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J. Biol. Chem., Vol. 269, Issue 6, 3928-3933, Feb, 1994
HY Naim and MG Roth
Several proteins, including the hemagglutinin (HA)-Y543 mutant influenza
virus hemagglutinin, are internalized by clathrin-coated pits but do not
have a sequence that fits a recently proposed consensus for internalization
signals containing tyrosine. To determine whether or not the HA-543 signal
is a degenerate form of the internalization signal found in proteins such
as the transferrin receptor and mannose 6- phosphate/insulin-like growth
factor (IGF) II receptor, we have mutated amino acid positions of HA-Y543
shown to be important for internalization of the two receptors. Our results
indicate that the HA- Y543 mutant contains a sub-optimum sequence for a
tyrosine-based internalization signal similar to those found in the
receptors for transferrin, low density lipoprotein, and mannose
6-phosphate/IGFII. However, amino acids with side chains having very
different chemical properties functioned well in positions that are
important for the internalization signal. The variety of amino acid side
chains found in known internalization sequences suggests that atoms of the
polypeptide chain backbone may contribute important interactions for
binding proteins to clathrin coats, with many of the side chains serving
mainly to permit these interactions, a situation similar to that observed
for the binding of peptides by histocompatibility proteins.
Characteristics of the internalization signal in the Y543 influenza virus hemagglutinin suggest a model for recognition of internalization signals containing tyrosine
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9038.
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