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PMID: 1860878 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin.

The Journal of cell biology ·Vol. 114 ·No. 3 ·1991-08-00 ·Pages 413-21

Brewer CB, Roth MG

Abstract

In the polarized kidney cell line MDCK, the influenza virus hemagglutinin (HA) has been well characterized as a model for apically sorted membrane glycoproteins. Previous work from our laboratory has shown that a single amino acid change in the cytoplasmic sequence of HA converts it from a protein that is excluded from coated pits to one that is efficiently internalized. Using trypsin or antibodies to mark protein on the surface, we have shown in MDCK cells that HA containing this mutation is no longer transported to the apical surface but instead is delivered directly to the basolateral plasma membrane. We propose that a cytoplasmic feature similar to an endocytosis signal can cause exclusive basolateral delivery.

MeSH Terms
Animals Antibodies/immunology Biological Transport Cell Line Cytoplasm/chemistry,metabolism Endocytosis Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral/chemistry,metabolism Kinetics Methionine/metabolism Mutation Precipitin Tests Transfection Transferrin/metabolism Trypsin/metabolism Tyrosine/chemistry,immunology
Chemicals
Antibodies Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral Transferrin Tyrosine Methionine Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Brewer C B
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9038.
Roth M G
References (44)
44 references, click to expand
  1. Alteration of the cytoplasmic domain of the membrane-spanning glycoprotein p62 of Semliki Forest virus does not affect its polar distribution in established lines of Madin-Darby canine kidney cells.
    J Cell Biol. 1986 Dec;103(6 Pt 2):2607-18 PMID: 3539942
  2. Development of cell surface polarity in the epithelial Madin-Darby canine kidney (MDCK) cell line.
    EMBO J. 1984 Nov;3(11):2687-94 PMID: 6391916
  3. Characteristics of the tyrosine recognition signal for internalization of transmembrane surface glycoproteins.
    J Cell Biol. 1990 Oct;111(4):1393-407 PMID: 2120240
  4. Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain.
    Cell Regul. 1990 Mar;1(4):369-77 PMID: 2100204
  5. Mutations in the cytoplasmic domain of the 275 kd mannose 6-phosphate receptor differentially alter lysosomal enzyme sorting and endocytosis.
    Cell. 1989 Jun 2;57(5):787-96 PMID: 2541923
  6. Steady-state distribution and biogenesis of endogenous Madin-Darby canine kidney glycoproteins: evidence for intracellular sorting and polarized cell surface delivery.
    J Cell Biol. 1989 Nov;109(5):2117-27 PMID: 2808522
  7. The large external domain is sufficient for the correct sorting of secreted or chimeric influenza virus hemagglutinins in polarized monkey kidney cells.
    J Cell Biol. 1987 Mar;104(3):769-82 PMID: 3546337
  8. Basolateral expression of a chimeric protein in which the transmembrane and cytoplasmic domains of vesicular stomatitis virus G protein have been replaced by those of the influenza virus hemagglutinin.
    J Biol Chem. 1987 Nov 25;262(33):16233-40 PMID: 2824483
  9. Nonpolarized secretion of truncated forms of the influenza hemagglutinin and the vesicular stomatitus virus G protein from MDCK cells.
    Proc Natl Acad Sci U S A. 1987 Jun;84(11):3738-42 PMID: 3035552
  10. Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers.
    J Cell Biol. 1988 Mar;106(3):629-39 PMID: 3279048
  11. A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits.
    Cell. 1988 Jun 3;53(5):743-52 PMID: 2897244
  12. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport.
    Cell. 1986 Sep 12;46(6):939-50 PMID: 3757030
  13. Heterologous transmembrane and cytoplasmic domains direct functional chimeric influenza virus hemagglutinins into the endocytic pathway.
    J Cell Biol. 1986 Apr;102(4):1271-83 PMID: 3007532
  14. Assembly of influenza hemagglutinin trimers and its role in intracellular transport.
    J Cell Biol. 1986 Oct;103(4):1179-91 PMID: 2429970
  15. A sorting signal for the basolateral delivery of the vesicular stomatitis virus (VSV) G protein lies in its luminal domain: analysis of the targeting of VSV G-influenza hemagglutinin chimeras.
    Proc Natl Acad Sci U S A. 1989 Jun;86(11):4112-6 PMID: 2542964
  16. Transferrin receptor polarity and recycling accuracy in "tight" and "leaky" strains of Madin-Darby canine kidney cells.
    J Cell Biol. 1986 Nov;103(5):1767-79 PMID: 2877994
  17. Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport.
    J Cell Biol. 1985 Mar;100(3):704-14 PMID: 3972890
  18. Nonpolarized expression of a secreted murine leukemia virus glycoprotein in polarized epithelial cells.
    Cell. 1986 Dec 26;47(6):1053-9 PMID: 3022940
  19. Polarized expression of a chimeric protein in which the transmembrane and cytoplasmic domains of the influenza virus hemagglutinin have been replaced by those of the vesicular stomatitis virus G protein.
    Proc Natl Acad Sci U S A. 1986 Dec;83(24):9318-22 PMID: 3025835
  20. Sorting and endocytosis of viral glycoproteins in transfected polarized epithelial cells.
    J Cell Biol. 1986 Apr;102(4):1242-55 PMID: 3007530
  21. Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells.
    Proc Natl Acad Sci U S A. 1987 May;84(9):2756-60 PMID: 3033661
  22. Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells.
    J Cell Biol. 1984 Dec;99(6):2131-9 PMID: 6501415
  23. High-frequency transfection of CHO cells using polybrene.
    Somat Cell Mol Genet. 1986 May;12(3):237-44 PMID: 3459255
  24. Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosis.
    Cell. 1986 Nov 7;47(3):359-64 PMID: 3768957
  25. Cell surface polarity in epithelia.
    Annu Rev Cell Biol. 1985;1:243-88 PMID: 3939606
  26. Glycophospholipid membrane anchoring provides clues to the mechanism of protein sorting in polarized epithelial cells.
    Trends Biochem Sci. 1990 Mar;15(3):113-8 PMID: 2139258
  27. Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization.
    J Cell Biol. 1990 Feb;110(2):283-94 PMID: 2298808
  28. Surface distribution of the mannose 6-phosphate receptors in epithelial Madin-Darby canine kidney cells.
    J Biol Chem. 1990 Jul 25;265(21):12629-35 PMID: 1973688
  29. The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin.
    J Biol Chem. 1990 Mar 15;265(8):4760-7 PMID: 2307684
  30. Polarized sorting in epithelia.
    Cell. 1990 Jul 27;62(2):207-10 PMID: 2196994
  31. Polarized expression of functional rat liver asialoglycoprotein receptor in transfected Madin-Darby canine kidney cells.
    J Biol Chem. 1990 Jan 15;265(2):1216-24 PMID: 2404008
  32. Deletions in the cytoplasmic domain of the polymeric immunoglobulin receptor differentially affect endocytotic rate and postendocytotic traffic.
    J Biol Chem. 1990 Aug 15;265(23):13750-7 PMID: 2380185
  33. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation.
    Cell. 1983 Aug;34(1):233-43 PMID: 6883510
  34. Dog kidney cell monolayers can display properties similar to high-resistance epithelia [proceedings].
    J Physiol. 1979 Apr;289:33P-34P PMID: 572421
  35. Polarized monolayers formed by epithelial cells on a permeable and translucent support.
    J Cell Biol. 1978 Jun;77(3):853-80 PMID: 567227
  36. The reaction of ferric salts with transferrin.
    J Biol Chem. 1973 May 10;248(9):3228-32 PMID: 4735577
  37. Transepithelial transport in cell culture.
    Proc Natl Acad Sci U S A. 1976 Apr;73(4):1212-6 PMID: 1063404
  38. The low density lipoprotein receptor. Identification of amino acids in cytoplasmic domain required for rapid endocytosis.
    J Biol Chem. 1987 Mar 25;262(9):4075-82 PMID: 3104336
  39. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells.
    J Cell Biol. 1989 Nov;109(5):2145-56 PMID: 2478564
  40. Expression of macrophage-lymphocyte Fc receptors in Madin-Darby canine kidney cells: polarity and transcytosis differ for isoforms with or without coated pit localization domains.
    J Cell Biol. 1989 Dec;109(6 Pt 2):3291-302 PMID: 2574723
  41. Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells.
    Science. 1989 Sep 29;245(4925):1499-501 PMID: 2571189
  42. Vectorial targeting of apical and basolateral plasma membrane proteins in a human adenocarcinoma epithelial cell line.
    Proc Natl Acad Sci U S A. 1989 Dec;86(23):9313-7 PMID: 2687880
  43. Polarized endocytosis by Madin-Darby canine kidney cells transfected with functional chicken liver glycoprotein receptor.
    J Cell Biol. 1989 Dec;109(6 Pt 1):2809-16 PMID: 2687287
  44. Polymeric immunoglobulin receptor expressed in MDCK cells transcytoses IgA.
    Cell. 1986 Aug 15;46(4):613-21 PMID: 3524859
Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1991-08-00
Pages
413-21
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2289095
Subset
IM
Grants
NIGMS NIH HHS · GM37547 · United States
NIGMS NIH HHS · GM41050 · United States
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