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Tissue-specific alternative splicing of protein 4.1 inserts an exon
necessary for formation of the ternary complex with erythrocyte spectrin
and F-actin
WC Horne, SC Huang, PS Becker, TK Tang and EJ Benz
Department of Pathology, Yale University School of Medicine, New Haven, CT.
Erythrocyte protein 4.1 is an 78- to 80-Kd peripheral membrane protein that
promotes the interaction of spectrin with actin protofilaments and links
the resulting interlocking network to the integral membrane proteins. There
are several isoforms of protein 4.1 that appear to be expressed in a
restricted group of tissues. These arise from alternative mRNA splicing
events that lead to the combinational insertion or deletion of at least 10
blocks of nucleotides (motifs) within the mature mRNA. One of these, motif
I, consists of 63 nucleotides encoding 21 amino acids in the N-terminal
region of the putative spectrin/actin-binding domain. The expression of the
motif U- containing isoform occurs late in erythroid maturation. We
generated recombinant isoforms of protein 4.1 and of the putative 10-Kd
spectrin/actin-binding fragment that contain or lack this 21 amino acid
sequence and examined their ability to form a ternary complex with
erythrocyte spectrin and F-actin. The isoforms of the complete protein and
of the 10-Kd fragment that contain the sequence encoded by motif I
efficiently form the ternary complex. Isoforms that lack this sequence, but
are otherwise identical, do not participate in the formation of the ternary
complex. These results, in conjunction with the expression of motif I
during late erythroid maturation, suggest that interaction with actin and
the erythroid form of spectrin is a specialized property of the erythrocyte
form of protein 4.1. Alternative mRNA splicing in developing red blood
cells thus plays a key adaptive role in the formation of the highly
specialized erythrocyte membrane.
Volume 82,
Issue 8,
pp. 2558-2563,
10/15/1993
Copyright © 1993 by The American Society of Hematology
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