TY - JOUR
T1 - A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits
AU - Lazarovits, Janette
AU - Roth, Michael
N1 - Funding Information:
We would like to thank Dr. M.-J. Gething for anti-Japan HA rabbit serums and Dr. R. G. Webster for anti-Guyang 33 monoclonal antibody. We thank Jerry Allen for preparing thin sections alnd Catherina Bird for advice in mutagenesis techniques. This research was supported by grant GM37547 from the National Institutes of Health and grant 86G-091 from the American Heart Association Texas Affiliate to MGR. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC. Section 1734 solely to indicate this fact.
PY - 1988/6/3
Y1 - 1988/6/3
N2 - Through site-specific mutagenesis, three of the ten amino acids of the cytoplasmic domain of the influenza virus hemagglutinin (HA) were individually changed to tyrosines. None of these changes had significant effect on the rate of export, the rate of folding, or the antigenicity of the mutant HAs. However, one of these mutations, substituting tyrosine for cysteine at amino acid 543, changed HA from a protein that was endocytosed at a very low rate to a protein that readily entered coated pits, was internalized, and apparently recycled to the cell surface. Replacement of cysteine 543 with phenylalanine or serine did not increase the rate of internalization of HA. Phosphorylation of the mutant HA bearing a tyrosine at position 543 was not detected. These results indicate a specific and local role for the tyrosine introduced into the cytoplasmic domain of HA that is necessary for interaction of the protein with coated pits.
AB - Through site-specific mutagenesis, three of the ten amino acids of the cytoplasmic domain of the influenza virus hemagglutinin (HA) were individually changed to tyrosines. None of these changes had significant effect on the rate of export, the rate of folding, or the antigenicity of the mutant HAs. However, one of these mutations, substituting tyrosine for cysteine at amino acid 543, changed HA from a protein that was endocytosed at a very low rate to a protein that readily entered coated pits, was internalized, and apparently recycled to the cell surface. Replacement of cysteine 543 with phenylalanine or serine did not increase the rate of internalization of HA. Phosphorylation of the mutant HA bearing a tyrosine at position 543 was not detected. These results indicate a specific and local role for the tyrosine introduced into the cytoplasmic domain of HA that is necessary for interaction of the protein with coated pits.
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U2 - 10.1016/0092-8674(88)90092-X
DO - 10.1016/0092-8674(88)90092-X
M3 - Article
C2 - 2897244
AN - SCOPUS:0024276904
SN - 0092-8674
VL - 53
SP - 743
EP - 752
JO - Cell
JF - Cell
IS - 5
ER -