PMID: 3771631Oct 1, 1986Paper

Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza hemagglutinin

The Journal of Cell Biology
C DoyleM J Gething

Abstract

Site-directed oligonucleotide mutagenesis has been used to introduce chain termination codons into the cloned DNA sequences encoding the carboxy-terminal transmembrane (27 amino acids) and cytoplasmic (10 amino acids) domains of influenza virus hemagglutinin (HA). Four mutant genes were constructed which express truncated forms of HA that lack the cytoplasmic domain and terminate at amino acids 9, 14, 17, or 27 of the wild-type hydrophobic domain. Analysis of the biosynthesis and intracellular transport of these mutants shows that the cytoplasmic tail is not needed for the efficient transport of HA to the cell surface; the stop-transfer sequences are located in the hydrophobic domain; 17 hydrophobic amino acids are sufficient to anchor HA stably in the membrane; and mutant proteins with truncated hydrophobic domains show drastic alterations in transport, membrane association, and stability.

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Citations

Aug 1, 1991·Current Opinion in Cell Biology·J S Bonifacino, J Lippincott-Schwartz
Jan 10, 1995·Virology·J J MeulenbergG Wensvoort
Oct 1, 1986·The Journal of Cell Biology·C S CopelandA Helenius
Nov 1, 1988·The Journal of Cell Biology·M S Poruchynsky, P H Atkinson
Jun 1, 1989·The Journal of Cell Biology·S M HurtleyC S Copeland
Aug 1, 1989·The Journal of Cell Biology·E V ProchownikV M Dixit
Aug 1, 1991·The Journal of Cell Biology·I BraakmanA Helenius
Dec 1, 1991·The Journal of Cell Biology·F J Stafford, J S Bonifacino
Jul 1, 1992·The Journal of Cell Biology·M S SegalM J Gething
Jun 1, 1989·Immunological Reviews·C DoyleJ L Strominger
Jun 11, 2002·The Journal of Biological Chemistry·Ralf JacobHassan Y Naim
Jun 5, 1998·The Journal of Biological Chemistry·P PanzerH Y Naim
Jun 6, 2018·Archives of Virology·Khrisdiana PutriAmir H Noormohammadi

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