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Artigos de revistas sobre o tema "Membrane proteins"

Autor: Grafiati

Publicado: 4 de junho de 2021

Última modificação: 25 de julho de 2025

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1

Jin, Wenzhen, and Syoji T. akada. "1P103 Asymmetry in membrane protein sequence and structure : Glycine outside rule(Membrane proteins,Oral Presentations)." Seibutsu Butsuri 47, supplement (2007): S49. http://dx.doi.org/10.2142/biophys.47.s49_2.

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2

Kühlbrandt, Werner. "Membrane proteins." Current Opinion in Structural Biology 1, no. 4 (1991): 531–33. http://dx.doi.org/10.1016/s0959-440x(05)80073-9.

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3

KUHLBRANDT, W., and E. GOUAUX. "Membrane proteins." Current Opinion in Structural Biology 9, no. 4 (1999): 445–47. http://dx.doi.org/10.1016/s0959-440x(99)80062-1.

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4

Hurley, James H. "Membrane Proteins." Chemistry & Biology 10, no. 1 (2003): 2–3. http://dx.doi.org/10.1016/s1074-5521(03)00006-1.

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5

Gennis, Robert B., and Werner Kühlbrandt. "Membrane proteins." Current Opinion in Structural Biology 3, no. 4 (1993): 499–500. http://dx.doi.org/10.1016/0959-440x(93)90074-u.

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6

Garavito, RMichael, and Arthur Karlin. "Membrane proteins." Current Opinion in Structural Biology 5, no. 4 (1995): 489–90. http://dx.doi.org/10.1016/0959-440x(95)80033-6.

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7

Picard, Martin. "Membrane proteins." Biochimie 205 (February 2023): 1–2. http://dx.doi.org/10.1016/j.biochi.2023.01.018.

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8

Ralston, GB. "Proteins of Marsupial Erythrocyte Membranes." Australian Journal of Biological Sciences 38, no. 1 (1985): 121. http://dx.doi.org/10.1071/bi9850121.

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The proteins of erythrocyte membranes from the red kangaroo, western grey kangaroo, eastern grey wallaroo (euro), red-necked wallaby, Tammar wallaby, and brush-tail possum have been fractionated on acrylamide gels in the presence of sodium dodecyl sulfate. The pattern of proteins was remarkably similar between the different marsupial species. The pattern of Coomassie blue-staining proteins in the membranes of these species was also very similar to that of the human erythrocyte membrane. However, the glycoproteins in the marsupial erythrocyte membranes were markedly less conspicuous than those

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9

Corey, Robin A., Phillip J. Stansfeld, and Mark S. P. Sansom. "The energetics of protein–lipid interactions as viewed by molecular simulations." Biochemical Society Transactions 48, no. 1 (2019): 25–37. http://dx.doi.org/10.1042/bst20190149.

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Membranes are formed from a bilayer containing diverse lipid species with which membrane proteins interact. Integral, membrane proteins are embedded in this bilayer, where they interact with lipids from their surroundings, whilst peripheral membrane proteins bind to lipids at the surface of membranes. Lipid interactions can influence the function of membrane proteins, either directly or allosterically. Both experimental (structural) and computational approaches can reveal lipid binding sites on membrane proteins. It is, therefore, important to understand the free energies of these interactions

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10

Thoma, Johannes, and Björn M. Burmann. "Fake It ‘Till You Make It—The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics." International Journal of Molecular Sciences 22, no. 1 (2020): 50. http://dx.doi.org/10.3390/ijms22010050.

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Membrane proteins evolved to reside in the hydrophobic lipid bilayers of cellular membranes. Therefore, membrane proteins bridge the different aqueous compartments separated by the membrane, and furthermore, dynamically interact with their surrounding lipid environment. The latter not only stabilizes membrane proteins, but directly impacts their folding, structure and function. In order to be characterized with biophysical and structural biological methods, membrane proteins are typically extracted and subsequently purified from their native lipid environment. This approach requires that lipid

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11

Brown, D., and G. L. Waneck. "Glycosyl-phosphatidylinositol-anchored membrane proteins." Journal of the American Society of Nephrology 3, no. 4 (1992): 895–906. http://dx.doi.org/10.1681/asn.v34895.

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Many proteins of eukaryotic cells are anchored to membranes by covalent linkage to glycosyl-phosphatidylinositol (GPI). These proteins lack a transmembrane domain, have no cytoplasmic tail, and are, therefore, located exclusively on the extracellular side of the plasma membrane. GPI-anchored proteins form a diverse family of molecules that includes membrane-associated enzymes, adhesion molecules, activation antigens, differentiation markers, protozoan coat components, and other miscellaneous glycoproteins. In the kidney, several GPI-anchored proteins have been identified, including uromodulin

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12

Walker, J. "Membrane proteins Membrane protein structure." Current Opinion in Structural Biology 6, no. 4 (1996): 457–59. http://dx.doi.org/10.1016/s0959-440x(96)80109-6.

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13

Tan, Sandra, Hwee Tong Tan, and Maxey C. M. Chung. "Membrane proteins and membrane proteomics." PROTEOMICS 8, no. 19 (2008): 3924–32. http://dx.doi.org/10.1002/pmic.200800597.

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14

Epand, Richard M. "Membrane Fusion." Bioscience Reports 20, no. 6 (2000): 435–41. http://dx.doi.org/10.1023/a:1010498618600.

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The fusion of biological membranes results in two bilayer-based membranes merging into a single membrane. In this process the lipids have to undergo considerable rearrangement. The nature of the intermediates that are formed during this rearrangement has been investigated. Certain fusion proteins facilitate this process. In many cases short segments of these fusion proteins have a particularly important role in accelerating the fusion process. Studies of the interaction of model peptides with membranes have allowed for increased understanding at the molecular level of the mechanism of the prom

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15

Tosaka, Toshiyuki, and Koki Kamiya. "Function Investigations and Applications of Membrane Proteins on Artificial Lipid Membranes." International Journal of Molecular Sciences 24, no. 8 (2023): 7231. http://dx.doi.org/10.3390/ijms24087231.

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Membrane proteins play an important role in key cellular functions, such as signal transduction, apoptosis, and metabolism. Therefore, structural and functional studies of these proteins are essential in fields such as fundamental biology, medical science, pharmacology, biotechnology, and bioengineering. However, observing the precise elemental reactions and structures of membrane proteins is difficult, despite their functioning through interactions with various biomolecules in living cells. To investigate these properties, methodologies have been developed to study the functions of membrane p

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16

Egger, Denise, Natalya Teterina, Ellie Ehrenfeld, and Kurt Bienz. "Formation of the Poliovirus Replication Complex Requires Coupled Viral Translation, Vesicle Production, and Viral RNA Synthesis." Journal of Virology 74, no. 14 (2000): 6570–80. http://dx.doi.org/10.1128/jvi.74.14.6570-6580.2000.

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ABSTRACT Poliovirus (PV) infection induces the rearrangement of intracellular membranes into characteristic vesicles which assemble into an RNA replication complex. To investigate this transformation, endoplasmic reticulum (ER) membranes in HeLa cells were modified by the expression of different cellular or viral membrane-binding proteins. The membrane-binding proteins induced two types of membrane alterations, i.e., extended membrane sheets and vesicles similar to those found during a PV infection. Cells expressing membrane-binding proteins were superinfected with PV and then analyzed for vir

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17

Ishikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh та Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly". Journal of Cell Biology 166, № 5 (2004): 621–27. http://dx.doi.org/10.1083/jcb.200405138.

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Mitochondrial outer and inner membranes contain translocators that achieve protein translocation across and/or insertion into the membranes. Recent evidence has shown that mitochondrial β-barrel protein assembly in the outer membrane requires specific translocator proteins in addition to the components of the general translocator complex in the outer membrane, the TOM40 complex. Here we report two novel mitochondrial outer membrane proteins in yeast, Tom13 and Tom38/Sam35, that mediate assembly of mitochondrial β-barrel proteins, Tom40, and/or porin in the outer membrane. Depletion of Tom13 or

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18

Colasante, Claudia, Frank Voncken, Theresa Manful, et al. "Proteins and lipids of glycosomal membranes from Leishmania tarentolae and Trypanosoma brucei." F1000Research 2 (January 29, 2013): 27. http://dx.doi.org/10.12688/f1000research.2-27.v1.

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In kinetoplastid protists, several metabolic pathways, including glycolysis and purine salvage, are located in glycosomes, which are microbodies that are evolutionarily related to peroxisomes. With the exception of some potential transporters for fatty acids, and one member of the mitochondrial carrier protein family, proteins that transport metabolites across the glycosomal membrane have yet to be identified. We show here that the phosphatidylcholine species composition of Trypanosoma brucei glycosomal membranes resembles that of other cellular membranes, which means that glycosomal membranes

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19

Fujiyoshi, Yoshinori. "Structural Physiology of Membrane Proteins." MEMBRANE 42, no. 5 (2017): 164–69. http://dx.doi.org/10.5360/membrane.42.164.

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20

Mitaku, Shigeki. "Structure Prediction of Membrane Proteins." membrane 19, no. 5 (1994): 305–10. http://dx.doi.org/10.5360/membrane.19.305.

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21

Mitaku, Shigeki, Ryusuke Sawada, Toshiyuki Tsuji, and Yasunori Yokoyama. "Membrane Proteins–Physics and Evolution." MEMBRANE 35, no. 2 (2010): 42–49. http://dx.doi.org/10.5360/membrane.35.42.

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22

Brijder, Robert, Matteo Cavaliere, Agustín Riscos-Núñez, Grzegorz Rozenberg, and Dragoş Sburlan. "Membrane systems with proteins embedded in membranes." Theoretical Computer Science 404, no. 1-2 (2008): 26–39. http://dx.doi.org/10.1016/j.tcs.2008.04.002.

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23

Garni, Martina, Sagana Thamboo, Cora-Ann Schoenenberger, and Cornelia G. Palivan. "Biopores/membrane proteins in synthetic polymer membranes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1859, no. 4 (2017): 619–38. http://dx.doi.org/10.1016/j.bbamem.2016.10.015.

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24

Winocour, Peter D., Cezary Watala, Dennis W. Perry, and Raelene L. Kinlough-Rathbone. "Decreased Platelet Membrane Fluidity Due to Glycation or Acetylation of Membrane Proteins." Thrombosis and Haemostasis 68, no. 05 (1992): 577–82. http://dx.doi.org/10.1055/s-0038-1646320.

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SummaryPlatelets from diabetic subjects and animals are hypersensitive to agonists in vitro. Membrane fluidity modulates cell function and previously we observed reduced membrane fluidity in platelets from diabetic patients associated with hypersensitivity to thrombin. We previously reported that decreased fluidity of isolated platelet membranes from diabetic patients is associated with increased glycation of platelet membrane proteins, but not with any change in the cholesterol to phospholipid molar ratio. We have now examined in vitro whether incubation of platelet membranes in a high glucos

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25

Koch, Johannes, and Cécile Brocard. "Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation." BioMolecular Concepts 2, no. 5 (2011): 353–64. http://dx.doi.org/10.1515/bmc.2011.031.

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AbstractSeparation of metabolic pathways in organelles is critical for eukaryotic life. Accordingly, the number, morphology and function of organelles have to be maintained through processes linked with membrane remodeling events. Despite their acknowledged significance and intense study many questions remain about the molecular mechanisms by which organellar membranes proliferate. Here, using the example of peroxisome proliferation, we give an overview of how proteins elongate membranes. Subsequent membrane fission is achieved by dynamin-related proteins shared with mitochondria. We discuss b

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26

Simunovic, Mijo, and Patricia Bassereau. "Reshaping biological membranes in endocytosis: crossing the configurational space of membrane-protein interactions." Biological Chemistry 395, no. 3 (2014): 275–83. http://dx.doi.org/10.1515/hsz-2013-0242.

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Abstract Lipid membranes are highly dynamic. Over several decades, physicists and biologists have uncovered a number of ways they can change the shape of membranes or alter their phase behavior. In cells, the intricate action of membrane proteins drives these processes. Considering the highly complex ways proteins interact with biological membranes, molecular mechanisms of membrane remodeling still remain unclear. When studying membrane remodeling phenomena, researchers often observe different results, leading them to disparate conclusions on the physiological course of such processes. Here we

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27

WANG, XUEJING, LEI WANG, XIAOJUN HAN, and CHANGJUN GUO. "MIGRATION OF CHARGED SPECIES IN LIPID BILAYER MEMBRANES UNDER AN ELECTRIC FIELD." Nano 08, no. 01 (2013): 1230006. http://dx.doi.org/10.1142/s179329201230006x.

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This paper reviews recent progress in studies on the migration of charged species, including charged lipids, membrane-attached proteins and vesicles, and integrated membrane proteins, in lipid bilayer membranes under an external electric field. The migration of these charged substances is controlled by the interplay of electrophoresis and electroosmosis. This phenomenon can be employed to separate the charged lipids and membrane-attached proteins, and concentrate integrated membrane proteins.

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28

de Almeida, J. B., E. J. Holtzman, P. Peters, L. Ercolani, D. A. Ausiello, and J. L. Stow. "Targeting of chimeric G alpha i proteins to specific membrane domains." Journal of Cell Science 107, no. 3 (1994): 507–15. http://dx.doi.org/10.1242/jcs.107.3.507.

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Heterotrimeric guanine nucleotide-regulatory (G) proteins are associated with a variety of intracellular membranes and specific plasma membrane domains. In polarized epithelial LLC-PK1 cells we have shown previously that endogenous G alpha i-2 is localized on the basolateral plasma membrane, whereas G alpha i-3 is localized on Golgi membranes. The targeting of these highly homologous G alpha i proteins to distinct membrane domains was studied by the transfection and expression of chimeric G alpha i proteins in LLC-PK1 cells. Chimeric cDNAs were constructed from the cDNAs for G alpha i-3 and G

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29

Borgese, N., S. Brambillasca, P. Soffientini, M. Yabal, and M. Makarow. "Biogenesis of tail-anchored proteins." Biochemical Society Transactions 31, no. 6 (2003): 1238–42. http://dx.doi.org/10.1042/bst0311238.

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A group of integral membrane proteins, known as C-tail anchored, is defined by the presence of a cytosolic N-terminal domain that is anchored to the phospholipid bilayer by a single segment of hydrophobic amino acids close to the C-terminus. The mode of insertion into membranes of these proteins, many of which play key roles in fundamental intracellular processes, is obligatorily post-translational, is highly specific and may be subject to regulatory processes that modulate the protein's function. Recent work has demonstrated that tail-anchored proteins translocate their C-termini across the e

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30

Asano, Shinji. "Functional Regulation of Transport Proteins by ERM (Ezrin / Radixin / Moesin) Proteins." membrane 35, no. 6 (2010): 278–84. http://dx.doi.org/10.5360/membrane.35.278.

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31

Bowden, G. H., N. Nolette, A. S. McKee, and I. R. Hamilton. "The stability of outer-membrane protein and antigen profiles of a strain of Bacteroides intermedius grown in continuous culture at different pH and growth rates." Canadian Journal of Microbiology 37, no. 5 (1991): 368–76. http://dx.doi.org/10.1139/m91-060.

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The stability of the outer-membrane proteins and antigens of a strain of Bacteroides intermedius (VP1 8944 group genotype II) grown in contious culture at varying pH and growth rates (D = 0.025–0.2 h−1, pH 6.0–7.3) has been measured. The membranes showed nine major proteins (> 67–19.55 kilodaltons) and six major antigens (65–28 kilodaltons). Membrane proteins and antigens were stable under the conditions tested; the major proteins were detected in all membranes, and the antigen profiles tested with different antisera showed maximum similarities of 82–95%. Differences did occur in the amount

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32

Carmichael, Stephen W. "Probing Individual Proteins in Unsupported Membranes." Microscopy Today 15, no. 4 (2007): 3–5. http://dx.doi.org/10.1017/s1551929500055644.

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Proteins in biologic membranes perform a large variety of essential functions. The fact that about one third of all genes code for membrane proteins, and that the majority of drugs target these proteins, attest to that fact. However, until now, proteins have been studied under artificial conditions, such as after being crystallized, frozen, or adsorbed to a substrate. Rui Pedro Gonçalves, Guillaume Agnus, Pierre Sens, Christine Houssin, Bernard Bartenlian, and Simon Scheuring have devised a novel setup with the atomic force microscope (AFM) to allow proteins to be probed while they are in unsu

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33

Nicolson, Garth L., and Gonzalo Ferreira de Mattos. "A Brief Introduction to Some Aspects of the Fluid–Mosaic Model of Cell Membrane Structure and Its Importance in Membrane Lipid Replacement." Membranes 11, no. 12 (2021): 947. http://dx.doi.org/10.3390/membranes11120947.

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Early cell membrane models placed most proteins external to lipid bilayers in trimolecular structures or as modular lipoprotein units. These thermodynamically untenable structures did not allow lipid lateral movements independent of membrane proteins. The Fluid–Mosaic Membrane Model accounted for these and other properties, such as membrane asymmetry, variable lateral mobilities of membrane components and their associations with dynamic complexes. Integral membrane proteins can transform into globular structures that are intercalated to various degrees into a heterogeneous lipid bilayer matrix

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34

Sansom, Clare. "Studying membrane proteins." Biochemist 31, no. 5 (2009): 40–41. http://dx.doi.org/10.1042/bio03105040.

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35

Weber, Manfred. "Basement membrane proteins." Kidney International 41, no. 3 (1992): 620–28. http://dx.doi.org/10.1038/ki.1992.95.

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36

Winchester, Bryan G. "Lysosomal membrane proteins." European Journal of Paediatric Neurology 5 (January 2001): 11–19. http://dx.doi.org/10.1053/ejpn.2000.0428.

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37

Bowie, J. "Stabilizing membrane proteins." Current Opinion in Structural Biology 11, no. 4 (2001): 397–402. http://dx.doi.org/10.1016/s0959-440x(00)00223-2.

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38

Prinz, William A., and Jenny E. Hinshaw. "Membrane-bending proteins." Critical Reviews in Biochemistry and Molecular Biology 44, no. 5 (2009): 278–91. http://dx.doi.org/10.1080/10409230903183472.

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39

Popot, Jean-Luc, and Matti Saraste. "Engineering membrane proteins." Current Opinion in Biotechnology 6, no. 4 (1995): 394–402. http://dx.doi.org/10.1016/0958-1669(95)80068-9.

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40

Ford, Robert C. "Photosynthetic membrane proteins." Current Opinion in Structural Biology 2, no. 4 (1992): 527–33. http://dx.doi.org/10.1016/0959-440x(92)90082-i.

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41

Kleinschmidt, J. H. "Membrane Proteins ? Introduction." Cellular and Molecular Life Sciences (CMLS) 60, no. 8 (2003): 1527–28. http://dx.doi.org/10.1007/s00018-003-3167-8.

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42

Fischer, Wolfgang B., Gerhard Thiel, and Rainer H. A. Fink. "Viral membrane proteins." European Biophysics Journal 39, no. 7 (2009): 1041–42. http://dx.doi.org/10.1007/s00249-009-0525-y.

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43

Hirano, Satoshi, Ryohei Goto, and Yasuo Uchida. "SWATH-Based Comprehensive Determination of the Localization of Apical and Basolateral Membrane Proteins Using Mouse Liver as a Model Tissue." Biomedicines 10, no. 2 (2022): 383. http://dx.doi.org/10.3390/biomedicines10020383.

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The purpose of this study was to develop a method to comprehensively determine the localization of apical and basolateral membrane proteins, using a combination of apical/basolateral membrane separation and accurate SWATH (Sequential Window Acquisition of all THeoretical fragment ion spectra) proteomics. The SWATH analysis of basolateral and apical plasma membrane fractions in mouse liver quantified the protein expression of 1373 proteins. The basolateral/apical ratios of the protein expression levels were compared with the reported immunohistochemical localization for 41 model proteins (23 ba

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44

Karotki, Lena, Juha T. Huiskonen, Christopher J. Stefan, et al. "Eisosome proteins assemble into a membrane scaffold." Journal of Cell Biology 195, no. 5 (2011): 889–902. http://dx.doi.org/10.1083/jcb.201104040.

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Spatial organization of membranes into domains of distinct protein and lipid composition is a fundamental feature of biological systems. The plasma membrane is organized in such domains to efficiently orchestrate the many reactions occurring there simultaneously. Despite the almost universal presence of membrane domains, mechanisms of their formation are often unclear. Yeast cells feature prominent plasma membrane domain organization, which is at least partially mediated by eisosomes. Eisosomes are large protein complexes that are primarily composed of many subunits of two Bin–Amphiphysin–Rvs

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45

Brône, Bert, and Jan Eggermont. "PDZ proteins retain and regulate membrane transporters in polarized epithelial cell membranes." American Journal of Physiology-Cell Physiology 288, no. 1 (2005): C20—C29. http://dx.doi.org/10.1152/ajpcell.00368.2004.

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PDZ proteins retain and regulate membrane transporters in polarized epithelial cell membranes. Am J Physiol Cell Physiol 288: C20–C29, 2005; doi:10.1152/ajpcell.00368.2004.—The plasma membrane of epithelial cells is subdivided into two physically separated compartments known as the apical and basolateral membranes. To obtain directional transepithelial solute transport, membrane transporters (i.e., ion channels, cotransporters, exchangers, and ion pumps) need to be targeted selectively to either of these membrane domains. In addition, the transport properties of an epithelial cell will be main

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46

Mirza, Shama P., Brian D. Halligan, Andrew S. Greene, and Michael Olivier. "Improved method for the analysis of membrane proteins by mass spectrometry." Physiological Genomics 30, no. 1 (2007): 89–94. http://dx.doi.org/10.1152/physiolgenomics.00279.2006.

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Membrane-bound and membrane-associated proteins are difficult to analyze by mass spectrometry, since the association with lipids impedes the isolation and solubilization of the proteins in buffers suitable for mass spectrometry and the efficient generation of positively charged peptide ions by electrospray ionization. Current methods mostly utilize detergents for the isolation of proteins from membranes. In this study, we present an improved detergent-free method for the isolation and mass spectrometric identification of membrane-bound and membrane-associated proteins. We delipidate proteins f

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47

Hanashima, Shinya, Takanori Nakane, and Eiichi Mizohata. "Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins." Membranes 11, no. 11 (2021): 823. http://dx.doi.org/10.3390/membranes11110823.

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Membrane proteins reside in the lipid bilayer of biomembranes and the structure and function of these proteins are closely related to their interactions with lipid molecules. Structural analyses of interactions between membrane proteins and lipids or detergents that constitute biological or artificial model membranes are important for understanding the functions and physicochemical properties of membrane proteins and biomembranes. Determination of membrane protein structures is much more difficult when compared with that of soluble proteins, but the development of various new technologies has

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48

Nomura, Kaoru, Shoko Mori, and Keiko Shimamoto. "Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion." Membranes 14, no. 2 (2024): 48. http://dx.doi.org/10.3390/membranes14020048.

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Membrane protein integrase (MPIase), an endogenous glycolipid in Escherichia coli (E. coli) membranes, is essential for membrane protein insertion in E. coli. We have examined Sec-independent membrane protein insertion mechanisms facilitated by MPIase using physicochemical analytical techniques, namely solid-state nuclear magnetic resonance, fluorescence measurements, and surface plasmon resonance. In this review, we outline the physicochemical characteristics of membranes that may affect membrane insertion of proteins. Subsequently, we introduce our results verifying the effects of membrane l

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49

Rawlings, Andrea E. "Membrane proteins: always an insoluble problem?" Biochemical Society Transactions 44, no. 3 (2016): 790–95. http://dx.doi.org/10.1042/bst20160025.

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Membrane proteins play crucial roles in cellular processes and are often important pharmacological drug targets. The hydrophobic properties of these proteins make full structural and functional characterization challenging because of the need to use detergents or other solubilizing agents when extracting them from their native lipid membranes. To aid membrane protein research, new methodologies are required to allow these proteins to be expressed and purified cheaply, easily, in high yield and to provide water soluble proteins for subsequent study. This mini review focuses on the relatively ne

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50

Rodgers, W., B. Crise, and J. K. Rose. "Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction." Molecular and Cellular Biology 14, no. 8 (1994): 5384–91. http://dx.doi.org/10.1128/mcb.14.8.5384-5391.1994.

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Glycosyl-phosphatidylinositol (GPI)-anchored membrane proteins and certain protein tyrosine kinases associate with a Triton X-100-insoluble, glycolipid-enriched membrane fraction in MDCK cells. Also, certain protein tyrosine kinases have been shown to associate with GPI-anchored proteins in other cell types. To characterize the interaction between GPI-anchored proteins and protein tyrosine kinases, GPI-anchored proteins were coexpressed with p56lck in HeLa cells. Both proteins were shown to target independently to the glycolipid-enriched membranes. Coimmunoprecipitation of GPI-anchored protein

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