scholarly journals Multisite Mutagenesis of Interleukin 5 Differentiates Sites for Receptor Recognition and Receptor Activation

Biochemistry ◽  
2001 ◽  
Vol 40 (3) ◽  
pp. 852-852 ◽  
Author(s):  
Carmela G. Plugariu ◽  
Sheng-Jiun Wu ◽  
Wentao Zhang ◽  
Irwin Chaiken
Keyword(s):  
Receptor Activation ◽  
Interleukin 5 ◽  
Receptor Recognition

Multisite Mutagenesis of Interleukin 5 Differentiates Sites for Receptor Recognition and Receptor Activation†

Biochemistry ◽  
2000 ◽  
Vol 39 (48) ◽  
pp. 14939-14949 ◽  
Author(s):  
Carmela G. Plugariu ◽  
Sheng-Jiun Wu ◽  
Wentao Zhang ◽  
Irwin Chaiken
Keyword(s):  
Receptor Activation ◽  
Interleukin 5 ◽  
Receptor Recognition

Coiled coil miniprotein randomization on phage leads to charge pattern mimicry of the receptor recognition determinant of interleukin 5

2002 ◽  
Vol 15 (1) ◽  
pp. 33-43 ◽  
Author(s):  
Chuanzhao Li ◽  
Carmela G. Plugariu ◽  
Joanna Bajgier ◽  
John R. White ◽  
Kristin M. Liefer ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Interleukin 5 ◽  
Receptor Recognition ◽  
Recognition Determinant

scholarly journals Epitope Randomization Redefines the Functional Role of Glutamic Acid 110 in Interleukin-5 Receptor Activation

2000 ◽  
Vol 275 (10) ◽  
pp. 7351-7358 ◽  
Author(s):  
Sheng-Jiun Wu ◽  
Rabindra Tambyraja ◽  
Wentao Zhang ◽  
Stefan Zahn ◽  
A. Paul Godillot ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Functional Role ◽  
Receptor Activation ◽  
Interleukin 5

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 ◽  
...  
Keyword(s):  
Receptor Activation ◽  
Interleukin 5 ◽  
Charged Residues

scholarly journals Contributions of Intracellular Loops 2 and 3 of the Lutropin Receptor in Gs Coupling

2008 ◽  
Vol 22 (1) ◽  
pp. 126-138 ◽  
Author(s):  
Krassimira Angelova ◽  
Francesca Fanelli ◽  
David Puett
Keyword(s):  
G Protein ◽  
Hot Spots ◽  
Computational Models ◽  
Structural Changes ◽  
Protein Complexes ◽  
Receptor Activation ◽  
Receptor Sites ◽  
Receptor Recognition ◽  
Intracellular Loops

Abstract A number of amino acids essential for Gs coupling, i.e. hot spots, were identified after in vitro Ala-scanning mutagenesis of the cytosolic extensions of helices 3, 5, and 6 and of intracellular loops 2 and 3 (IL2 and IL3) of the human LH receptor (LHR). Consistent with the results of in vitro experiments involving ligand binding and ligand-mediated signaling in transiently transfected human embryonic kidney 293 cells, computational modeling of the isolated receptor and of the receptor-G protein complexes suggests an important role of the cytosolic extension of helix 3 and the N-terminal portion of the IL2 in Gsα interaction, whereas the contribution of IL3 is marginal. Mapping the hot spots into the computational models of LHR and the LHR-Gs complexes allowed for a distinction between receptor sites required for intramolecular structural changes (i.e. I460, T461, H466, and I549) and receptor sites more likely involved in G protein recognition (i.e. R464, T467, I468, Y470, Y550, and D564). The latter sites include the highly conserved arginine of the (E/D)R(Y/W) motif, which is therefore likely to be a receptor recognition point for Gs rather than a switch of receptor activation. The results of in vitro and in silico experiments carried out in this study represent the first comprehensive delineation of functionality of the individual residues in the intracellular domains of LHR and establish potential switches of receptor activation as well as a map of the primary receptor recognition sites for Gs. A novel way to consider constitutively active mutants was inferred from this study, i.e. receptor states with improved complementarity for the G protein compared to the wild-type receptor.

scholarly journals Alternative modes of GM-CSF receptor activation revealed using activated mutants of the common β-subunit

Blood ◽  
2010 ◽  
Vol 115 (16) ◽  
pp. 3346-3353 ◽  
Author(s):  
Michelle Perugini ◽  
Anna L. Brown ◽  
Diana G. Salerno ◽  
Grant W. Booker ◽  
Cvetan Stojkoski ◽  
...  
Keyword(s):  
Direct Interaction ◽  
Receptor Activation ◽  
Janus Kinase ◽  
Receptor Complex ◽  
Α Subunit ◽  
Interleukin 5 ◽  
Downstream Signaling ◽  
Gm Csf ◽  
Phosphoinositide 3 Kinase ◽  
High Level

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.

Interleukin-4, interferon-gamma and interleukin-5 in peripheral blood of children with moderate atopic asthma

1997 ◽  
Vol 27 (11) ◽  
pp. 1254-1260 ◽  
Author(s):  
M. O. HOEKSTRA ◽  
Y. HOEKSTRA ◽  
D. DE REUS ◽  
B. RUTGERS ◽  
J. GERRITSEN ◽  
...  
Keyword(s):  
Interferon Gamma ◽  
Peripheral Blood ◽  
Atopic Asthma ◽  
Interleukin 4 ◽  
Interleukin 5
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