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Blood, 1 July 2002, Vol. 100, No. 1, pp. 276-282
RED CELLS
Band 3 is an anchor protein and a target for SHP-2 tyrosine
phosphatase in human erythrocytes
Luciana Bordin,
Anna Maria Brunati,
Arianna Donella-Deana,
Bruno Baggio,
Antonio Toninello, and
Giulio Clari
From the Dipartimento di Chimica Biologica, and Centro
di Studio delle Biomembrane del Consiglio Nazionale delle Ricerche
(CNR); and the Istituto di Medicina Interna, Divisione di Nefrologia,
University of Padova, Italy.
Tyr phosphorylation of the multifunctional transmembrane
protein band 3 has been implicated in several erythrocyte functions and
disorders. We previously demonstrated that pervanadate treatment of
human erythrocytes induces band-3 Tyr phosphorylation, which is
catalyzed by the sequential action of tyrosine kinase Syk and tyrosine
kinase(s) belonging to the Src family. In this study, we show that Tyr
phosphorylation of band 3, elicited by pervanadate, N-ethylmaleimide,
or diamide, greatly increases band-3 interaction with the tyrosine
phosphatase SHP-2 in parallel with the translocation of SHP-2 to
erythrocyte membranes. These events seem to be mediated by Src-like
catalyzed phosphorylation of band 3 because both SHP-2 translocation to
cellular membranes and its interaction with Tyr-phosphorylated protein
are greatly counteracted by PP2, a specific inhibitor of Src kinases.
Binding-competition experiments demonstrate that SHP-2 recruitment to
band 3 occurs via its SH2 domain(s). In particular, our data support
the view that SHP-2 docks specifically with P-Y359 of band 3. Experiments performed with intact erythrocytes in the presence of the
SHP-2 inhibitor calpeptin suggest that, once recruited to
Tyr-phosphorylated band 3, the tyrosine phosphatase dephosphorylates the protein. P-Y8, 21, and 904 are the residues affected by SHP-2, as
judged by 32P-peptide mapping of band 3 digested with
trypsin. These results indicate that in treated erythrocytes,
recruitment of cytosolic SHP-2 to band 3 is a prerequisite for the
subsequent dephosphorylation of the transmembrane protein.
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