Phospholipid-binding

Annexins form an evolutionary conserved family of Ca2+ and phospholipid binding proteins implicated in membrane trafficking and the regulation of Ca2+ currents across membranes. 

Cytoplasmic membrane Polymyxins Polyenes Imidazoles and triazoles Naftidine Disrupt bacterial membranes Disrupt fungal membranes Inhibit ergosterol synthesis Inhibits ergosterol synthesis Bind to LPS and phospholipids Bind preferentially to ergosterol Pathway not in mammalian cells Pathway not in mammalian cells... 

Proteins from cDNA libraries are used for measurement of kinase substrate specificity and identification of phospholipid-binding proteins. 

DMS also has been used to study the interaction between the Helicobacter pylori accessory proteins HypA and UreE (Benoit et al., 2007) as well as to identify the interaction between the Ca2+-binding protein S100A11 and the Ca2+- and phospholipid-binding protein annexin A6 (Chang et al., 2007). 

Tait, J.F. and Gibson, D., 1992, Phospholipid binding of annexin V effects of calcium and membrane phosphatidylserine content. Arclr Biochem. Biophys., 298 187-191. 

Fig. 9.7. Domain structure of pl20-GAP. The functional domains of pl20-GAP are shown in linear form. PH pleckstrin homology domain SH Sarc homology domain A2 possibly Ca -dependent phospholipid binding motif 1,2,3, conserved sequences characteristic for GTPase-sti-mulating activity.

Most of the proteins involved in signaling at the plasma membrane have one or more protein- or phospholipid-binding domains many have three or more, and thus are multivalent in their interactions with other signaling proteins. Figure 12-24 shows a few of the many multivalent proteins known to participate in signaling. 

Many larger lipid carrier proteins are known. The 476-residue plasma cholesteryl ester transfer protein is discussed briefly in Chapter 22. Plasma phospholipid transfer proteins are of similar size.t/U A 456-residue human phospholipid-binding protein interacts with the lipopolysaccharide of the surfaces of gram-negative bacteria (Fig. 8-30) and participates in the immune response to the bacteria. It has an elongated boomerang shape with two cavities, both of which bind a molecule of phosphatidylcholine. Other plasma lipid transfer proteins may have similar structures/... 

Bizzaro, N., Tonutti, E., Villalta, D., Tampoia, M., and R. Tozzoli, 2005, Prevalence and clinical correlation of anti-phospholipid-binding protein antibodies in anticardiolipin-negative patients with systemic lupus erythematosus and women with unexplained recurrent miscarriages. Arch Pathol Lab Med.l29(l) 61-8. 

Tompa, P., Emori, Y., Sorimachi, H., Suzuki, K., Friedrich, P., 2001, Domain 111 of calpain is a Ca2+ -regulated phospholipid-binding domain, Biochem. Biophys. Res. Commun., 280, 1333-1339 Tompa, P., Mucsi, Z., Orosz, G., Friedrich, P., 2002, Calpastatin subdomains A and C are activators of calpain, J. Biol. Chem., 277, 9022-6... 

Corticosteroids block all the known pathways of eicosanoid synthesis, perhaps by stimulating the synthesis of several inhibitory proteins collectively called annexins or lipocortins. They inhibit phospholipase A2 activity, probably by interfering with phospholipid binding and thus preventing the release of arachidonic acid. 

Li C, Takei K, Geppert M et al (1994) Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C. Neuron 13 885-98 Li L, Chin LS, Shupliakov O et al (1995) Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice. Proc Natl Acad Sci USA 92 9235-9... 

I 84 Asherson FLA, Antiphospholipid antibodies. Clinical complications reported in medical literature, In Harris EN, Exner T, Hughes GRY Asherson FLA, eds, Phospholipid-Binding Antibodies. Boston CRC Press, Inc, 1991 388-402,... 

Ching-hsien H., in Phospholipid Binding Antibodies, E.N. Harris, T. Exner, G.R.V. Hughes, R.A. Asherson (Eds.), CRC Press, Boca Raton 1991, pp. 4-27. 

Apolipoprotein C-II can also be isolated from VLDL or HDL (H20, L5, N3). It contains 78 residues (J3) and has been shown by Chou-Fasman analysis to bind phospholipids (M26, M40), with three predicted helical sequences (M26). ApoC-II has attracted a great deal of attention because it activates one of the most important enzymes in plasma lipid metabolism, lipoprotein lipase, responsible for the hydrolysis of triglyceride in chylomicrons and VLDL. Sparrow and Gotto have summarized a number of studies on structure-function relationships (S52). These, taken together, indicate that there are separate functional domains in apoC-II, in that lipoprotein lipase activation is mediated by residues 55-78 and phospholipid binding by... 

Perisic, O., Fong, S., Lynch, D.E., Bycroft, M., and Williams, R.L., 1998, Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273 1596-1604. 

Structure of the first C2 domain of synaptotagmin I a novel calcium/phospholipid-binding fold. Cell 80 929-938. 

Sutton, R.B., and Sprang, S.R., 1998, Structure ofthe protein kinase C phospholipid-binding C2 domain complexed with Ca2+. Structure 6 1395-1405. 

Vascular anticoagulant beta a novel human Ga /phospholipid binding protein that inhibits coagulation and phospholipase A2 activity. Its molecular cloning, expression and comparison with VAG-alpha. Eur. J. Biochem. 185,... 

M. J. Bottomley, K. Salim, and G. Panayotou. Phospholipid-binding protein domains. Biochim Biophys Acta, 1436, 165-183, 1998. 

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