Conformational change of band 3 protein induced by diethyl pyrocarbonate modification in human erythrocyte ghosts

Biochemistry ◽  
1989 ◽  
Vol 28 (11) ◽  
pp. 4725-4728 ◽  
Author(s):  
Kenji Izuhara ◽  
Kenshi Okubo ◽  
Naotaka Hamasaki
Keyword(s):  
Conformational Change ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Erythrocyte Ghosts ◽  
Band 3 Protein ◽  
Diethyl Pyrocarbonate

scholarly journals Phosphotyrosine phosphatase associated with band 3 protein in the human erythrocyte membrane

1996 ◽  
Vol 314 (3) ◽  
pp. 881-887 ◽  
Author(s):  
Yehudit ZIPSER ◽  
Nechama S. KOSOWER
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Intact Cell ◽  
Band 3 ◽  
Band 3 Protein ◽  
Human Erythrocyte Membrane ◽  
Major Fraction ◽  
Phosphotyrosine Phosphatase ◽  
A Minor ◽  
Triton X

The anion-exchange band 3 protein is the main erythrocyte protein that is phosphorylated by tyrosine kinase. To study the regulation of band 3 phosphorylation, we examined phosphotyrosine phosphatase (PTP) activity in the human erythrocyte. We show that the human erythrocyte membrane contains a band 3-associated neutral PTP which is activated by Mg2+ and inhibited by Mn2+ and vanadate. The PTP is active in the intact cell and in the isolated membrane. A major fraction of the PTP is tightly bound to the membrane and can be extracted from it by Triton X-100; a minor part is associated with the Triton X-100-insoluble cytoskeleton. The behaviour of the PTP parallels that of band 3, the major fraction of which is extractable by detergents with a minor fraction being anchored to the cytoskeleton. Moreover, band 3 is co-precipitated when the PTP is immunoprecipitated from solubilized membranes, and PTP is co-precipitated when band 3 is immunoprecipitated. The PTP appears to be related to PTP1B (identified using an antibody to an epitope in its catalytic domain and by molecular mass). The system described here has a unique advantage for PTP research, since it allows the study of the interaction of a PTP with an endogenous physiological substrate that is present in substantial amounts in the cell membrane. The membrane-bound, band 3-associated, PTP may play a role in band 3 function in the erythrocyte and in other cells which have proteins analogous to band 3.

scholarly journals Cytoskeleton-membrane connections in the human erythrocyte membrane: band 4.1 binds to tetrameric band 3 protein

1997 ◽  
Vol 1325 (2) ◽  
pp. 226-234 ◽  
Author(s):  
Bogdan von Rückmann ◽  
Thomas Jöns ◽  
Frank Dölle ◽  
Detlev Drenckhahn ◽  
Dieter Schubert
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Band 3 Protein ◽  
Human Erythrocyte Membrane

Protoporphyrin-induced photodynamic effects on band 3 protein of human erythrocyte membranes

1981 ◽  
Vol 649 (2) ◽  
pp. 310-316 ◽  
Author(s):  
T.M.A.R. Dubbelman ◽  
A.F.P.M. De Goeij ◽  
K. Christianse ◽  
J. Van Steveninck
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
Human Erythrocyte Membranes

Further Studies on Zn2+-Mediated Domain–Domain Communication in Human Erythrocyte Band 3

1998 ◽  
Vol 18 (5) ◽  
pp. 265-277
Author(s):  
Hong Xu ◽  
Xujia Zhang ◽  
Fu Yu Yang
Keyword(s):  
Conformational Change ◽  
Human Erythrocyte ◽  
Cytoplasmic Domain ◽  
Band 3 ◽  
Anion Transport ◽  
Intrinsic Fluorescence ◽  
Transport Activity ◽  
Membrane Domain ◽  
Nmr Study ◽  
Anion Transport Activity

Human erythrocyte band 3 is purified and reconstituted into vesicles, forming right-side-out proteoliposomes. Zn2+ entrapped inside the proteoliposomes inhibits the anion transport activity of band 3, and removal of the cytoplasmic domain of band 3 is able to diminish Zn2+ inhibition. Thus, the inhibition of activity of band 3 results from the Zn2+ induced conformational change of the cytoplasmic domain, which in turn is transmitted to the membrane domain. The results of intrinsic fluorescence and its quenching by HB and the 35Cl NMR study indicate that the cytoplasmic domain is essential for the conformational change induced by Zn2+.SH-blocking reagents, CH3I and GSSG, are used to modify the cytoplasmic domain, where they specifically bind to Cys201 and Cys317. It is observed that the Zn2+ induced inhibition of anion transport activity is blocked. This demonstrates that Cys201 and Cys317 are required in Zn2+-mediated domain–domain communication.

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