronan C. O'Malley ◽  
Fernando I. Rodriguez ◽  
Jeffrey J. Esch ◽  
Brad M. Binder ◽  
Philip O'Donnell ◽  
...  
Keyword(s):  
Gene Expression ◽  
Family Members ◽  
Binding Activity ◽  
Ethylene Receptor ◽  
Receptor System ◽  
Expression Levels ◽  
Ethylene Binding ◽  
System Output ◽  
Receptor Family ◽  
Gene Expression Levels

scholarly journals Subcellular Localization and In Vivo Interactions of the Arabidopsis thaliana Ethylene Receptor Family Members

2008 ◽  
Vol 1 (2) ◽  
pp. 308-320 ◽  
Author(s):  
Christopher Grefen ◽  
Katrin Städele ◽  
Kamil Růžička ◽  
Petr Obrdlik ◽  
Klaus Harter ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Subcellular Localization ◽  
Family Members ◽  
Ethylene Receptor ◽  
Receptor Family

Identification of Toll-like receptor family members in Oncomelania hupensis and their role in defense against Schistosoma japonicum

Acta Tropica ◽  
2018 ◽  
Vol 181 ◽  
pp. 69-78 ◽  
Author(s):  
Qin Ping Zhao ◽  
Qian Gao ◽  
Yan Zhang ◽  
Yan Wei Li ◽  
Wen Ling Huang ◽  
...  
Keyword(s):  
Schistosoma Japonicum ◽  
Family Members ◽  
Toll Like Receptor ◽  
Oncomelania Hupensis ◽  
Receptor Family

Characterization of Teleost Insulin Receptor Family Members

1999 ◽  
Vol 115 (2) ◽  
pp. 270-281 ◽  
Author(s):  
Michael W. Greene ◽  
Thomas T. Chen
Keyword(s):  
Insulin Receptor ◽  
Family Members ◽  
Receptor Family

scholarly journals Binding of SH2-B Family Members within a Potential Negative Regulatory Region Maintains JAK2 in an Active State

2006 ◽  
Vol 26 (17) ◽  
pp. 6381-6394 ◽  
Author(s):  
Jason H. Kurzer ◽  
Pipsa Saharinen ◽  
Olli Silvennoinen ◽  
Christin Carter-Su
Keyword(s):  
Amino Acids ◽  
Regulatory Region ◽  
Family Members ◽  
Sh2 Domain ◽  
Janus Kinase ◽  
Adapter Proteins ◽  
Active Conformation ◽  
Jak2 Inhibitor ◽  
Direct Competition ◽  
Receptor Family

ABSTRACT The tyrosine kinase Janus kinase 2 (JAK2) transduces signaling for the majority of known cytokine receptor family members and is constitutively activated in some cancers. Here we examine the mechanisms by which the adapter proteins SH2-Bβ and APS regulate the activity of JAK2. We show that like SH2-Bβ, APS binds JAK2 at multiple sites and that binding to phosphotyrosine 813 is essential for APS to increase active JAK2 and to be phosphorylated by JAK2. Binding of APS to a phosphotyrosine 813-independent site inhibits JAK2. Both APS and SH2-Bβ increase JAK2 activity independent of their N-terminal dimerization domains. SH2-Bβ-induced increases in JAK2 dimerization require only the SH2 domain and only one SH2-Bβ to be bound to a JAK2 dimer. JAK2 mutations and truncations revealed that amino acids 809 to 811 in JAK2 are a critical component of a larger regulatory region within JAK2, most likely including amino acids within the JAK homology 1 (JH1) and JH2 domains and possibly the FERM domain. Together, our data suggest that SH2-Bβ and APS do not activate JAK2 as a consequence of their own dimerization, recruitment of an activator of JAK2, or direct competition with a JAK2 inhibitor for binding to JAK2. Rather, they most likely induce or stabilize an active conformation of JAK2.

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