Insights into Tyrosine Phosphorylation Control of Protein−Protein Association from the NMR Structure of a Band 3 Peptide Inhibitor Bound to Glyceraldehyde-3-phosphate Dehydrogenase†,‡

Biochemistry ◽  
1998 ◽  
Vol 37 (3) ◽  
pp. 867-877 ◽  
Author(s):  
Elan Zohar Eisenmesser ◽  
Carol Beth Post
1987 ◽  
Vol 262 (10) ◽  
pp. 4592-4596 ◽  
Author(s):  
P.S. Low ◽  
D.P. Allen ◽  
T.F. Zioncheck ◽  
P. Chari ◽  
B.M. Willardson ◽  
...  

Blood ◽  
2017 ◽  
Vol 130 (8) ◽  
pp. 1031-1040 ◽  
Author(s):  
Antonella Pantaleo ◽  
Kristina R. Kesely ◽  
Maria Carmina Pau ◽  
Ioannis Tsamesidis ◽  
Evelin Schwarzer ◽  
...  

Key PointsInhibitors of human Syk kinase suppress parasite egress. Syk inhibitors prevent the tyrosine phosphorylation of band 3 in P falciparum parasitized red blood cells, reducing the release of microparticles.


Blood ◽  
2011 ◽  
Vol 117 (22) ◽  
pp. 5998-6006 ◽  
Author(s):  
Emanuela Ferru ◽  
Katie Giger ◽  
Antonella Pantaleo ◽  
Estela Campanella ◽  
Jesse Grey ◽  
...  

Abstract The cytoplasmic domain of band 3 serves as a center of erythrocyte membrane organization and constitutes the major substrate of erythrocyte tyrosine kinases. Tyrosine phosphorylation of band 3 is induced by several physiologic stimuli, including malaria parasite invasion, cell shrinkage, normal cell aging, and oxidant stress (thalassemias, sickle cell disease, glucose-6-phosphate dehydrogenase deficiency, etc). In an effort to characterize the biologic sequelae of band 3 tyrosine phosphorylation, we looked for changes in the polypeptide's function that accompany its phosphorylation. We report that tyrosine phosphorylation promotes dissociation of band 3 from the spectrin-actin skeleton as evidenced by: (1) a decrease in ankyrin affinity in direct binding studies, (2) an increase in detergent extractability of band 3 from ghosts, (3) a rise in band 3 cross-linkability by bis-sulfosuccinimidyl-suberate, (4) significant changes in erythrocyte morphology, and (5) elevation of the rate of band 3 diffusion in intact cells. Because release of band 3 from its ankyrin and adducin linkages to the cytoskeleton can facilitate changes in multiple membrane properties, tyrosine phosphorylation of band 3 is argued to enable adaptive changes in erythrocyte biology that permit the cell to respond to the above stresses.


Biochemistry ◽  
1988 ◽  
Vol 27 (19) ◽  
pp. 7447-7452 ◽  
Author(s):  
Akihiko Tsuji ◽  
Kazunori Kawasaki ◽  
Shunichi Ohnishi ◽  
Hellmut Merkle ◽  
Akihiro Kusumi

FEBS Letters ◽  
1999 ◽  
Vol 455 (1-2) ◽  
pp. 87-91 ◽  
Author(s):  
Alexander Barbul ◽  
Yehudit Zipser ◽  
Alexander Nachles ◽  
Rafi Korenstein

2009 ◽  
Vol 484 (2) ◽  
pp. 173-182 ◽  
Author(s):  
Alessio Metere ◽  
Egidio Iorio ◽  
Donatella Pietraforte ◽  
Franca Podo ◽  
Maurizio Minetti

1991 ◽  
Vol 266 (7) ◽  
pp. 4106-4111
Author(s):  
M L Harrison ◽  
P Rathinavelu ◽  
P Arese ◽  
R L Geahlen ◽  
P S Low

Author(s):  
H.T.M.B. Terra ◽  
M.J.A. Saad ◽  
C.R.O. Carvalho ◽  
D.L. Vicentin ◽  
F.F. Costa ◽  
...  

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