Abstract
HLA-A and -B antigens are phosphorylated in transformed lymphoblastoid cells and peripheral blood lymphocytes, both incubated with 32Pi. The phosphate group is attached to HLA-A and -B heavy chain (p44) as identified by immunoprecipitation with anti-beta2-microglobulin IgG, sodium dodecyl sulfate/polyacrylamide gel electrophoresis, isoelectric focusing, and susceptibility to limited proteolysis by papain and trypsin. The site(s) of phosphorylation is identified as a serine residue(s) located in the hydrophilic carboxy terminus of the p44 chain. HLA antigens are also phosphorylated in isolated membranes from transformed lymphoblastoid cells that are incubated with [gamma32P]ATP. The phosphorylation of the carboxy terminus of HLA-A and -B antigens in vivo is good evidence that this portion of the molecule is intracellular. Furthermore, this modification suggests a general way in which interactions between membrane proteins and cytoskeletal elements may be regulated.
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Selected References
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- Ash J. F., Louvard D., Singer S. J. Antibody-induced linkages of plasma membrane proteins to intracellular actomyosin-containing filaments in cultured fibroblasts. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5584–5588. doi: 10.1073/pnas.74.12.5584. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bourguignon L. Y., Singer S. J. Transmembrane interactions and the mechanism of capping of surface receptors by their specific ligands. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5031–5035. doi: 10.1073/pnas.74.11.5031. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bárány K., Bárány M. Phosphorylation of the 18,000-dalton light chain of myosin during a single tetanus of frog muscle. J Biol Chem. 1977 Jul 25;252(14):4752–4754. [PubMed] [Google Scholar]
- Cotmore S. F., Furthmayr H., Marchesi V. T. Immunochemical evidence for the transmembrane orientation of glycophorin A. Localization of ferritin-antibody conjugates in intact cells. J Mol Biol. 1977 Jul 5;113(3):539–553. doi: 10.1016/0022-2836(77)90237-6. [DOI] [PubMed] [Google Scholar]
- Cresswell P., Turner M. J., Strominger J. L. Papain-solubilized HL-A antigens from cultured human lymphocytes contain two peptide fragments. Proc Natl Acad Sci U S A. 1973 May;70(5):1603–1607. doi: 10.1073/pnas.70.5.1603. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Edelman G. M. Surface modulation in cell recognition and cell growth. Science. 1976 Apr 16;192(4236):218–226. doi: 10.1126/science.769162. [DOI] [PubMed] [Google Scholar]
- Engelhard V. H., Guild B. C., Helenius A., Terhorst C., Strominger J. L. Reconstitution of purified detergent-soluble HLA-A and HLA-B antigens into phospholipid vesicles. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3230–3234. doi: 10.1073/pnas.75.7.3230. [DOI] [PMC free article] [PubMed] [Google Scholar]
- England P. J., Stull J. T., Krebs E. G. Dephosphorylation of the inhibitor component of troponin by phosphorylase phosphatase. J Biol Chem. 1972 Aug 25;247(16):5275–5277. [PubMed] [Google Scholar]
- Guthrow C. E., Jr, Allen J. E., Rasmussen H. Phosphorylation of an endogenous membrane protein by an endogenous, membrane-associated cyclic adenosine 3',5'-monophosphate-dependent protein kinase in human erythrocyte ghosts. J Biol Chem. 1972 Dec 25;247(24):8145–8153. [PubMed] [Google Scholar]
- Kemp B. E., Graves D. J., Benjamini E., Krebs E. G. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase. J Biol Chem. 1977 Jul 25;252(14):4888–4894. [PubMed] [Google Scholar]
- Koch G. L., Smith M. J. An association between actin and the major histocompatibility antigen H-2. Nature. 1978 May 25;273(5660):274–278. doi: 10.1038/273274a0. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lemonnier F., Mescher T. M., sherman L., Burakoff S. The induction of cytolytic T lymphocytes with purified plasma membranes. J Immunol. 1978 Apr;120(4):1114–1120. [PubMed] [Google Scholar]
- McCune J. M., Humphreys R. E., Yocum R. R., Strominger J. L. Enhanced representation of HL-A antigens on human lymphocytes after mitogenesis induced by phytohemagglutinin or Epstein-Barr virus. Proc Natl Acad Sci U S A. 1975 Aug;72(8):3206–3209. doi: 10.1073/pnas.72.8.3206. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicolson G. L. Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over surface components. Biochim Biophys Acta. 1976 Apr 13;457(1):57–108. doi: 10.1016/0304-4157(76)90014-9. [DOI] [PubMed] [Google Scholar]
- Parham P., Humphreys R. E., Turner M. J., Strominger J. L. Heterogeneity of HL-A antigen preparations is due to variable sialic acid content. Proc Natl Acad Sci U S A. 1974 Oct;71(10):3998–4001. doi: 10.1073/pnas.71.10.3998. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Perrie W. T., Smillie L. B., Perry S. V. A phosphorylated light-chain component of myosin. Biochem J. 1972 Jul;128(3):105P–106P. doi: 10.1042/bj1280105p. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ribolow H., BARANY M. Phosphorylation of tropomyosin in live frog muscle. Arch Biochem Biophys. 1977 Mar;179(2):718–720. doi: 10.1016/0003-9861(77)90162-x. [DOI] [PubMed] [Google Scholar]
- Robb R. J., Strominger J. L. Rapid purification of detergent-solubilized HLA antigen by affinity chromatography employing anti-beta2-microglobulin serum. J Biol Chem. 1976 Sep 10;251(17):5427–5428. [PubMed] [Google Scholar]
- Robb R. J., Terhorst C., Strominger J. L. Sequence of the COOH-terminal hydrophilic region of histocompatibility antigens HLA-A2 and HLA-B7. J Biol Chem. 1978 Aug 10;253(15):5319–5324. [PubMed] [Google Scholar]
- Rubin C. S., Rosen O. M. Protein phosphorylation. Annu Rev Biochem. 1975;44:831–887. doi: 10.1146/annurev.bi.44.070175.004151. [DOI] [PubMed] [Google Scholar]
- Shapiro D. L., Marchesi V. T. Phosphorylation in membranes of intact human erythrocytes. J Biol Chem. 1977 Jan 25;252(2):508–517. [PubMed] [Google Scholar]
- Springer T. A., Strominger J. L. Detergent-soluble HLA antigens contain a hydrophilic region at the COOH-terminus and a penultimate hydrophobic region. Proc Natl Acad Sci U S A. 1976 Jul;73(7):2481–2485. doi: 10.1073/pnas.73.7.2481. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stull J. T., Brostrom C. O., Krebs E. G. Phosphorylation of the inhibitor component of troponin by phosphorylase kinase. J Biol Chem. 1972 Aug 25;247(16):5272–5274. [PubMed] [Google Scholar]
- Stull J. T., High C. W. Phosphorylation of skeletal muscle contractile proteins in vivo. Biochem Biophys Res Commun. 1977 Aug 8;77(3):1078–1083. doi: 10.1016/s0006-291x(77)80088-0. [DOI] [PubMed] [Google Scholar]
- Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2964–2968. doi: 10.1073/pnas.72.8.2964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wallach D., Davies P., Bechtel P., Willingham M., Pastan I. Cyclic AMP-dependent phosphorylation of the actin-binding protein filamin. Adv Cyclic Nucleotide Res. 1978;9:371–379. [PubMed] [Google Scholar]
- Walsh F. S., Crumpton M. J. Orientation of cell-surface antigens in the lipid bilayer of lymphocyte plasma membrane. Nature. 1977 Sep 22;269(5626):307–311. doi: 10.1038/269307a0. [DOI] [PubMed] [Google Scholar]