membrane fusion proteins


Summary: Proteins that catalyze MEMBRANE FUSION.

Top Publications

  1. Zgurskaya H, Yamada Y, Tikhonova E, Ge Q, Krishnamoorthy G. Structural and functional diversity of bacterial membrane fusion proteins. Biochim Biophys Acta. 2009;1794:794-807 pubmed publisher
    b>Membrane Fusion Proteins (MFPs) are functional subunits of multi-component transporters that perform diverse physiological functions in both Gram-positive and Gram-negative bacteria...
  2. De Angelis F, Lee J, O Connell J, Miercke L, Verschueren K, Srinivasan V, et al. Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proc Natl Acad Sci U S A. 2010;107:11038-43 pubmed publisher
    ..The structural rearrangements between the two states suggest an active role in substrate efflux through metal binding and release. ..
  3. Srinivasan V, Rajamohan G, Pancholi P, Marcon M, Gebreyes W. Molecular cloning and functional characterization of two novel membrane fusion proteins in conferring antimicrobial resistance in Acinetobacter baumannii. J Antimicrob Chemother. 2011;66:499-504 pubmed publisher
    The aim of this study was to elucidate the role of two novel membrane fusion proteins (MFPs) in the susceptibility of Acinetobacter baumannii to antimicrobial agents. The genome sequence of A...
  4. Song J, Wang X, Lei C, Piao J, Yin C, Zhang Z, et al. Fusion of chemotactic peptide to a single-chain bi-specific antibody (scBsAb) potentiates its cytotoxicity to target tumour cells. Biotechnol Appl Biochem. 2006;45:147-54 pubmed
    ..The results indicated that fusion of chemotactic peptide to BsAb potentiated its cytotoxicity to tumour cells in vitro. It suggests that 18TBHL may be a promising candidate agent in cancer immunotherapy. ..
  5. Yum S, Xu Y, Piao S, Sim S, Kim H, Jo W, et al. Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. J Mol Biol. 2009;387:1286-97 pubmed publisher
    ..The hexameric structure of MacA provides insight into the oligomeric state in the functional complex of the drug efflux pump and type I secretion system...
  6. Ding B, Hong N, Christofidou Solomidou M, Gottstein C, Albelda S, Cines D, et al. Anchoring fusion thrombomodulin to the endothelial lumen protects against injury-induced lung thrombosis and inflammation. Am J Respir Crit Care Med. 2009;180:247-56 pubmed publisher
    ..Targeting TM to the endothelium using an scFv anchor enhances its antithrombotic and antiinflammatory effectiveness in models of ALI. ..
  7. Nocentini G, Cuzzocrea S, Genovese T, Bianchini R, Mazzon E, Ronchetti S, et al. Glucocorticoid-induced tumor necrosis factor receptor-related (GITR)-Fc fusion protein inhibits GITR triggering and protects from the inflammatory response after spinal cord injury. Mol Pharmacol. 2008;73:1610-21 pubmed publisher
    ..In conclusion, GITR plays a role in SCI, and administration of GITR-Fc results in amelioration of SCI severity, prompting further studies on the potential anti-inflammatory properties of GITR-Fc. ..
  8. Liu Q, Stone J, Bradel Tretheway B, Dabundo J, Benavides Montano J, Santos Montanez J, et al. Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry. PLoS Pathog. 2013;9:e1003770 pubmed publisher
    ..Based on these and recent paramyxovirus findings, we present a comprehensive and fundamentally conserved mechanistic model of paramyxovirus membrane fusion triggering and cell entry. ..
  9. Coonrod E, Karren M, Shaw J. Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion. Traffic. 2007;8:500-11 pubmed
    ..These studies identify PCD2 as a functional domain of Ugo1p and provide the first experimental evidence for a multipass topology of this essential fusion component. ..

More Information


  1. Buzon V, Natrajan G, Schibli D, Campelo F, Kozlov M, Weissenhorn W. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 2010;6:e1000880 pubmed publisher
  2. Grasnick D, Sternberg U, Strandberg E, Wadhwani P, Ulrich A. Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations. Eur Biophys J. 2011;40:529-43 pubmed publisher
    ..Such irregular conformation explains why the structure of the fusion peptide could not be reliably determined by any biophysical method so far. ..
  3. Karan S, Tam B, Moritz O, Baehr W. Targeting of mouse guanylate cyclase 1 (Gucy2e) to Xenopus laevis rod outer segments. Vision Res. 2011;51:2304-11 pubmed publisher
    ..Our results suggest targeting is due to either multiple weak signals in the cytoplasmic domain of GC1, or co-transport to the OS with an accessory protein. ..
  4. Read J, Duncan R. Biophysical and functional assays for viral membrane fusion peptides. Methods. 2011;55:122-6 pubmed publisher
    ..We present details of fluorescence assays used to elucidate the kinetics of membrane fusion as well as complimentary assays used to characterize peptide-induced liposome binding and aggregation. ..
  5. Ellerman D, Myles D, Primakoff P. A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev Cell. 2006;10:831-7 pubmed
    ..Conformational changes mediated by thiol-disulfide exchange are involved in the activation of some virus membrane fusion proteins. Here we asked whether that mechanism is also operative in sperm-egg fusion...
  6. Sutter J, Campanoni P, Tyrrell M, Blatt M. Selective mobility and sensitivity to SNAREs is exhibited by the Arabidopsis KAT1 K+ channel at the plasma membrane. Plant Cell. 2006;18:935-54 pubmed
  7. Moreno M, Giudici M, Villalain J. The membranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein. Biochim Biophys Acta. 2006;1758:111-23 pubmed
  8. Roussel A, Lescar J, Vaney M, Wengler G, Wengler G, Rey F. Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure. 2006;14:75-86 pubmed publisher
    ..These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly...
  9. Neumann S, Langosch D. Conserved conformational dynamics of membrane fusion protein transmembrane domains and flanking regions indicated by sequence statistics. Proteins. 2011;79:2418-27 pubmed publisher
    ..These results suggest evolutionary conservation of key structural features of fusion proteins and are discussed in light of experimental findings that link these features to the fusogenic function of these proteins. ..
  10. Poschner B, Quint S, Hofmann M, Langosch D. Sequence-specific conformational dynamics of model transmembrane domains determines their membrane fusogenic function. J Mol Biol. 2009;386:733-41 pubmed publisher
    ..Their structural and functional analysis suggests that dynamic domains close to the helix termini are more relevant for fusogenicity than central domains but cooperate with the latter to achieve strong fusogenicity. ..
  11. LaPlante J, Falardeau J, Brown E, Slaugenhaupt S, Vassilev P. The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain. Exp Cell Res. 2011;317:691-705 pubmed publisher
    ..MLN1 is absent or mutated in patients with mucolipidosis IV (MLIV), a lysosomal disorder with devastating neurological and other consequences. This study provides potential insight into the pathophysiology of MLIV. ..
  12. Angeletti S, Sanchez J, Chamley L, Genti Raimondi S, Perillo M. StarD7 behaves as a fusogenic protein in model and cell membrane bilayers. Biochim Biophys Acta. 2012;1818:425-33 pubmed publisher
    ..Moreover, this process was favored by phosphatidylethanolamine which is known to stabilize non-lamellar phases considered as intermediary in the fusion process. Altogether these findings allow postulate StarD7 as a fusogenic protein...
  13. Su C, Long F, Lei H, Bolla J, Do S, Rajashankar K, et al. Charged amino acids (R83, E567, D617, E625, R669, and K678) of CusA are required for metal ion transport in the Cus efflux system. J Mol Biol. 2012;422:429-41 pubmed publisher
    ..Genetic analysis and transport assays indicate that charged residues, in addition to the methionine pairs and clusters, are essential for extruding metal ions out of the cell. ..
  14. Suloway C, Chartron J, Zaslaver M, Clemons W. Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc Natl Acad Sci U S A. 2009;106:14849-54 pubmed publisher
    ..Using structural information, we generated mutants to confirm important interfaces and essential residues. These results point to a model of how Get3 couples ATP hydrolysis to the binding and release of TA-proteins. ..
  15. Singh R, Tiwari S, Mishra V, Tiwari R, Dhole T. Molecular epidemiology of Chikungunya virus: mutation in E1 gene region. J Virol Methods. 2012;185:213-20 pubmed publisher
    ..These unique molecular features of the isolates with the continuing epidemic demonstrated high evolutionary potential and thereby indicating higher virulence. ..
  16. Nehme D, Poole K. Interaction of the MexA and MexB components of the MexAB-OprM multidrug efflux system of Pseudomonas aeruginosa: identification of MexA extragenic suppressors of a T578I mutation in MexB. Antimicrob Agents Chemother. 2005;49:4375-8 pubmed
    ..These data confirm the importance of the MexA C-terminal region in MexB binding and the likely significance of the region surrounding T587I of MexB in MexA interaction. ..
  17. Thomas S, Holland I, Schmitt L. The Type 1 secretion pathway - the hemolysin system and beyond. Biochim Biophys Acta. 2014;1843:1629-41 pubmed publisher
    ..This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. ..
  18. Singh V, Wang S, Chan K, Clark S, Kool E. Genetically encoded multispectral labeling of proteins with polyfluorophores on a DNA backbone. J Am Chem Soc. 2013;135:6184-91 pubmed publisher
  19. Vernon S, Bejarano P. Low-grade fibromyxoid sarcoma: a brief review. Arch Pathol Lab Med. 2006;130:1358-60 pubmed
    ..Because of similar clinical behavior and the common cytogenetic abnormality, some authors prefer to consider both lesions as a single entity within the spectrum of low-grade sarcomas. ..
  20. Hoffmann D, Wildner O. Enhanced killing of pancreatic cancer cells by expression of fusogenic membrane glycoproteins in combination with chemotherapy. Mol Cancer Ther. 2006;5:2013-22 pubmed
    ..Qualitatively similar results were obtained in a s.c. pancreatic xenograft model. ..
  21. Akiba M, Lin J, Barton Y, Zhang Q. Interaction of CmeABC and CmeDEF in conferring antimicrobial resistance and maintaining cell viability in Campylobacter jejuni. J Antimicrob Chemother. 2006;57:52-60 pubmed
    ..jejuni. CmeABC is the predominant efflux pump in C. jejuni, whereas CmeDEF plays a secondary role in conferring intrinsic resistance to antimicrobials. ..
  22. Dennison S, Bowen M, Brunger A, Lentz B. Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion. Biophys J. 2006;90:1661-75 pubmed
    ..Thus, it is likely that proteins or factors other than the SNARE complex must trigger fusion in vivo. ..
  23. Basak S, Hao X, Chen A, Chretien M, Basak A. Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein. Protein Pept Lett. 2008;15:874-86 pubmed
    ..Data revealed that HR-C domains (1153-1189), (1153-1172) and (1164-1184) all exhibit potent binding interactions with HR-N(892-931) domain. These peptides may find useful therapeutic applications in SARS intervention. ..
  24. Chanel Vos C, Kielian M. Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein. J Virol. 2006;80:6115-22 pubmed publisher
    ..Together the revertants reveal specific and interconnected aspects of the fusion protein refolding reaction...
  25. Sackett K, Wexler Cohen Y, Shai Y. Characterization of the HIV N-terminal fusion peptide-containing region in context of key gp41 fusion conformations. J Biol Chem. 2006;281:21755-62 pubmed
    ..This study is the first to characterize the FP region in the context of the folded core and provides a basic understanding of the role of the elusive FP for key gp41 fusion conformations. ..
  26. LoPachin R, Barber D, Geohagen B, Gavin T, He D, Das S. Structure-toxicity analysis of type-2 alkenes: in vitro neurotoxicity. Toxicol Sci. 2007;95:136-46 pubmed
    ..This is consistent with our hypothesis that the mechanism of ACR neurotoxicity involves formation of Michael adducts with protein sulfhydryl groups. ..
  27. Tomes C. Molecular mechanisms of membrane fusion during acrosomal exocytosis. Soc Reprod Fertil Suppl. 2007;65:275-91 pubmed
  28. Yang Q, Li G, Singh S, Alexander E, Schwartz J. Vacuolar H+ -ATPase B1 subunit mutations that cause inherited distal renal tubular acidosis affect proton pump assembly and trafficking in inner medullary collecting duct cells. J Am Soc Nephrol. 2006;17:1858-66 pubmed
    ..B1 point mutations prevent normal assembly of the H+ -ATPase and also may act as an inhibitor of H+ -ATPase function by competing with endogenous intact H+ -ATPase for trafficking in inner medullary collecting duct cells...
  29. Gao Y, Bezchlibnyk Y, Sun X, Wang J, McEwen B, Young L. Effects of restraint stress on the expression of proteins involved in synaptic vesicle exocytosis in the hippocampus. Neuroscience. 2006;141:1139-48 pubmed
  30. Maekawa A, Hayase M, Yubisui T, Minami Y. A cDNA cloned from Physarum polycephalum encodes new type of family 3 beta-glucosidase that is a fusion protein containing a calx-beta motif. Int J Biochem Cell Biol. 2006;38:2164-72 pubmed
    ..Thus, the membrane beta-glucosidase is a new type family 3 enzyme fused with the Calx-beta domain. We propose that Calx-beta domain may modulate the beta-glucosidase activity in response to changes in the Ca(2+) concentration. ..
  31. Yamasaki S, Nagasawa S, Hayashi Nishino M, Yamaguchi A, Nishino K. AcrA dependency of the AcrD efflux pump in Salmonella enterica serovar Typhimurium. J Antibiot (Tokyo). 2011;64:433-7 pubmed publisher
    ..Our results indicate that the AcrA MFP and TolC outer membrane protein, in addition to their roles in the AcrB efflux system, are required for the function of the AcrD efflux pump in S. enterica serovar Typhimurium. ..
  32. Andreeva A, Kutuzov M, Voyno Yasenetskaya T. A ubiquitous membrane fusion protein alpha SNAP: a potential therapeutic target for cancer, diabetes and neurological disorders?. Expert Opin Ther Targets. 2006;10:723-33 pubmed
    ..Here, the authors review the evidence available for animal models and for humans, and discuss possible therapeutic approaches that may target alphaSNAP. ..
  33. Jackson M, Chapman E. Fusion pores and fusion machines in Ca2+-triggered exocytosis. Annu Rev Biophys Biomol Struct. 2006;35:135-60 pubmed
    ..We summarize present knowledge of fusion machines and fusion pores studied in vitro, in neurons, and in neuroendocrine cells, and synthesize this knowledge into some specific and detailed hypotheses for exocytosis. ..
  34. Utreras E, Henriquez D, Contreras Vallejos E, Olmos C, Di Genova A, Maass A, et al. Cdk5 regulates Rap1 activity. Neurochem Int. 2013;62:848-53 pubmed publisher
    ..These results suggest that Cdk5-mediated serine-phosphorylation of C3G may control Rap1 stability and activity, and this may potentially impact various neuronal functions such as migration, differentiation, and polarity. ..
  35. Fedry J, Liu Y, Pehau Arnaudet G, Pei J, Li W, Tortorici M, et al. The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein. Cell. 2017;168:904-915.e10 pubmed publisher
    ..studies on the unicellular alga Chlamydomonas reinhardtii HAP2 that reveal homology to class II viral membrane fusion proteins. We further show that targeting the segment corresponding to the fusion loop by mutagenesis or by ..
  36. Castorino J, Deborde S, Deora A, Schreiner R, Gallagher Colombo S, Rodriguez Boulan E, et al. Basolateral sorting signals regulating tissue-specific polarity of heteromeric monocarboxylate transporters in epithelia. Traffic. 2011;12:483-98 pubmed publisher
    ..They introduce a new paradigm for the sorting of heterodimeric transporters in which a hierarchy of apical and BLSS in the catalytic and/or accessory subunits regulates their tissue-specific polarity. ..
  37. Conner M, Conner A, Brown J, Bill R. Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity. Biochemistry. 2010;49:821-3 pubmed publisher
    ..This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization. ..
  38. Pan J, Lai C, Scott W, Straus S. Synthetic fusion peptides of tick-borne encephalitis virus as models for membrane fusion. Biochemistry. 2010;49:287-96 pubmed publisher
    ..It was found that WT, L107F, TFPmn, and TFPtr could penetrate better into the acyl chain region of the lipids than the other peptides tested. The implications of these results on the fusion mechanism of TBEV E protein will be presented. ..
  39. Agrawal P, Kiihne S, Hollander J, Hofmann M, Langosch D, de Groot H. A solid-state NMR study of changes in lipid phase induced by membrane-fusogenic LV-peptides. Biochim Biophys Acta. 2010;1798:202-9 pubmed publisher
    ..The data support the idea that fusogenic peptides accumulate PE in a non-bilayer phase which may be critical for the induction of fusion. ..
  40. Zorzano A, Sebastian D, Segalés J, Palacin M. The molecular machinery of mitochondrial fusion and fission: An opportunity for drug discovery?. Curr Opin Drug Discov Devel. 2009;12:597-606 pubmed
  41. Jackson M, Chapman E. The fusion pores of Ca2+ -triggered exocytosis. Nat Struct Mol Biol. 2008;15:684-9 pubmed publisher
  42. Su C, Yang F, Long F, Reyon D, Routh M, Kuo D, et al. Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol. 2009;393:342-55 pubmed publisher
    ..These findings reveal novel structural features of an MFP in the resistance-nodulation-division efflux system and provide direct evidence that this protein specifically interacts with transported substrates. ..
  43. Bish S, Song W, Stein D. Quantification of bacterial internalization by host cells using a beta-lactamase reporter strain: Neisseria gonorrhoeae invasion into cervical epithelial cells requires bacterial viability. Microbes Infect. 2008;10:1182-91 pubmed publisher
    ..The reporter system that we have developed can be adapted to studying the internalization of any bacterial species into any host cell. ..
  44. Takahashi Y, Nishikawa M, Takakura Y. [Analysis and Control of in Vivo Kinetics of Exosomes for the Development of Exosome-based DDS]. Yakugaku Zasshi. 2016;136:49-53 pubmed publisher
    ..The gradient method is more time-consuming than others; therefore the development of a more efficient method for exosome isolation will advance the development of exosome-based DDS. ..
  45. Liu Q, Han H, Zhang Z, Gao B. [Comparison of two transmemembrane proteins as fusion partner for protein expression on the surface of cell]. Sheng Wu Gong Cheng Xue Bao. 2008;24:1888-94 pubmed
    ..The results indicate that glycosylated deltaLNGFR is a good candidate partner for the expression of a soluble protein on the cell surface. ..
  46. Staron P, Forchhammer K, Maldener I. Structure-function analysis of the ATP-driven glycolipid efflux pump DevBCA reveals complex organization with TolC/HgdD. FEBS Lett. 2014;588:395-400 pubmed publisher
    In Gram-negative bacteria, trans-envelope efflux pumps have periplasmic membrane fusion proteins (MFPs) as essential components. MFPs act as mediators between outer membrane factors (OMFs) and inner membrane factors (IMFs)...
  47. Liu Y, Liu A, Deng P, Wu X, Li T, Liu Y, et al. [Prokaryotic expression of S2 extracellular domain of SARS coronavirus spike protein and its fusion with Hela cell membrane]. Nan Fang Yi Ke Da Xue Xue Bao. 2009;29:381-6 pubmed
  48. Reithinger J, Yim C, Park K, Björkholm P, von Heijne G, Kim H. A short C-terminal tail prevents mis-targeting of hydrophobic mitochondrial membrane proteins to the ER. FEBS Lett. 2013;587:3480-6 pubmed publisher
    ..These results imply that if nuclear-encoded mitochondrial proteins contain strongly hydrophobic transmembrane domains and a long C-terminal tail, they have the potential to be recognized by SRP and mis-targeted to the ER. ..
  49. Cho M, Park D, Lee J, Chi H, Sohn S, Jeon B, et al. Quantitative real-time PCR assay for detection of Paenibacillus polymyxa using membrane-fusion protein-based primers. J Microbiol Biotechnol. 2012;22:1575-9 pubmed
    ..This study reports that the qPCR-based method is applicable for the rapid and sensitive detection of P. polymyxa and can be used as an alternative method for agricultural soil monitoring. ..
  50. Churchward M, Coorssen J. Cholesterol, regulated exocytosis and the physiological fusion machine. Biochem J. 2009;423:1-14 pubmed publisher
  51. Kang M, Shim J, Cho M, Seol Y, Hahn J, Hwang D, et al. Specific detection of Xanthomonas oryzae pv. oryzicola in infected rice plant by use of PCR assay targeting a membrane fusion protein gene. J Microbiol Biotechnol. 2008;18:1492-5 pubmed
    ..sp. dianthi. The results suggested that the assay detected the pathogen more rapidly and accurately than standard isolation methods...
  52. Wagner S, Klepsch M, Schlegel S, Appel A, DRAHEIM R, Tarry M, et al. Tuning Escherichia coli for membrane protein overexpression. Proc Natl Acad Sci U S A. 2008;105:14371-6 pubmed publisher
    ..The generality and simplicity of our approach make it ideal for high-throughput applications. ..
  53. Koschinski A, Wengler G, Wengler G, Repp H. Rare earth ions block the ion pores generated by the class II fusion proteins of alphaviruses and allow analysis of the biological functions of these pores. J Gen Virol. 2005;86:3311-20 pubmed