Abstract
The interaction of proteins with lipids is one of the central problems of membrane biophysics. Of particular interest is that some proteins require a distinct category of lipids for their function. For example, several functionally related groups of proteins that interact preferentially with acidic lipids were discovered in recent years. They include vitamin K-dependent blood coagulation proteins (Jackson and Nemerson, 1980), annexins (Geisow et al., 1987), calpactins (Glenney, 1986), synexins (Creutz et al., 1983), the protein kinase C family (Nishizuka, 1989), and actin-severing or actin-cap-ping proteins (Stossel, 1989). Many other proteins, particularly enzymes, also require acidic lipids for activation (Cornell, 1991; Enyedi et al., 1987; Moritz et al., 1992). There are excellent reviews available on many of the particular groups of proteins that interact with acidic lipids (Geisow et al., 1987; Glenney, 1986; Jackson and Nemerson, 1980; Stossel, 1989). Therefore, we decided to focus this chapter on the roles played by acidic lipids in lipid-protein interactions. For the sake of clarity, we used a limited number of examples to describe the four distinct functions performed by acidic lipids. We also review recent models of the mechanism of acidic lipid-protein interaction.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adam G, Delbrück M (1968): In: Structural Biochemistry and Molecular Biology, Rich A, Davidson N, eds., pp. 198–215. San Francisco: Freeman.
Alexander KA, Cimier B, Meier K, Storm DR (1987): J Biol Chem 262:6108–6113.
Andersson H, Bakker E, von Heijne G (1992): J Biol Chem 267:1491–1495.
Ashendel CL (1985): Biochim Biophys Acta 882:219–242.
Bazzi MD, Nelsestuen GL (1987): Biochemistry 26:5002–5008.
Bazzi MD, Nelsestuen GL (1991a): Biochemistry 30:7961–7969.
Bazzi MD, Nelsestuen GL (1991b): Biochemistry 30:7969–7977.
Bazzi MD, Nelsestuen GL (1992): Biochemistry 31:1125–1134.
Berridge MJ, Irvine RF (1984): Nature (London) 341:197–205.
Beschiaschvili G, Seelig J (1990): Biochemistry 29:52–58.
Bloom JW, Mann KG (1978): Biochemistry 17:4430–4438.
Borowski M, Furie BC, Bauminger S, Furie B (1986): J Biol Chem 261:14969–14975.
Bretscher A, Weber K (1979): Proc Natl Acad Sci USA 76:2321–2325.
Brown SS, Yamaoto K, Spudich JA (1982): JCell Biol 93:205–210.
Cafiso D, McLaughlin A, McLaughlin S, Winiski A (1989): Methods Enzymol 171:342–364.
Carnie SL/Torrie GM (1984): Adv Chem Phys 56:141–253.
Chung L, Kaloyanides R, McDaniel R, McLaughlin A, McLaughlin S (1985): Biochemistry 24:442–452.
Cornell RB (1991): Biochemistry 30:5873–5880.
Creutz CE, Dowling LG, Sando JJ, Villar-Palasi C, Whipple JH, Zaks WJ (1983): JBiol Chem 258:14664–14674.
Cutsforth GA, Whitaker RN, Hermans J, Lentz BR (1989): Biochemistry 28:7453–7461.
Del Castillo AR, Lemaire S, Tchakarov L, Jeyapragasan M, Doucet J-P, Vitale L, Trifaro J-M (1990): EMBO J 9:43–52.
Demel RA, Goormagtigh E, de Kruijff B (1990): Biochim Biophys Acta 1027:155–162.
De Vrije T, de Swart RL, Dowhan W, Tommassen J, de Kruijff B (1988): Nature (London) 334:173–175.
Dombrose FA, Gitel SN, Zawalich K, Jackson CM (1979): J Biol Chem 254:5027–5040.
Eichinger L, Schleicher M (1992): Biochemistry 31:4779–4787.
Enyedi A, Flura M, Sarkadi B, Gardos G, Crafoli E (1987): J Biol Chem 262:6425–6430.
Epand RM, Epand RF (1992): In: The Structure of Biological Membranes, Yeagle P, ed., pp. 573–601. Boca Raton: CRC Press.
Furie B, Furie BC (1988): Cell 53:505–518.
Geisow MJ, Walker JH, Boustead C, Taylor W (1987): Biosci Rep 7:291–298.
Glenney JR (1986): J Biol Chem 261:7247–7252.
Goldschmidt-Clermont PJ, Machesky LM, Baldassare JJ, Pollard TD (1990): Science 247:1575–1578.
Goldschmidt-Clermont PJ, Kim JW, Machesky LM, Rhee SG, Pollard TD (1991): Science 251:1231–1233.
Graff JM, Young TM, Johnson JD, Blackshear PJ (1989):J Biol Chem 264:21818–21823.
Hannun YA, Loomis CR, Bell RM (1985): J Biol Chem 260:10039–10043.
Hartmann E, Rapoport TA, Lodish HF (1989): Proc Natl Acad Sci USA 86:5786–5780.
Hasegawa T, Takashi S, Hayashi H, Hatano S (1980): Biochemistry 19:2677–2683.
Houbre D, Duportail G, Deloulme JC, Baudier J (1991): J Biol Chem 266:7121–7131.
Jackson CM, Nemerson Y (1980): Annu Rev Biochem 49:765–811.
Janmey PA, Stossel TP (1987): Nature (London) 325:362–364.
Janmey PA, Lamb J, Allen PG, Matsudaira PT (1992): J Biol Chem 267:11818–11823.
Jones ME, Lentz BR (1986): Biochemistry 25:567–574.
Jordi W, Hergersberg C, de Kruijff B (1992): EurJBiochem 204:841–846.
Kim J, Mosior M, Chung L, Wu H, McLaughlin S (1991): Biophys J 60:l5–U8.
Kuchinka E, Seelig J (1989): Biochemistry 28:4216–4221.
Küsters R, Dowhan W, de Kruijff B (1991): J Biol Chem 266:8659–8705.
Langner M, Cafiso D, Marcelja S, McLaughlin S (1990): Biophys J 57 :M5–M9.
Lassing I, Lindberg U (1985): Nature (London) 314:472–475.
Lester D, Epand RM (1992): Protein Kinase C: Current Concepts and Future Perspectives. Chichester, England: Ellis Horwood.
Lim TK, Bloomfield VA, Nelsestuen GL (1977): Biochemistry 16:4177–4181.
Maekawa S, Toriyama M, Hisanaga S-I, Yonezawa N, Endo S, Hirokawa N, Sakai H (1989): J5*0/ Chem 264:7458–7465.
Mann KG, Nesheim ME, Church WR, Haley P, Krishnaswamy S (1990): Blood 76:1–16.
McLaughlin S (1977): Curr Top Membr Transp 7:71–144.
McLaughlin S (1989): Annu Rev Biophys Biophys Chem 18:113–136.
Moritz A, De Graan PNE, Gispen WH, Wirtz KWA (1992):J Biol Chem 267:7207–7210.
Mosior M, Epand RM (1993): Biochemistry 32:66–75.
Mosior M, McLaughlin S (1991): Biophys J60:149–159.
Mosior M, McLaughlin S (1992a): Biochemistry 31:1768–1773.
Mosior M, McLaughlin S (1992b): Biochim Biophys Acta 1105:185–187.
Newton AC, Koshland DE, Jr. (1989): J Biol Chem 264:14909–14915.
Nicholson DW, Hergersberg C, Neupert W (1989): J Biol Chem 263:19034–19042.
Nilsson I, von Heijne G (1990): Cell 62:1135–1141.
Nishida E, Maekawa S, Sakai H (1984): Biochemistry 23:5307–5313.
Nishizuka Y (1989): Nature (London) 334:6661–6666.
Pearce KG, Hiskey RG, Thompson NL (1992): Biochemistry 31:5983–5985.
Rebecchi MJ, Peterson AA, McLaughlin S (1992): Biochemistry 31:12742–12747.
Reynolds JA (1979): Biochemistry 18:264–269.
Rosing J, Tans G, Speijer H, Zwaal RFA (1988): Biochemistry 27:9048–9055.
Roux M, Neumann J-M, Bloom M, Devaux PF (1988): Eur Biophys J 16:267–273.
Schwyzer R (1987): EMBO J 6:2255–2259.
Seelig A, Macdonald PM (1989): Biochemistry 28:4216–4221.
Stanislawski B, Ruterjans H (1987): Eur Biophys J 15:1–12.
Stossel TP (1989): J Biol Chem 264:18261–18264.
Swanljung-Collins H, Collins JH (1992): J Biol Chem 267:3445–3454.
Thelen M, Rosen A, Nairn AC, Aderem A (1991): Nature (London) 351:320–322.
Tulinsky A, Park CH, Skrzypczak-Jankun E (1988): J MolBiol 203:885–901.
von Heijne G (1986): EMBO J 5:3021–3027.
von Heinje G (1990): J Membr Biol 115:195–201.
Wei GJ, Bloomfield VA, Resnick RM, Nelsestuen GL (1982): Biochemistry 21:1949–1959.
Yin H (1979): Nature (London) 281:583–586.
Yin HL, Stossel TP (1979): Nature (London) 281:581–583.
Yonezawa N, Homma Y, Yahara I, Sakai H, Nishida E (1991):J Biol Chem 266:17218–17221.
Yu F-X, Johnston PA, Sudhof TC, Yin HL (1990): Science 250:1413–1415.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Birkhäuser Boston
About this chapter
Cite this chapter
Mosior, M., Epand, R.M. (1994). The Binding of Peptides and Proteins to Membranes Containing Anionic Lipid. In: Basava, C., Anantharamaiah, G.M. (eds) Peptides. Birkhäuser Boston. https://doi.org/10.1007/978-1-4615-8176-5_15
Download citation
DOI: https://doi.org/10.1007/978-1-4615-8176-5_15
Publisher Name: Birkhäuser Boston
Print ISBN: 978-1-4615-8178-9
Online ISBN: 978-1-4615-8176-5
eBook Packages: Springer Book Archive