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Blood, 15 August 2000, Vol. 96, No. 4, pp. 1550-1557
RED CELLS
Sequential phosphorylation of protein band 3 by Syk and Lyn
tyrosine kinases in intact human erythrocytes: identification of
primary and secondary phosphorylation sites
Anna Maria Brunati,
Luciana Bordin,
Giulio Clari,
Peter James,
Manfredo Quadroni,
Elisabetta Baritono,
Lorenzo A. Pinna, and
Arianna Donella-Deana
From the Dipartimento di Chimica Biologica and Centro
di Studio delle Biomembrane del C.N.R., University of Padova, Padova,
Italy; and Protein Chemistry Laboratory, ETH Zurich,
Zurich, Switzerland.
Treatment of intact human erythrocytes with pervanadate induces Tyr
(Y)-phosphorylation of the transmembrane protein band 3; in parallel,
the activity of the immunoprecipitated tyrosine kinases Syk and Lyn is
increased. When erythrocytes are incubated with pervanadate together
with PP1, a specific inhibitor of Src kinases, including Lyn, the
Y-phosphorylation of band 3 is only partially reduced. Indeed, the
PP1-resistant phosphorylation of band 3 precedes and is a prerequisite
for its coimmunoprecipitation with Lyn, which interacts with the
phosphoprotein via the SH2 domain of the enzyme, as proven by binding
competition experiments. Upon recruitment to primarily phosphorylated
band 3, Lyn catalyzes the secondary phosphorylation of the
transmembrane protein. These data are consistent with the view that
band 3 is phosphorylated in intact erythrocytes by both PP1-resistant
(most likely Syk) and PP1-inhibited (most likely Lyn) tyrosine kinases
according to a sequential phosphorylation process. Similar radiolabeled peptide maps are obtained by tryptic digestion of
32P-band 3 isolated from either pervanadate-treated
erythrocytes or red cell membranes incubated with exogenous Syk
and Lyn. It has also been demonstrated by means of mass
spectrometry that the primary phosphorylation of band 3 occurs at Y8
and Y21, while the secondary phosphorylation affects Y359 and Y904.
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