scholarly journals Asymmetric Usage of Antagonist Charged Residues Drives Interleukin-5 Receptor Recruitment but Is Insufficient for Receptor Activation†

Biochemistry ◽  
2006 ◽  
Vol 45 (4) ◽  
pp. 1106-1115 ◽  
Author(s):  
Tetsuya Ishino ◽  
Udaya Pillalamarri ◽  
Dominick Panarello ◽  
Madhushree Bhattacharya ◽  
Cecilia Urbina ◽  
...  
1995 ◽  
Vol 270 (26) ◽  
pp. 15762-15769 ◽  
Author(s):  
Pierre Graber ◽  
Amanda E. I. Proudfoot ◽  
Franois Talabot ◽  
Alain Bernard ◽  
Murray McKinnon ◽  
...  

2000 ◽  
Vol 275 (10) ◽  
pp. 7351-7358 ◽  
Author(s):  
Sheng-Jiun Wu ◽  
Rabindra Tambyraja ◽  
Wentao Zhang ◽  
Stefan Zahn ◽  
A. Paul Godillot ◽  
...  

Biochemistry ◽  
2001 ◽  
Vol 40 (3) ◽  
pp. 852-852 ◽  
Author(s):  
Carmela G. Plugariu ◽  
Sheng-Jiun Wu ◽  
Wentao Zhang ◽  
Irwin Chaiken

Biochemistry ◽  
2000 ◽  
Vol 39 (48) ◽  
pp. 14939-14949 ◽  
Author(s):  
Carmela G. Plugariu ◽  
Sheng-Jiun Wu ◽  
Wentao Zhang ◽  
Irwin Chaiken

Blood ◽  
2010 ◽  
Vol 115 (16) ◽  
pp. 3346-3353 ◽  
Author(s):  
Michelle Perugini ◽  
Anna L. Brown ◽  
Diana G. Salerno ◽  
Grant W. Booker ◽  
Cvetan Stojkoski ◽  
...  

Abstract Granulocyte/macrophage colony-stimulating factor promotes growth, survival, differentiation, and activation of normal myeloid cells and plays an important role in myeloid leukemias. The GM-CSF receptor (GMR) shares a signaling subunit, βc, with interleukin-3 and interleukin-5 receptors and has recently been shown to induce activation of Janus kinase 2 (JAK2) and downstream signaling via formation of a unique dodecameric receptor complex. In this study we use 2 activated βc mutants that display distinct signaling capacity and have differential requirements for the GMR α-subunit (GMR-α) to dissect the signaling pathways associated with the GM-CSF response. The V449E transmembrane mutant selectively activates JAK2/signal transducer and activator of transcription 5 and extracellular signal-regulated kinase (ERK) pathways, resulting in a high level of sensitivity to JAK and ERK inhibitors, whereas the extracellular mutant (FIΔ) selectively activates the phosphoinositide 3-kinase/Akt and IκKβ/nuclear factorκB pathways. We also demonstrate a novel and direct interaction between the SH3 domains of Lyn and Src with a conserved proline-rich motif in GMR-α and show a selective requirement for Src family kinases by the FIΔ mutant. We relate the nonoverlapping nature of signaling by the activated mutants to the structure of the unique GMR complex and propose alternative modes of receptor activation acting synergistically in the mature liganded receptor complex.


1997 ◽  
Vol 27 (11) ◽  
pp. 1254-1260 ◽  
Author(s):  
M. O. HOEKSTRA ◽  
Y. HOEKSTRA ◽  
D. DE REUS ◽  
B. RUTGERS ◽  
J. GERRITSEN ◽  
...  

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