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Journal articles on the topic 'Membrane proteins'

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Published: 4 June 2021

Last updated: 7 September 2023

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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 (August 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 (August 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 (January 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 (August 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 (August 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

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

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9

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

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10

Brown, D., and G. L. Waneck. "Glycosyl-phosphatidylinositol-anchored membrane proteins." Journal of the American Society of Nephrology 3, no. 4 (October 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 (Tamm-Horsfall glycoprotein), carbonic anhydrase type IV, alkaline phosphatase, Thy-1, BP-3, aminopeptidase P, and dipeptidylpeptidase. GPI-anchored proteins can be released from membranes with specific phospholipases and can be recovered from the detergent-insoluble pellet after Triton X-114 treatment of membranes. All GPI-anchored proteins are initially synthesized with a transmembrane anchor, but after translocation across the membrane of the endoplasmic reticulum, the ecto-domain of the protein is cleaved and covalently linked to a preformed GPI anchor by a specific transamidase enzyme. Although it remains obscure why so many proteins are endowed with a GPI anchor, the presence of a GPI anchor does confer some functional characteristics to proteins: (1) it is a strong apical targeting signal in polarized epithelial cells; (2) GPI-anchored proteins do not cluster into clathrin-coated pits but instead are concentrated into specialized lipid domains in the membrane, including so-called smooth pinocytotic vesicles, or caveoli; (3) GPI-anchored proteins can act as activation antigens in the immune system; (4) when the GPI anchor is cleaved by PI-phospholipase C or PI-phospholipase D, second messengers for signal transduction may be generated; (5) the GPI anchor can modulate antigen presentation by major histocompatibility complex molecules. Finally, at least one human disease, paroxysmal nocturnal hemoglobinuria, is a result of defective GPI anchor addition to plasma membrane proteins.

11

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 of the human erythrocyte membrane. Furthermore, the mobilities of the glycoproteins from the marsupials were different from those of the human erythrocyte membrane.

12

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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13

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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14

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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15

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 (September 2008): 26–39. http://dx.doi.org/10.1016/j.tcs.2008.04.002.

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16

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 (April 2017): 619–38. http://dx.doi.org/10.1016/j.bbamem.2016.10.015.

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17

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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18

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 (December 23, 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 membranes are replaced by suitable surrogates, which ideally closely mimic the native bilayer, in order to maintain the membrane proteins structural and functional integrity. In this review, we survey the currently available membrane mimetic environments ranging from detergent micelles to bicelles, nanodiscs, lipidic-cubic phase (LCP), liposomes, and polymersomes. We discuss their respective advantages and disadvantages as well as their suitability for downstream biophysical and structural characterization. Finally, we take a look at ongoing methodological developments, which aim for direct in-situ characterization of membrane proteins within native membranes instead of relying on membrane mimetics.

19

Sansom, Clare. "Studying membrane proteins." Biochemist 31, no. 5 (October 1, 2009): 40–41. http://dx.doi.org/10.1042/bio03105040.

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20

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

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21

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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22

Bowie, J. "Stabilizing membrane proteins." Current Opinion in Structural Biology 11, no. 4 (August 1, 2001): 397–402. http://dx.doi.org/10.1016/s0959-440x(00)00223-2.

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23

Prinz, William A., and Jenny E. Hinshaw. "Membrane-bending proteins." Critical Reviews in Biochemistry and Molecular Biology 44, no. 5 (September 25, 2009): 278–91. http://dx.doi.org/10.1080/10409230903183472.

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24

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

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25

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

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26

Kleinschmidt, J. H. "Membrane Proteins ? Introduction." Cellular and Molecular Life Sciences (CMLS) 60, no. 8 (August 1, 2003): 1527–28. http://dx.doi.org/10.1007/s00018-003-3167-8.

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27

Fischer, Wolfgang B., Gerhard Thiel, and Rainer H. A. Fink. "Viral membrane proteins." European Biophysics Journal 39, no. 7 (August 12, 2009): 1041–42. http://dx.doi.org/10.1007/s00249-009-0525-y.

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28

Takeuchi, Toshihumi. "Molecular Imprinting for Proteins." MEMBRANE 34, no. 6 (2009): 316–21. http://dx.doi.org/10.5360/membrane.34.316.

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29

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 (December 24, 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. This affords a more complete view of the engagement of a particular protein with the biological membrane surrounding it. Here, we describe many computational approaches currently in use for this purpose, including recent advances using both free energy and unbiased simulation methods. In particular, we focus on interactions of integral membrane proteins with cholesterol, and with anionic lipids such as phosphatidylinositol 4,5-bis-phosphate and cardiolipin. Peripheral membrane proteins are exemplified via interactions of PH domains with phosphoinositide-containing membranes. We summarise the current state of the field and provide an outlook on likely future directions of investigation.

30

Epand, Richard M. "Membrane Fusion." Bioscience Reports 20, no. 6 (December 1, 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 promotion of membrane fusion by fusion proteins. There is an increased appreciation of the roles of several independent segments of fusion proteins in promoting the fusion process. Many of the studies of the fusion of biological membranes have been done with the fusion of enveloped viruses with other membranes. One reason for this is that the number of proteins involved in viral fusion is relatively simple, often requiring only a single protein. For many enveloped viruses, the structure of their fusion proteins has certain common elements, suggesting that they all promote fusion by an analogous mechanism. Some aspects of this mechanism also appears to be common to intracellular fusion, although several proteins are involved in that process which is more complex and regulated than is fusion.

31

Stevens, Timothy J., and Isaiah T. Arkin. "Are membrane proteins ?inside-out? proteins?" Proteins: Structure, Function, and Genetics 36, no. 1 (July 1, 1999): 135–43. http://dx.doi.org/10.1002/(sici)1097-0134(19990701)36:1<135::aid-prot11>3.0.co;2-i.

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32

Ataka, Kenichi, Joachim Heberle, Axel Baumann, Silke Kerruth, Ramona Schlesinger, Joerg Fitter, and Georg Bueldt. "2P103 Direct monitoring of membrane protein folding process during in-vitro expression by Surface Enhanced IR spectroscopy(03. Membrane proteins,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S176. http://dx.doi.org/10.2142/biophys.53.s176_1.

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33

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 glucose medium causes sufficient glycation to reduce membrane fluidity. Incubation of platelet membranes from control subjects in a high glucose (16.1 mM) medium for 10 days at 37° C led to an increase in the extent of glycation of membrane proteins and a decrease in membrane fluidity (indicated by an increase in steady state fluorescence polarization); most of the changes occurred within the first 3 days of incubation. Incubation of platelet membranes with 5.4 mM glucose had less effect. In contrast, incubation of platelet membranes with the same concentrations of 1–0-methylglucose did not cause a change in either the extent of glycation of proteins or membrane fluidity. We also determined if acetylation by aspirin or acetyl chloride of the sites available for glycation on platelet membrane proteins leads to a similar reduction in membrane fluidity. Pretreatment of platelet membranes with aspirin or acetyl chloride diminished the extent of glycation that occurred when platelet membranes were subsequently incubated with glucose, but membrane fluidity was reduced even in the absence of glucose; subsequent incubation with glucose caused no further reduction in membrane fluidity. Similar results were obtained when red blood cells were incubated with high concentrations of glucose or methyl glucose either with or without pretreatment with aspirin or acetyl chloride. Further experiments using platelet membranes showed that the reduction in membrane fluidity due to aspirin was independent of its acetylating effect on platelet cyclo-oxygenase. Ingestion of aspirin also caused a reduction in membrane fluidity of platelets. Therefore, glycation of platelet membrane proteins reduces membrane fluidity, but the effect results from occupation of the sites available for glycation and not the presence of glucose moieties per se at these sites. Acetylation of platelet membrane proteins either in vitro or in vivo also reduces membrane fluidity; this effect is not associated with platelet hypersensitivity to thrombin.

34

Lu, Yiqin, and Junfan Liu. "Erythrocyte membrane proteins and membrane skeleton." Frontiers of Biology in China 2, no. 3 (July 2007): 247–55. http://dx.doi.org/10.1007/s11515-007-0035-1.

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35

Okada, Tetsuji, and Tsutomu Kouyama. "Structure and Function of Membrane Proteins." membrane 21, no. 4 (1996): 230–39. http://dx.doi.org/10.5360/membrane.21.230.

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36

Nishino, Yuri, and Atsuo Miyazawa. "Two-dimensional Crystallization of Membrane Proteins." MEMBRANE 32, no. 1 (2007): 25–31. http://dx.doi.org/10.5360/membrane.32.25.

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37

Kimura, Katsuki. "Polysaccharides and Proteins Causing Membrane Fouling." MEMBRANE 37, no. 5 (2012): 230–34. http://dx.doi.org/10.5360/membrane.37.230.

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38

Karotki, Lena, Juha T. Huiskonen, Christopher J. Stefan, Natasza E. Ziółkowska, Robyn Roth, Michal A. Surma, Nevan J. Krogan, et al. "Eisosome proteins assemble into a membrane scaffold." Journal of Cell Biology 195, no. 5 (November 28, 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 domain–containing proteins, Pil1 and Lsp1. In this paper, we show that these proteins self-assemble into higher-order structures and bind preferentially to phosphoinositide-containing membranes. Using a combination of electron microscopy approaches, we generate structural models of Pil1 and Lsp1 assemblies, which resemble eisosomes in cells. Our data suggest that the mechanism of membrane organization by eisosomes is mediated by self-assembly of its core components into a membrane-bound protein scaffold with lipid-binding specificity.

39

Miyoshi, Taro, Yuhei Nagai, Tomoyasu Aizawa, Katsuki Kimura, and Yoshimasa Watanabe. "Proteins causing membrane fouling in membrane bioreactors." Water Science and Technology 72, no. 6 (June 2, 2015): 844–49. http://dx.doi.org/10.2166/wst.2015.282.

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In this study, the details of proteins causing membrane fouling in membrane bioreactors (MBRs) treating real municipal wastewater were investigated. Two separate pilot-scale MBRs were continuously operated under significantly different operating conditions; one MBR was a submerged type whereas the other was a side-stream type. The submerged and side-stream MBRs were operated for 20 and 10 days, respectively. At the end of continuous operation, the foulants were extracted from the fouled membranes. The proteins contained in the extracted foulants were enriched by using the combination of crude concentration with an ultrafiltration membrane and trichloroacetic acid precipitation, and then separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The N-terminal amino acid sequencing analysis of the proteins which formed intensive spots on the 2D-PAGE gels allowed us to partially identify one protein (OmpA family protein originated from genus Brevundimonas or Riemerella anatipestifer) from the foulant obtained from the submerged MBR, and two proteins (OprD and OprF originated from genus Pseudomonas) from that obtained from the side-stream MBR. Despite the significant difference in operating conditions of the two MBRs, all proteins identified in this study belong to β-barrel protein. These findings strongly suggest the importance of β-barrel proteins in developing membrane fouling in MBRs.

40

Rawlings, Andrea E. "Membrane proteins: always an insoluble problem?" Biochemical Society Transactions 44, no. 3 (June 9, 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 new area of water soluble membrane proteins and in particular two innovative approaches: the redesign of membrane proteins to yield water soluble variants and how adding solubilizing fusion proteins can help to overcome these challenges. This review also looks at naturally occurring membrane proteins, which are able to exist as stable, functional, water soluble assemblies with no alteration to their native sequence.

41

Carmichael, Stephen W. "Probing Individual Proteins in Unsupported Membranes." Microscopy Today 15, no. 4 (July 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 unsupported membranes. Their method is similar in principle to methods where a small area of a membrane is sampled, such as when a piece of membrane is examined by patch clamping. The difference is that instead of attaching a membrane to the end of a pipette, it is spread across a piece of perforated Si(001).

42

Borgese, N., S. Brambillasca, P. Soffientini, M. Yabal, and M. Makarow. "Biogenesis of tail-anchored proteins." Biochemical Society Transactions 31, no. 6 (December 1, 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 endoplasmic reticulum membrane by a mechanism different from that used for Sec61-dependent post-translational signal-peptide-driven translocation. Here we summarize recent results on the insertion of tail-anchored proteins and discuss possible mechanisms that could be involved.

43

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 (July 15, 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 virus replication, location of membranes, viral protein, and RNA by immunofluorescence and fluorescent in situ hybridization. Cultures expressing cellular or viral membrane-binding proteins, but not those expressing soluble proteins, showed a markedly reduced ability to support PV replication as a consequence of the modification of ER membranes. The altered membranes, regardless of their morphology, were not used for the formation of viral replication complexes during a subsequent PV infection. Specifically, membrane sheets were not substrates for PV-induced vesicle formation, and, surprisingly, vesicles induced by and carrying one or all of the PV replication proteins did not contribute to replication complexes formed by the superinfecting PV. The formation of replication complexes required active viral RNA replication. The extensive alterations induced by membrane-binding proteins in the ER resulted in reduced viral protein synthesis, thus affecting the number of cells supporting PV multiplication. Our data suggest that a functional replication complex is formed in cis, in a coupled process involving viral translation, membrane modification and vesicle budding, and viral RNA synthesis.

44

Tosaka, Toshiyuki, and Koki Kamiya. "Function Investigations and Applications of Membrane Proteins on Artificial Lipid Membranes." International Journal of Molecular Sciences 24, no. 8 (April 13, 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 proteins that have been purified from biological cells. In this paper, we introduce various methods for creating liposomes or lipid vesicles, from conventional to recent approaches, as well as techniques for reconstituting membrane proteins into artificial membranes. We also cover the different types of artificial membranes that can be used to observe the functions of reconstituted membrane proteins, including their structure, number of transmembrane domains, and functional type. Finally, we discuss the reconstitution of membrane proteins using a cell-free synthesis system and the reconstitution and function of multiple membrane proteins.

45

Ishikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh, and Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly." Journal of Cell Biology 166, no. 5 (August 23, 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 Tom38/Sam35 affects assembly pathways of the β-barrel proteins differently, suggesting that they mediate different steps of the complex assembly processes of β-barrel proteins in the outer membrane.

46

Colasante, Claudia, Frank Voncken, Theresa Manful, Thomas Ruppert, Aloysius G. M. Tielens, Jaap J. van Hellemond, and Christine Clayton. "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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Abstract:

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 are expected to be impermeable to small hydrophilic molecules unless transport is facilitated by specialized membrane proteins. Further, we identified 464 proteins in a glycosomal membrane preparation from Leishmania tarentolae. The proteins included approximately 40 glycosomal matrix proteins, and homologues of peroxisomal membrane proteins - PEX11, GIM5A and GIM5B; PXMP4, PEX2 and PEX16 - as well as the transporters GAT1 and GAT3. There were 27 other proteins that could not be unambiguously assigned to other compartments, and that had predicted trans-membrane domains. However, no clear candidates for transport of the major substrates and intermediates of energy metabolism were found. We suggest that, instead, these metabolites are transported via pores formed by the known glycosomal membrane proteins.

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Mulkidjanian, Armen Y., Michael Y. Galperin, and Eugene V. Koonin. "Co-evolution of primordial membranes and membrane proteins." Trends in Biochemical Sciences 34, no. 4 (April 2009): 206–15. http://dx.doi.org/10.1016/j.tibs.2009.01.005.

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Javanainen, Matti, O. H. Samuli Ollila, and Hector Martinez-Seara. "Rotational Diffusion of Membrane Proteins in Crowded Membranes." Journal of Physical Chemistry B 124, no. 15 (March 18, 2020): 2994–3001. http://dx.doi.org/10.1021/acs.jpcb.0c00884.

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Dunleavy, Katie, Anika Rannikko, Anne Rice, Samantha Jaworski, Michael Fealey, Ryan Mahling, and Anne Hinderliter. "Membranes in Flux: Proteins Effect on Membrane Permeability." Biophysical Journal 106, no. 2 (January 2014): 302a. http://dx.doi.org/10.1016/j.bpj.2013.11.1754.

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Im, Wonpil. "Bacterial Outer Membranes and Interactions with Membrane Proteins." Biophysical Journal 108, no. 2 (January 2015): 370a. http://dx.doi.org/10.1016/j.bpj.2014.11.2030.

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