Physiology of Membrane Disorders pp 45-55 | Cite as
Membrane Proteins
Abstract
The membranes of a cell have the principal function of setting the boundaries between the cell and the environment and between compartments within the cell. These boundaries prevent the movement of all polar solutes from one compartment to another, unless such movement is required for biological activity; under these circumstances, special transport systems are required. Thus, membranes can be considered as structures which are selectively permeable. The barrier to movement of polar solutes across the membrane is provided by one of the two major components of the membrane: the lipids. The other major component of the membrane, the proteins, provides the permeability function. Membrane proteins also determine most of the other properties of a membrane: They carry the determinants of specificity which distinguish one cell from another and allow for recognition between cells; they determine the shape and architecture of the membrane; they are the receptors for information about the environment and relay that information to other parts of the cell; and they are enzymes with a precise compartmental localization.
Keywords
Human Erythrocyte Intrinsic Protein Extrinsic Protein Human Erythrocyte Membrane Intrinsic Membrane ProteinPreview
Unable to display preview. Download preview PDF.
References
- 1.Guidotti, G. 1972. Membrane proteins. Annu. Rev. Biochem. 41: 731–752.PubMedCrossRefGoogle Scholar
- 2.Singer, S. J. 1974. The molecular organization of membranes. Annu. Rev. Biochem. 43: 805–833.PubMedCrossRefGoogle Scholar
- 3.Clarke, S. 1975. The size and detergent binding of membrane proteins. J. Biol. Chem. 250: 5459–5469.PubMedGoogle Scholar
- 4.Steck, T. L. 1974. The organization of proteins in the human red blood cell membrane. J. Cell Biol. 62: 1–19.PubMedCrossRefGoogle Scholar
- 5.Marchesi, V. T., H. Furthmayr, and M. Tomita. 1976. The red cell membrane. Annu. Rev. Biochem. 45: 667–698.PubMedCrossRefGoogle Scholar
- 6.Bretscher, M. S., andM. C. Raff. 1975. Mammalian plasma mem-branes. Nature (.London) 258: 43–49.CrossRefGoogle Scholar
- 7.Rothman, J. E., and J. Lenard. 1977. Membrane asymmetry: The nature of membrane asymmetry provides clues to the puzzle of how membranes are assembled. Science 195: 743–753.PubMedCrossRefGoogle Scholar
- 8.Murthy, S. N. P., T. Lin, R. K. Kaul, H. Kohler, andT. L. Steck. 1981. The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3. J. Biol. Chem. 256: 11203–11208.PubMedGoogle Scholar
- 9.Branton, D., C. M. Cohen, and J. Tyler. 1981. Interaction of cytoskeletal proteins on the human erythrocyte membrane. Cell 24: 24–32.PubMedCrossRefGoogle Scholar
- 10.Bennett, V. 1982. The molecular basis for membrane-cytoskeleton association in human erythrocytes. J. Cell Biochem. 18: 49–66.PubMedCrossRefGoogle Scholar
- 11.Goodman, S. R., J. Yu, C. F. Whitfield, E. N. Culp, and E. J. Posnak. 1982. Erythrocyte membrane skeletal protein bands 4.1a and b are sequence-related phosphoproteins. J. Biol. Chem. 257: 4564–4569.PubMedGoogle Scholar
- 12.Tyler, J. M., B. N. Reinhardt, andD. Branton. 1980. Associations of erythrocyte membrane proteins: Binding of purified bands 2.1 and 4.1 to spectrin. J. Biol. Chem. 255: 7034–7039.PubMedGoogle Scholar
- 13.Goodman, S. R., and K. Shiffer. 1983. The spectrin membrane skeleton of normal and abnormal human erythrocytes: A review. Am. J. Physiol. 244: C121–C141.PubMedGoogle Scholar
- 14.Lazarides, E., and W. J. Nelson. 1982. Expression of spectrin in nonerythroid cells. Cell 31: 505–508.PubMedCrossRefGoogle Scholar
- 15.Nelson, W. J., and Lazarides, E. 1983. Switching of subunit com-position of muscle spectrin during myogenesis in vitro. Nature (London) 304: 364–368.CrossRefGoogle Scholar
- 16.Bennett, V. 1979. Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues. Nature (London) 281: 597–599.CrossRefGoogle Scholar
- 17.Cohen, C. M., S. F. Foley, and C. Korsgren. 1981. A protein immunologically related to erythrocyte band 4.1 is found on stress fibers of non-erythroid cells. Nature (London) 294: 648–650.CrossRefGoogle Scholar
- 18.Rothman, J. E., and H. F. Lodish. 1977. Synchronized trans-membrane insertion and glycosylation of a nascent membrane protein. Nature (London) 269: 775–780.CrossRefGoogle Scholar
- 19.Wilson, I. A., J. J. Skehel, andD. C. Wiley, 1981. Structure of the haemagglutinin membrane glycoprotein in influenza virus at 3A resolution. Nature (London) 289: 366–373.CrossRefGoogle Scholar
- 20.Nathenson, S. G., H. Uehara, andB. M. Ewenstein. 1981. Primary structural analysis of the transplantation antigens of the murine H-2 major histocompatibility complex. Annu. Rev. Biochem. 50: 1025–1052.PubMedCrossRefGoogle Scholar
- 21.Kaufman, J. F., and J. L. Strominger. 1979. Both chains of HLA- DR bind to the membrane with a penultimate hydorphobic region and the heavy chain is phosphorylated at its hydrophilic carboxy terminus. Proc. Natl. Acad. Sci. U.S.A. 76: 6304–6308.PubMedCrossRefGoogle Scholar
- 22.Hauri, H. P., H. Wacker, E. E. Rickli, B. Bigler-Meier, A. Quaroni, and G. Semenza. 1982. Biosynthesis of sucrase-iso- maltase: Purification and NH2-terminal amino acid sequence of the rat sucrase-isomaltase precursor (pro-sucrase-isomaltase) from fetal intestinal transplants. J. Biol. Chem. 257: 4522–4528.PubMedGoogle Scholar
- 23.Ward, C. W., T. C. Ellman, and A. A. Azad. 1982. Amino acid sequence of the Pronase-related heads of neuraminidase subtype N2 from the Asian strain A/Tokyo/3/67 of influenza virus. Biochem. J. 207: 91–95.PubMedGoogle Scholar
- 24.Enook, H. G., A. Catola, and P. Strittmatter. 1976. Mechanism of rat liver microsomal stearyl-CoA desaturase. J. Biol. Chem. 251: 5095–5103.Google Scholar
- 25.Takagaki, Y., R. Radhakrishnan, K. W. A. Wirtz, and H. G. Khorana. 1983. The membrane-embedded segment of cytochrome b5 as studied by cross-linking with photoactivatable phospholipids. J. Biol. Chem. 258: 9136–9142.PubMedGoogle Scholar
- 26.Cantley, L. C. 1981. Structure and mechanism of the (Na, K)- ATPase. Curr. Top. Bioenerg. 11: 201–237.Google Scholar
- 27.Ikemoto, N. 1982. Structure and function of the calcium pump protein of sarcoplasmic reticulum. Annu. Rev. Physiol. 44: 297–317.PubMedCrossRefGoogle Scholar
- 28.Guidotti, G. 1980. The structure of the band 3 polypeptide. Alfred Benzon Symp. 14: 300–311.Google Scholar
- 29.Knauf, P. A. 1979. Erythrocyte anion exchange and the band 3 protein: Transport kinetics and molecular structure. Curr. Top. Membr. Transp. 12: 249–363.Google Scholar
- 30.Dratz, E. A., and P. A. Hargrave. 1983. The structure of rhodopsin and the rod outer segment disk membrane. Trends Biochem. Sci. 8: 128–131.CrossRefGoogle Scholar
- 31.Stoeckenius, W., and R. A. Bogomolni. 1982. Bacteriorhodopsin. Annu. Rev. Biochem. 52: 587–616.CrossRefGoogle Scholar
- 32.Conti-Tronconi, B. M., and M. A. Raftery. 1982. The nicotinic cholinergic receptor: Correlation of molecular structure with functional properties. Annu. Rev. Biochem. 51: 491–530.PubMedCrossRefGoogle Scholar
- 33.Noda, M., H. Takahashi, T. Tanabe, M. Toyosato, S. Kikyyotani, Y. Furutani, T. Hirose, H. Takashimo, S. Inayama, T. Miyata, and S. Numa. 1983. Structural homology of Torpedo californica acetyl-choline receptor subunits. Nature 302: 528–532.PubMedCrossRefGoogle Scholar
- 34.Devillers-Thiery, A., J. Giraudat, M. Bentaboulet, and J. P. Changeux. 1983. Complete mRNA coding sequence of the acetyl-choline binding a-subunit of Torpedo marmorata acetylcholine re-ceptor: A model for the transmembrane organization of the polypeptide chain. Proc. Natl. Acad. Sci. U.S.A. 80: 2067–2071.PubMedCrossRefGoogle Scholar
- 35.Kyte, J. 1975. Structural studies of sodium and potassium ion activated adenosine triphosphatase. J. Biol. Chem. 250: 7443–7449.PubMedGoogle Scholar
- 36.Bretscher, M. S. 1971. A major protein which spans the human erythrocyte membrane. J. Mol. Biol. 59: 351–357.PubMedCrossRefGoogle Scholar
- 37.Guidotti, G. 1979. Coupling of ion transport to enzyme activity. In: The Neurosciences: Fourth Study Program. F. O. Schmitt and F. G. Worden, eds. MIT Press, Cambridge, Mass. pp. 831–840.Google Scholar
- 38.Monod, J., J. Wyman, and J. P. Changeux. 1965. On the nature of allosteric transitions: A plausible model. J. Mol. Biol. 12: 88–118.PubMedCrossRefGoogle Scholar
- 39.Palade, G. E. 1975. Intracellular aspects of the process of protein synthesis. Science 189: 347–358.PubMedCrossRefGoogle Scholar
- 40.Bretscher, M. S. 1973. Membrane structure: Some general principles. Science 181: 622–629.PubMedCrossRefGoogle Scholar
- 41.Kresheck, G. G., and I. M. Klotz. 1969. The thermodynamics of transfer of amides from an apolar to an aqueous solution. Biochemistry 8: 8–12.CrossRefGoogle Scholar
- 42.Henderson, R., and P. N. T. Unwin. 1975. Three dimensional model of purple membrane obtained by electron microscopy. Nature (London) 257: 28–32.CrossRefGoogle Scholar
- 43.McLachlan, A. D., and M. Stewart. 1975. Tropomyosin coiled- coil interactions: Evidence for an unstaggered structure. J. Mol. Biol. 98: 293–304.PubMedCrossRefGoogle Scholar
- 44.Clothia, C. 1976. The nature of accessible and buried surfaces in proteins. J. Mol. Biol. 105: 1–14.CrossRefGoogle Scholar
- 45.Kreil, G. 1981. Transfer of proteins across membranes. Annu. Rev. Biochem. 50: 317–348.PubMedCrossRefGoogle Scholar
- 46.Ploegh, H. L., L. F. Cannon, and J. L. Strominger. 1979. Cell-free translation of the mRNA for the heavy and light chains of HLA-A and HLA-B antigens. Proc. Natl. Acad. Sci. U.S.A. 76: 2273–2277.PubMedCrossRefGoogle Scholar
- 47.Porter, A. G., C. Barber, N. H. Carey, R. A. Hallewell, G. Threlfall, and J. S. Emtage. 1979. Complete nucleotide sequence of influenza virus haemagglutinin gene from cloned DNA. Nature (London) 282: 471–477.CrossRefGoogle Scholar
- 48.Walter, P., and G. Blobel. 1982. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature (London) 299: 691–698.CrossRefGoogle Scholar
- 49.Meyer, D. I., E. Krause, and B. Dobberstein. 1982. Secretory protein translocation across membranes: The role of the docking protein. Nature (London) 297: 647–650.CrossRefGoogle Scholar
- 50.Chin, G., and M. Forgac. 1983. Topological localization of proteolytic sites of sodium and potassium ion stimulated ade- nosinetriphosphatase. Biochemistry 22: 3405–3410.PubMedCrossRefGoogle Scholar
- 51.Reithmeier, R. A. F., and D. H. MacLennan. 1981. The NH2- terminus of the (Ca+ + + Mg+ +)-adenosine triphosphatase is located on the cytoplasmic surface of the sacroplasmic reticulum membrane. J. Biol. Chem. 256: 5957–5960.PubMedGoogle Scholar
- 52.Reithmeier, R. A. F., S. deLeon, and D. H. MacLennan. 1980. Assembly of the sarcoplasmic reticulum: Cell-free synthesis of the Ca + + + Mg+ +-adenosine triphosphatase and calsequestrin. J. Biol. Chem. 255: 11839–11846.PubMedGoogle Scholar
- 53.Chyn, T. L., A. N. Martonosi, T. Morimoto, and D. D. Sabatini. 1970. In vitro synthesis of the CA+ + transport ATPase by ribosomes bound to sarcoplasmic reticulum membranes. Proc. Natl. Acad. Sci. U.S.A. 76: 1241–1245.CrossRefGoogle Scholar