Molecular mechanisms of cell-cell spread of intracellular bacterial pathogens

Open Biology

Volumn 3, Issue JUL, 2013, Pages

  Ireton, Keith ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

Actin based; Cell junctions; Listeria; Motility; Protrusions; Rickettsia; Shigella

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; BACTERIAL PROTEIN; FETOPROTEIN; FORMIN 1; NUCLEAR PROTEIN;

ACTIN-BASED MOTILITY; CELL JUNCTIONS; HOST PATHOGEN INTERACTION; HUMAN; LISTERIA; METABOLISM; PHYSIOLOGY; PROTRUSIONS; REVIEW; RICKETTSIA; SHIGELLA;

ACTIN-BASED MOTILITY; CELL JUNCTIONS; LISTERIA; PROTRUSIONS; RICKETTSIA; SHIGELLA;

ACTIN-RELATED PROTEIN 2-3 COMPLEX; ACTINS; BACTERIAL PROTEINS; FETAL PROTEINS; HOST-PATHOGEN INTERACTIONS; HUMANS; LISTERIA; MICROFILAMENT PROTEINS; NUCLEAR PROTEINS; RICKETTSIA; SHIGELLA;

EID: 84885613441     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.130079     Document Type: Review

References (180)

1. Gouin E, Welch MD, Cossart P. 2005 Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol. 8, 35-45. (doi:10.1016/j.mib.2004.12.013) (Pubitemid 40203224)
2. Haglund CM, Welch MD. 2011 Pathogens and polymers: microbe-host interactions illuminate the cytoskeleton. J. Cell Biol. 195, 7-17. (doi:10.1083/jcb.201103148)
3. Vazquez-Boland JA, Kuhn M, Berche P, Chakraborty T, Dominguez-Bernal G, Goebel W, Gonzalez-Zorn B, Wehland J, Kreft J. 2001 Listeria pathogenesis and molecular virulence determinants. Clin. Microbiol. Rev. 14, 584-640. (doi:10.1128/CMR.14.3.584-640.2001) (Pubitemid 32642752)
4. Walker DH, Ismail N. 2008 Emerging and reemerging rickettsioses: endothelial cell infection and early disease events. Nat. Rev. Microbiol. 6, 375-386. (doi:10.1038/nrmicro1866) (Pubitemid 351552658)
5. Mavris M, Sansonetti PJ. 2004 Microbial-gut interactions in health and disease: epithelial cell responses. Best Pract. Res. Clin. Gastroenterol. 18, 373-386. (doi:10.1016/j.bpg.2003.10.007) (Pubitemid 38444137)
6. Ray K, Marteyn B, Sansonetti PJ, Tang CM. 2009 Life on the inside: the intracellular lifestyle of cytosolic bacteria. Nat. Rev. Microbiol. 7, 333-340. (doi:10.1038/nrmicro2112)
7. Stavru F, Archambaud C, Cossart P. 2011 Cell biology and immunology of Listeria monocytogenes infections: novel insights. Immunol. Rev. 240, 160-184. (doi:10.1111/j.1600-065X.2010.00993.x)
8. Tilney LG, Portnoy DA. 1989 Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite Listeria monocytogenes. J. Cell Biol. 109, 1597-1608. (doi:10.1083/jcb.109.4.1597)
9. Gaillard JL, Berche P, Frehel C, Gouin E, Cossart P. 1991 Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from Gram-positive cocci. Cell 65, 1127-1141. (doi:10.1016/0092-8674(91)90009-N) (Pubitemid 121001327)
10. Dramsi S, Biswas I, Maguin E, Braun L, Mastroeni P, Cossart P. 1995 Entry of Listeria monocytogenes into hepatocytes requires expression of InIB, a surface protein of the internalin multigene family. Mol. Microbiol. 16, 251-261. (doi:10.1111/j.1365-2958.1995.tb02297.x)
11. Kocks C, Gouin E, Tabouret M, Berche P, Ohayon H, Cossart P. 1992 Listeria monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68, 521-531. (doi:10.1016/0092-8674(92)90188-I)
12. Domann E, Wehland J, Rohde M, Pistor S, Hartl M, Goebel W, Leimeister-Wächter M, Wuenscher M, Chakraborty T. 1992 A novel bacterial gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J. 11, 1981-1990.
13. Welch MD, Iwamatsu A, Mitchison TJ. 1997 Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385, 265-269. (doi:10.1038/385265a0) (Pubitemid 27043727)
14. Mengaud J, Ohayon H, Gounon P, Mege RM, Cossart P. 1996 E-Cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84, 923-932. (doi:10.1016/S0092- 8674(00)81070-3) (Pubitemid 26106861)
15. Shen Y, Naujokas M, Park M, Ireton K. 2000 InlBdependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103, 501-510. (doi:10.1016/S0092-8674(00)00141-0)
16. Ireton K, Payrastre B, Chap H, Ogawa W, Sakaue H, Kasuga M, Cossart P. 1996 A role for phosphoinositide 3-kinase in bacterial invasion. Science 274, 780-782. (doi:10.1126/science.274.5288.780) (Pubitemid 26398257)
17. Sun H, Shen Y, Dokainish H, Holgado-Madruga M, Wong A, Ireton K. 2005 Host adaptor proteins Gab1 and CrkII promote InlB-dependent entry of Listeria monocytogenes. Cell. Microbiol. 7, 443-457. (doi:10.1111/j.1462-5822.2004.00475. x) (Pubitemid 40277923)
18. Veiga E, Cossart P. 2005 Listeria hijacks the clathrindependent endocytic machinery to invade mammalian cells. Nat. Cell Biol. 7, 894-900. (doi:10.1038/ncb1292) (Pubitemid 41486290)
19. Geoffroy C, Gaillard JL, Alouf JE, Berche P. 1987 Purification, characterization and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes. Infect. Immun. 55, 1641-1646. (Pubitemid 17084156)
20. Portnoy DA, Jacks PS, Hinrichs DJ. 1988 Role of hemolysin for the intracellular growth of Listeria monocytogenes. J. Exp. Med. 167, 1459-1471. (doi:10.1084/jem.167.4.1459)
21. Vicente MF, Baquero F, Perez-Diaz C. 1985 Cloning and expression of the Listeria monocytogenes haemolysin in Escherichia coli. FEMS Microbiol. Lett. 30, 77-79. (doi:10.1111/j.1574-6968.1985.tb00988.x) (Pubitemid 16231484)
22. Vazquez-Boland J-A, Kocks C, Dramsi S, Ohayon H, Geoffroy C, Mengaud J, Cossart P. 1992 Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Infect. Immun. 60, 219-230.
23. Camilli A, Goldfine H, Portnoy DA. 1991 Listeria monocytogenes mutants lacking phosphatidylspecific phospholipase C are avirulent. J. Exp. Med. 173, 751-754. (doi:10.1084/jem.173.3.751)
24. Leimeister-Wächter M, Domann E, Chakraborty T. 1991 Detection of a gene encoding a phosphatidylinositol-specific phospholipase C that is coordinately expressed with listeriolysin in Listeria monocytogenes. Mol. Microbiol. 5, 361-366. (doi:10.1111/j.1365-2958.1991.tb02117.x) (Pubitemid 21896054)
25. Mengaud J, Braun-Breton C, Cossart P. 1991 Identification of a phosphatidylinositol-specific phospholipase C in Listeria monocytogenes: a novel type of virulence factor?. Mol. Microbiol. 5, 367-372. (doi:10.1111/j.1365- 2958.1991.tb02118.x) (Pubitemid 21896055)
26. Bernardini ML, Mounier J, D'Hauteville H, Coquis- Rondon M, Sansonetti PJ. 1989 Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin. Proc. Natl Acad. Sci. USA 86, 3867-3871. (doi:10.1073/pnas.86.10.3867) (Pubitemid 19141846)
27. Lett M-C, Sasakawa C, Okada N, Sakai T, Makino S, Yamada M, Komatsu K, Yoshikawa M. 1989 virG, a plasmid-coded virulence gene of Shigella flexneri: Identification of the virG protein and determination of the complete coding sequence. J. Bacteriol. 171, 353-359. (Pubitemid 19031408)
28. Suzuki T, Miki H, Takenawa T, Sasakawa C. 1998 Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 17, 2767-2776. (doi:10.1093/emboj/17.10.2767) (Pubitemid 28227123)
29. Pal T, Newland JW, Tall BD, Formal SB, Hale TL. 1989 Intracellular spread of Shigella flexneri associated with the kcpA locus and a 140-kilodalton protein. Infect. Immun. 57, 477-486. (Pubitemid 19046370)
30. Makino S, Sasakawa C, Kamata K, Kurata T, Yoshikawa M. 1986 A genetic determinant required for continuous reinfection of adjacent cells on large plasmid in S. flexneri 2a. Cell 46, 551-555. (doi:10.1016/0092-8674(86)90880-9)
31. High N, Mounier J, Prévost MC, Sansonetti PJ. 1992 IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole. EMBO J. 11, 1991-1999.
32. Menard R, Sansonetti PJ, Parsot C. 1993 Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J. Bacteriol. 175, 5899-5906. (Pubitemid 23277438)
33. Sasakawa C, Makino S, Kamata K, Yoshikawa M. 1986 Isolation, characterization, and mapping of Tn5 insertions into the 140-megadalton invasion plasmid defective in the mouse Sereny test in Shigella flexneri 2a. Infect. Immun. 54, 32-36. (Pubitemid 16021209)
34. Chan YGY, Riley SP, Martinez JJ. 2010 Adherence to and invasion of host cells by spotted fever group Rickettsia species. Front. Microbiol. 1, 139. (doi:10.3389/fmicb.2010.00139)
35. Haglund CM, Choe JE, Skau CT, Kovar DR, Welch MD. 2010 Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility. Nat. Cell Biol. 12, 1057-1063. (doi:10.1038/ncb2109)
36. Kleba B, Clark TR, Lutter EI, Ellison DW, Hackstadt T. 2010 Disruption of the Rickettsia rickettsii Sca2 autotransporter inhibits actin-based motility. Infect. Immun. 78, 2240-2247. (doi:10.1128/IAI.00100-10)
37. Gouin E, Egile C, Dehoux P, Villiers V, Adams J, Gertler FB, Li R, Cossart P. 2004 The RickA protein of Rickettsia conorii activates the Arp2/3 complex. Nature 427, 29. (doi:10.1038/nature02318) (Pubitemid 38168500)
38. Jeng RL, Goley ED, D'Alession JA, Chaga OY, Svitkina TM, Borisy GG, Heinzen RA, Welch MD. 2004 A Rickettsia WASP-like protein activates the Arp2/3 complex and mediates actin-based motility. Cell. Microbiol. 6, 761-769. (doi:10.1111/j.1462-5822.2004.00402.x) (Pubitemid 39077382)
39. Martinez JJ, Seveau S, Veiga E, Matsuyama S, Cossart P. 2005 Ku70, a component of DNAdependent protein kinase, is a mammalian receptor for Rickettsia conorii. Cell 123, 1013-1023. (doi:10.1016/j.cell.2005.08.046) (Pubitemid 41785417)
40. Chan YG, Cardwell MM, Hermanas TM, Uchiyama T, Martinez JJ. 2009 Rickettsial outer-membrane protein B (rOmpB) mediates bacterial invasion through Ku70 in an actin, c-Cbl, clathrin and caveolin 2-dependent manner. Cell. Microbiol. 11, 629-644. (doi:10.1111/j.1462-5822.2008.01279.x)
41. Riley SP, Goh KC, Hermanas TM, Cardwell MM, Chan YG, Martinez JJ. 2010 The Rickettsia conorii autotransporter protein Sca1 promotes adherence to nonphagocytic mammalian cells. Infect. Immun. 78, 1895-1904. (doi:10.1128/IAI.01165-09)
42. Cardwell MM, Martinez JJ. 2009 The Sca2 autotransporter protein from Rickettsia conorii is sufficient to mediate adherence to and invasion of cultured mammalian cells. Infect. Immun. 77, 5272-5280. (doi:10.1128/IAI.01165- 09)
43. Monack DM, Theriot JA. 2001 Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake. Cell. Microbiol. 3, 633-647. (doi:10.1046/j.1462-5822.2001.00143.x) (Pubitemid 32851173)
44. Pust S, Morrison H, Wehland J, Sechi AS, Herrlich P. 2005 Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell. EMBO. J. 24, 1287-1300. (doi:10.1038/sj.emboj.7600595) (Pubitemid 40516611)
45. Rajabian T, Gavicherla B, Heisig M, Muller-Altrock S, Goebel W, Gray-Owen SD, Ireton K. 2009 The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria. Nat. Cell Biol. 11, 1212-1218. (doi:10.1038/ncb1964)
46. Bishai EA, Sidhu GS, Li W, Dhillon J, Bohil AB, Cheney RE, Hartwig JH, Southwick FS. 2013 Myosin- X facilitates Shigella-induced membrane protrusions and cell-to-cell spread. Cell. Microbiol. 15, 353-367. (doi:10.1111/cmi.12051)
47. Chong R, Squires R, Swiss R, Agaisse H. 2011 RNAi screen reveals host cell kinases specifically involved in Listeria monocytogenes spread from cell to cell. PLoS ONE 6, e23399. (doi:10.1371/journal.pone.0023399)
48. Fukumatsu M, Ogawa MFA, Suzuki M, Nakayama K, Shimizu S, Kim M, Mimuro H, Sasakawa C. 2012 Shigella targets epithelial tricellular junctions and uses a noncanonical clathrin-dependent endocytic pathway to spread between cells. Cell Host Microbe 11, 325-336. (doi:10.1016/j.chom.2012.03.001)
49. Ogawa M, Handa Y, Ashida H, Suzuki M, Sasakawa C. 2008 The versatility of Shigella effectors. Nat. Rev. Microbiol. 6, 11-16. (doi:10.1038/nrmicro1814) (Pubitemid 350286216)
50. Campellone KG, Welch MD. 2010 A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11, 237-251. (doi:10.1038/nrm2867)
51. Goldberg MB. 2001 Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65, 595-626. (doi:10.1128/MMBR.65.4. 595-626.2001) (Pubitemid 33123519)
52. Firat-Karalar EN, Welch MD. 2011 New mechanisms and functions and actin nucleation. Curr. Opin. Cell Biol. 23, 4-13. (doi:10.1016/j.ceb.2010.10.007)
53. Chesarone MA, DuPage AG, Goode BL. 2010 Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat. Rev. Mol. Cell Biol. 11, 62-74. (doi:10.1038/nrm2816)
54. Dominguez R, Holmes KC. 2011 Actin structure and function. Ann. Rev. Biophys. 40, 169-186. (doi:10.1146/annurev-biophys-042910-155359)
55. Goldschmidt-Clermont PJ, Machesky LM, Doberstein SK, Pollard TD. 1991 Mechanism of the interaction of human platelet profilin with actin. J. Cell Biol. 113, 1081-1089. (doi:10.1083/jcb.113.5.1081) (Pubitemid 21909740)
56. Pantaloni D, Carlier MF. 1993 How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell 75, 1007-1014. (doi:10.1016/0092-8674(93)90544-Z) (Pubitemid 24014557)
57. Suetsugu S, Gautreau A. 2012 Synergistic BAR-NPF interactions in actin-driven membrane remodeling. Trends Cell Biol. 22, 141-150. (doi:10.1016/j.tcb.2012.01.001)
58. Nightingale TD, Cutler DF, Cramer LP. 2012 Actin coats and rings promote regulated exocytosis. Trends Cell Biol. 22, 329-337. (doi:10.1016/j.tcb.2012.03. 003)
59. Scott CC, Dobson W, Botelho RJ, Coady-Osberg N, Chavrier P, Knecht DA, Heath C, Stahl P, Grinstein S. 2005 Phosphatidylinositol-4,5-bisphosphate hydrolysis directs actin remodeling during phagocytosis. J. Cell Biol. 11, 139-149. (doi:10.1083/jcb.200412162) (Pubitemid 40562921)
60. Welch MD, Rosenblatt J, Skoble J, Portnoy DA, Mitchison TJ. 1998 Interaction of human Arp2/3 complex and Listeria monocytogenes ActA protein in actin filament elongation. Science 281, 105-108. (doi:10.1126/science.281.5373. 105) (Pubitemid 28354054)
61. Sagot I, Rodal AA, Moseley J, Goode BL, Pellman D. 2002 An actin nucleation mechanism mediated by Bni1 and profilin. Nat. Cell Biol. 4, 626-631. (doi:10.1038/ncb83)
62. Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, Bretscher A, Boone C. 2002 Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612-615. (doi:10.1126/science.1072309) (Pubitemid 34815347)
63. Quinlan ME, Heuser JE, Kerkhoff E, Mullins RD. 2005 Drosophila Spire is an actin nucleation factor. Nature 433, 382-388. (doi:10.1038/nature03241)
64. Ahuja R, Pinyol R, Reichenbach N, Custer L, Klingensmith J, Kessels MM, Qualmann B. 2007 Cordon-bleu is an actin nucleation factor and controls neuronal morphology. Cell 131, 337-350. (doi:10.1016/j.cell.2007.08.030) (Pubitemid 47592919)
65. Chereau D, Boczkowska M, Skwarek-Maruszewska A, Fujiwara I, Hayes DB, Rebowski G, Lappalainen P, Pollard TD, Dominguez R. 2008 Leiomodin is an actin filament nucleator in muscle cells. Science 320, 239-243. (doi:10.1126/science. 1155313) (Pubitemid 351521421)
66. Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD. 1994 Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 127, 107-115. (doi:10.1083/jcb.127.1.107) (Pubitemid 24307660)
67. Lees-Miller JP, Henry G, Helfman DM. 1992 Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin. Proc. Natl Acad. Sci. USA 89, 80-83. (doi:10.1073/pnas.89.1.80)
68. Schwob E, Martin RP. 1992 New yeast actin-like gene required late in the cell cycle. Nature 355, 179-182. (doi:10.1038/355179a0)
69. Fyrberg C, Fyrberg E. 1993 A Drosophila homologue of the Schizosaccharomyces pombe act2 gene. Biochem. Genet. 31, 329-341. (doi:10.1007/BF00553175) (Pubitemid 23316954)
70. Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ. 1997 The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filaments assembly. J. Cell. Biol. 138, 375-384. (doi:10.1083/jcb.138.2.375) (Pubitemid 27323539)
71. Waterston R et al. 1992 A survey of expressed genes in Caenorhabditis elegans. Nat. Genet. 1, 114-123. (doi:10.1038/ng0592-114)
72. Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD. 2001 Crystal structure of Arp2/3 complex. Science 294, 1679-1684. (doi:10.1126/science.1066333) (Pubitemid 33104831)
73. Mullins RD, Heuser JE, Pollard TD. 1998 interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of actin filaments. Proc. Natl Acad. Sci. USA 95, 6181-6186. (doi:10.1073/pnas.95.11.6181) (Pubitemid 28248985)
74. Amann K, Pollard TD. 2001 Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc. Natl Acad. Sci. USA 98, 15 009-15 013. (doi:10.1073/pnas.211556398) (Pubitemid 34013960)
75. Rouiller I et al. 2008 The structural basis of actin filament branching by the Arp2/3 complex. J. Cell Biol. 180, 887-895. (doi:10.1083/jcb.200709092) (Pubitemid 351398416)
76. Beltzner CC, Pollard TD. 2004 Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species. J. Mol. Biol. 226, 551-565. (doi:10.1016/j.jmb.2003.12.017) (Pubitemid 38147646)
77. Machesky LM, Mullins RD, Higgs HN, Kaiser DA, Blanchoin L, May RC, Hall ME, Pollard TD. 1999 Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Curr. Biol. 96, 3739-3744. (doi:10.1073/pnas.96.7.3739) (Pubitemid 29168980)
78. Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T, Takenawa T, Kirschner MW. 1999 The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231. (doi:10.1016/S0092-8674(00)80732-1)
79. Yarar D, To W, Abo A, Welch MD. 1999 The Wiskott-Aldrich syndrome protein directs actinbased motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9, 555-558. (doi:10.1016/S0960-9822(99)80243-7) (Pubitemid 29257114)
80. Derivery E, Gautreau A. 2010 Generation of branched actin networks: assembly and regulation of the N-WASP and WAVE molecular machines. BioEssays 32, 119-131. (doi:10.1002/bies.200900123)
81. Goley ED, Rodenbusch SE, Martin AC, Welch MD. 2004 Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor. Mol. Cell. 22, 269-279. (doi:10.1016/j.molcel.2004. 09.018) (Pubitemid 39388841)
82. Zencheck WD, Xiao H, Nolen BJ, Angeletti RH, Pollard TD, Almo SC. 2009 Nucleotide- and activator-dependent structural and dynamic changes of arp2/3 complex monitored by hydrogen/ deuterium exchange and mass spectrometry. J. Mol. Biol. 390, 414-427. (doi:10.1016/j.jmb.2009.03.028)
83. Rodal AA, Sokolova O, Robins DB, Daugherty KM, Hippenmeyer S, Riezman H, Grigorieff N, Goode BL. 2005 Conformational changes in the Arp2/3 complex leading to actin nucleation. Nat. Struct. Mol. Biol. 12, 26-31. (doi:10.1038/nsmb870) (Pubitemid 40082913)
84. Kreishman-Deitrick M et al. 2005 NMR analyses of the activation of the Arp2/3 complex by neuronal Wiskott-Aldrich syndrome protein. Biochemistry 44, 15 247-15 256. (doi:10.1021/bi051065n) (Pubitemid 41681459)
85. Kelly AE, Kranitz H, Dotsch V, Mullins RD. 2006 Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex. J. Biol. Chem. 281, 10 589- 10 597. (doi:10.1074/jbc. M507470200) (Pubitemid 43864601)
86. Chereau D, Kerff F, Graceffa P, Grabarek Z, Langsetmo K, Dominguez R. 2005 Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl Acad. Sci. USA 102, 16 644-16 649. (doi:10.1073/pnas.0507021102) (Pubitemid 41688830)
87. Miki H, Sasaki T, Taka Y, Takenawa T. 1998 Induction of filopodium formation by a WASP-related actindepolymerrizing protein N-WASP. Nature 391, 93-96. (doi:10.1038/34208) (Pubitemid 28079222)
88. Anton IM, Jones GE, Wandosell F, Geha R, Ramesh N. 2007 WASP-interacting protein (WIP): working in polymerisation and much more. Trends. Cell. Biol. 11, 555-562. (doi:10.1016/j.tcb.2007.08.005) (Pubitemid 350087660)
89. Rohatgi R, Ho HY, Kirschner MW. 2000 Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J. Cell Biol. 150, 1299-1310. (doi:10.1083/jcb.150.6.1299)
90. Prehoda KE, Scott JA, Mullins RD, Lim WA. 2000 Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290, 801-806. (doi:10.1126/science.290.5492.80)
91. Higgs HN, Pollard TD. 2000 Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150, 1311-1320. (doi:10.1083/jcb.150.6.1311)
92. Carlier MF et al. 2000 GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex. J. Biol. Chem. 275, 21 946-21 952. (doi:10.1074/jbc.M000687200) (Pubitemid 30621767)
93. Rohatgi R, Nollau P, Ho HY. 2001 Nck and phosphatidylinositol4,5- bisphosphate synergistically activate actin polymerization through the N-WASPArp2/ 3 pathway. J. Biol. Chem. 276, 26 448- 26 452. (doi:10.1074/jbc. M103856200) (Pubitemid 37412864)
94. Ho HY, Rohatgi R, Lebensohn AM, Le M, Li J, Gygi SP, Kirschner MW. 2004 Toca-1 mediates Cdc42- dependent actin nucleation by activating the NWASP- WIP complex. Cell 118, 203-216. (doi:10.1016/j.cell.2004.06.027) (Pubitemid 38962576)
95. Cory GO, Cramer R, Blanchoin L, Ridley AJ. 2003 Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol. Cell 11, 1229-1239. (doi:10.1016/S1097-2765(03) 00172-2) (Pubitemid 36645142)
96. Moseley JB, Sagot I, Manning AL, Xu X, Eck MJ, Pellman D, Goode BL. 2004 A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol. Biol. Cell 15, 896-907. (doi:10.1091/mbc.E03-08-0621) (Pubitemid 38146502)
97. Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, Goode BL, Eck MJ. 2004 Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723. (doi:10.1016/S0092-8674(04)00210-7) (Pubitemid 38326729)
98. Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK. 2005 Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494. (doi:10.1038/nature03251) (Pubitemid 40204299)
99. Pring M, Evangelista M, Boone C, Yang C, Zigmond SH. 2003 Mechanism of formin-induced nucleation of actin filaments. Biochemistry 42, 486-496. (doi:10.1021/bi026520j) (Pubitemid 36105767)
100. Zigmond SH, Evangelista M, Boone C, Yang C, Dar AC, Sicheri F, Forkey J, Pring M. 2003 Formin leaky cap allows elongation in the presence of tight capping proteins. Curr. Biol. 13, 1820-1823. (doi:10.1016/j.cub.2003.09.057) (Pubitemid 37269124)
101. Kovar DR, Pollard TD. 2004 Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl Acad. Sci. USA 101, 14 725-14 730. (doi:10.1073/pnas.0405902101) (Pubitemid 39410742)
102. Romero S, Le Clainche C, Didry D, Egile C, Pantaloni D, Carlier MF. 2004 Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429. (doi:10.1016/j.cell.2004.09. 039) (Pubitemid 39423843)
103. Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD. 2006 Control of the assembly of ATP- and ADPactin by formins and profilin. Cell 124, 423-435. (doi:10.1016/j.cell.2005.11.038,) (Pubitemid 43121988)
104. Higgs HN, Peterson KJ. 2005 Phylogenetic analysis of the formin homology 2 domain. Mol. Biol. Cell. 16, 1-13. (doi:10.1091/mbc.E04-07-0565) (Pubitemid 40024285)
105. Li F, Higgs HN. 2003 The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13, 1335-1340. (doi:10.1016/S0960-9822(03)00540-2) (Pubitemid 36953308)
106. Li F, Higgs HN. 2005 Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1. J. Biol. Chem. 280, 6986-6992. (doi:10.1074/jbc.M411605200) (Pubitemid 40341254)
107. Peng J, Wallar BJ, Flanders A, Swiatek PJ, Alberts As. 2003 Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr. Biol. 13, 534-545. (doi:10.1016/S0960-9822(03) 00170-2) (Pubitemid 36391930)
108. Lammers M, Meyer S, Kuhlmann D, Wittenghofer A. 2008 Specificity of interactions between mDia isoforms and Rho proteins. J. Biol. Chem. 283, 35 236-35 246. (doi:10.1074/jbc.M805634200)
109. Lammers M, Rose R, Scrima A, Wittenghofer A. 2005 The regulation of mDia1 by autoinhibition and its release by Rho-GTP. EMBO J. 24, 4176-4187. (doi:10.1038/sj.emboj.7600879) (Pubitemid 41752886)
110. Posfay-Barbe KM, Wald ER. 2009 Listeriosis. Semin. Fetal Neonatal. Med. 14, 228-233. (doi:10.1016/j.siny.2009.01.006)
111. Brundage RA, Smith GA, Camilli A, Theriot JA, Portnoy DA. 1993 Expression and phosphorylation of the Listeria monocytogenes ActA protein in mammalian cells. Proc. Natl Acad. Sci. USA 90, 11 890-11 894. (doi:10.1073/pnas.90.24. 11890) (Pubitemid 24008745)
112. Leung N, Gianfelice A, Gray-Owen SD, Ireton K. 2013 Impact of the Listeria monocytogenes protein InlC on infection in mice. Infect. Immun. 81, 1334-1340. (doi:10.1128/IAI.01377-12)
113. Bakardjiev AL, Stacy BA, Fisher SJ, Portnoy DA. 2004 Listeriosis in the pregnant guinea pig: a model for vertical transmission. Infect. Immun. 72, 489-497. (doi:10.1128/IAI.72.1.489-497.2004) (Pubitemid 38018210)
114. Racz P, Tenner K, Mérö E. 1972 Experimental Listeria enteritis. I. An electron microscopic study of the epithelial phase in experimental Listeria infection. Lab Invest. 26, 694-700.
115. Marco AJ, Altimira J, Prats N, Lopez S, Dominguez L, Domingo M, Briones V. 1997 Penetration of Listeria monocytogenes in mice infected by the oral route. Microb. Pathog. 23, 255-263. (doi:10.1006/mpat.1997.0144) (Pubitemid 28020673)
116. Bakardjiev AI, Stacy BA, Portnoy DA. 2005 Growth of Listeria monocytogenes in the guinea pig placenta and role of cell-to-cell spread in fetal infection. J. Infect. Dis. 191, 1889-1897. (doi:10.1086/430090) (Pubitemid 40705397)
117. LeMonnier A, Autret N, Join-Lambert OF, Jaubert F, Charbit A, Berche P, Kayal S. 2007 ActA is required for crossing of the fetoplacental barrier by Listeria monocytogenes. Infect. Immun. 75, 950-957. (doi:10.1128/IAI.01570-06) (Pubitemid 46203460)
118. Theriot JA, Mitchison TJ, Tilney LG, Portnoy DA. 1992 The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 357, 257-260. (doi:10.1038/357257a0)
119. Zalevsky J, Grigorova I, Mullins RD. 2001 Activation of the Arp2/3 complex by the Listeria ActA protein. ActA binds two actin monomers and three subunits of the Arp2/3 complex. J. Biol. Chem. 276, 3468-3475. (doi:10.1074/jbc.M006407200)
120. Cicchetti G, Maurer P, Wagener P, Kocks C. 1999 Actin and phosphoinositide binding by the ActA protein of the bacterial pathogen Listeria monocytogenes. J. Biol. Chem. 274, 33 616-33 626. (doi:10.1074/jbc.274.47.33616) (Pubitemid 129511674)
121. Lauer P, Theriot JA, Skoble J, Welch MD, Portnoy DA. 2001 Systematic mutational analysis of the amino-terminal domain of the Listeria monocytogenes ActA protein reveals novel functions in actin-based motility. Mol. Microbiol. 42, 1163-1177. (doi:10.1046/j.1365-2958.2001.02677.x) (Pubitemid 34209079)
122. Chakraborty T et al. 1995 A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actinbased cytoskeleton of mammalian cells. EMBO J. 14, 1314-1321.
123. Gertler FB, Niebuhr K, Reinhard M, Wehland J, Soriano P. 1996 Mena, a relative of VASP and Drosophila enabled, is implicated in the control of microfilament dynamics. Cell 87, 227-239. (doi:10.1016/S0092-8674(00)81341-0) (Pubitemid 26359001)
124. Niebuhr K et al. 1997 A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J. 16, 5433-5444. (doi:10.1093/emboj/16.17.5433) (Pubitemid 27380150)
125. Pistor S, Chakraborty T, Walter U, Wehland J. 1995 The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Curr. Biol. 5, 517-525. (doi:10.1016/S0960- 9822(95)00104-7)
126. Smith GA, Theriot J, Portnoy D. 1996 The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator- stimulated phosphoprotein and profilin. J. Cell Biol. 135, 647-660. (doi:10.1083/jcb.135.3.647) (Pubitemid 26372922)
127. Reinhard M, Giel K, Abel K, Haffner C, Jarchau T, Hoppe V, Jockusch BM, Walter U. 1995 The prolinerich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 14, 1583-1589.
128. Machesky LM, Install RH. 1998 Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356. (doi:10.1016/S0960-9822(98)00015-3) (Pubitemid 29020143)
129. Winter D, Lechler T, Li R. 1999 Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9, 501-505. (doi:10.1016/S0960- 9822(99)80218-8) (Pubitemid 29228625)
130. Chong R, Swiss R, Briones G, Stone KL, Gulcicek EE, Agaisse H. 2009 Regulatory mimicry in Listeria monocytogenes actin-based motility. Cell Host Microbe 6, 268-278. (doi:10.1016/j.chom.2009.08.006)
131. Stebbins CE, Galan JE. 2001 Structural mimicry in bacterial virulence. Nature 412, 701-705. (doi:10.1038/35089000) (Pubitemid 32771986)
132. Ogawa H, Nakamura A, Nakaya R. 1968 Cinemicrographic study of tissue cell cultures infected with Shigella flexneri. Jpn J. Med. Sci. Biol. 21, 259-273.
133. Sansonetti PJ, Arondel J, Fontaine A, d'Hauteville H, Bernardini ML. 1991 OmpB (osmo-regulation) and icsA (cell-to-cell spread) mutants of Shigella flexneri: vaccine candidates and probes to study the pathogenesis of shigellosis. Vaccine 9, 416-422. (doi:10.1016/0264-410X(91)90128-S)
134. Egile C, Loisel TP, Laurent V, Li R, Pantaloni D, Sansonetti PJ, Carlier MF. 1999 Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146, 1319-1332. (doi:10.1083/jcb.146.6.1319) (Pubitemid 29477698)
135. Lommel S, Benesch S, Rottner K, Franz K, Wehland J, Kuhn R. 2001 Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2, 850-857. (doi:10.1093/embo-reports/kve197) (Pubitemid 32982755)
136. Snapper SB et al. 2001 N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility. Nat. Cell Biol. 3, 897-904. (doi:10.1038/ncb1001-897) (Pubitemid 32952254)
137. Mounier J, Laurent V, Hall A, Fort P, Carlier MF, Sansonetti PJ, Egile C. 1999 Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. J. Cell Sci. 112, 2069-2080. (Pubitemid 29355422)
138. Shibata T, Takeshima F, Chen F, Alt FW, Snapper SB. 2002 Cdc42 facilitates invasion but not the actinbased motility of Shigella. Curr. Biol. 12, 341-345. (doi:10.1016/S0960-9822(02)00689-9) (Pubitemid 34161481)
139. Moreau V, Frischknect F, Reckmann I, Vincentelli R, Rabut G, Stewart D, Way M. 2000 A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat. Cell Biol. 2, 441-448. (doi:10.1038/35017080)
140. Leung Y, Ally S, Goldberg MB. 2008 Bacterial actin assembly requires toca-1 to relieve N-Wasp autoinhibition. Cell Host Microbe 3, 39-47. (doi:10.1016/j.chom.2007.10.011)
141. Gouin E, Gantelet H, Egile C, Lasa I, Ohayon H, Villiers V, Gounon P, Sansonetti PJ, Cossart P. 1999 A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. J. Cell. Sci. 112, 1697-1708. (Pubitemid 29295046)
142. Harlander RS, Way M, Ren Q, Howe D, Grieshaber SS, Heinzen RA. 2003 Effects of ectopically expressed neuronal Wiskott-Aldrich syndrome protein domains on Rickettsia rickettsii actin-based motility. Infect. Immun. 71, 1551-1556. (doi:10.1128/IAI.71.3.1551-1556.2003) (Pubitemid 36254344)
143. Serio AW, Jeng RL, Haglund CM, Reed LJ, Welch MD. 2010 Defining a core set of actin cytoskeletal proteins critical for actin-based motility. Cell Host Microbe 7, 388-398. (doi:10.1016/j.chom.2010.04.008)
144. Engelbrecht F, Chun S-K, Ochs C, Hess J, Lottspeich F, Goebel W, Sokolovic Z. 1996 A new PrfAregulated gene of Listeria monocytogenes encoding a small, secred protein which belongs to the family of internalins. Mol. Microbiol. 21, 823-837. (doi:10.1046/j.1365-2958.1996.541414.x) (Pubitemid 26281529)
145. Otani T, Ichii T, Aono S, Takeichi M. 2006 Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells. J. Cell. Biol. 175, 135-146. (doi:10.1083/jcb.200605012) (Pubitemid 44537205)
146. Ivanov AI, Nusrat A, Parkos CA. 2005 Endocytosis of the apical junctional complex: mechanisms and possible roles in regulation of epithelial barriers. Bioessays 27, 356-365. (doi:10.1002/bies.20203) (Pubitemid 40592592)
147. Miyoshi J, Takai Y. 2005 Molecular perspective on tight-junction assembly and epithelial polarity. Adv. Drug. Deliv. Rev. 57, 815-855. (doi:10.1016/j.addr.2005.01.008) (Pubitemid 40488106)
148. Fehon RG, McClatchey AI, Bretscher A. 2010 Organizing the cell cortex: the role of ERM proteins. Nat. Rev. Mol. Cell Biol. 11, 276-287. (doi:10.1038/nrm2866)
149. Turenen O, Wahlstrom T, Vaheri A. 1994 Ezrin had a COOH-terminal actin binding site that is conserved in the ezrin protein family. J. Cell Biol. 126, 1445-1453. (doi:10.1083/jcb.126.6.1445) (Pubitemid 24284609)
150. Gary R, Bretscher A. 1995 Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol. Biol. Cell. 6, 1061-1075.
151. Reczek D, Berryman M, Bretscher A. 1997 Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J. Cell Biol. 139, 169-179. (doi:10.1083/jcb.139.1. 169) (Pubitemid 27444089)
152. Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S. 1998 Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J. Cell Biol. 140, 885-895. (doi:10.1083/jcb.140.4.885) (Pubitemid 28141226)
153. Nakamura F, Amieva MR, Furhmayr H. 1995 Phosphorylation of threonine 558 in the carboxylterminal actin-binding domain of moesin by thrombin activation of human platelets. J. Biol. Chem. 270, 31 377-31 385. (doi:10.1074/jbc.270.20. 12319) (Pubitemid 26012231)
154. Yonemura S, Matsui T, Tsukita S. 2002 Rhodependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. J. Cell Sci. 115, 2569-2580. (Pubitemid 34778074)
155. Fievet BT, Gautreau A, Roy C, Del Maestro L, Mangeat P, Louvard D, Arpin M. 2004 Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin. J. Cell Biol. 164, 653-659. (doi:10.1083/jcb. 200307032) (Pubitemid 38282949)
156. Sechi AS, Wehland J, Small JV. 1997 The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random. J. Cell. Biol. 137, 155-167. (doi:10.1083/jcb.137.1. 155) (Pubitemid 27167303)
157. Romero S, Van Nhieu GTV. 2009 A bacterial virulence factor that dissipates tension. Nat. Cell Biol. 11, 1174-1175. (doi:10.1038/ncb1009-1174)
158. Heindl JE, Saran I, Yi Cr, Lesser CF, Goldberg MB. 2010 Requirement for formin-induced actin polymerization during spread of Shigella flexneri. Infect. Immun. 78, 193-203. (doi:10.1128/IAI.00252-09)
159. Cheney RE, Sousa AD. 2005 Myosin-10: a molecular motor at the cell's fingertips. Trends Cell Biol. 15, 533-539. (doi:10.1016/j.tcb.2005.08.006) (Pubitemid 41396435)
160. Sansonetti PJ, Mournier J, Prevost MC, Mege RM. 1994 Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell 76, 829-839. (doi:10.1016/0092-8674(94)90358-1) (Pubitemid 24085321)
161. Robbins JR, Barth AI, Marquis H, de Hostos EI, Nelson WJ, Theriot JA. 1999 Listeria monocytogenes exploits normal host cell processes to spread from cell to cell. J. Cell. Biol. 146, 1333-1350. (doi:10.1083/jcb.146.6.1333) (Pubitemid 29477699)
162. Tran Van Nhieu G, Clair C, Bruzzone R, Mesnil M, Sansonetti PJ, Combettes L. 2003 Connexindependent inter-cellular communication increases invasion and dissemination of Shigella in epithelial cells. Nat. Cell Biol. 5, 720-726. (doi:10.1038/ncb1021) (Pubitemid 36986779)
163. Mariano C, Sasaki H, Brites D, Brito MA. 2011 A look at tricellulin and its role in tight junction formation and maintenance. Eur. J. Immunol. 90, 787-796. (doi:10.1016/j.ejcb.2011.06.005)
164. Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S, Tsukita S. 2005 Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J. Cell Biol. 171, 939-945. (doi:10.1083/jcb.200510043) (Pubitemid 41815826)
165. Loisel TP, Boujemaa R, Pantaloni D, Carlier M-F. 1999 Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401, 613-616. (doi:10.1083/jcb.144.6.1245) (Pubitemid 29157302)
166. Gomez GA, McLachlan RW, Yap AS. 2011 Productive tension: force-sensing and homeostasis of cell-cell junctions. Trends Cell Biol. 21, 499-505. (doi:10.1016/j.tcb.2011.05.006)
167. Luna A, Matas OB, Martinez-Menarguez JA, Mato E, Duran JM, Ballesta J, Way M, Egea G. 2002 Regulation of protein transport from the Golgi complex to the endoplasmic reticulum by CDC42 and N-WASP. Mol. Biol. Cell. 13, 866-879. (doi:10.1091/mbc.01-12-0579) (Pubitemid 34250352)
168. Matas OB, Martinez-Menarguez JA, Egea G. 2004 Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes. Traffic 5, 838-846. (doi:10.1111/j.1600-0854.2004.00225.x) (Pubitemid 39433554)
169. Harris K, Tepass U. 2010 Cdc42 and vesicle trafficking in polarized cells. Traffic 11, 1272-1279. (doi:10.1111/j.1600-0854.2010.01102.x)
170. Salazar MA et al. 2003 Tuba, a novel protein containing Bin/Amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton. J. Biol. Chem. 278, 49 031-49 043. (doi:10.1074/jbc. M308104200)
171. Kodani A, Kristensen I, Huang L, Sutterlin C. 2009 GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization. Mol. Biol. Cell. 20, 1192-1200. (doi:10.1091/mbc.E08-08-0834)
172. Mim C, Unger VM. 2012 Membrane curvature and its generation by BAR proteins. Trends Biochem. Sci. 37, 526-533. (doi:10.1016/j.tibs.2012.09.001)
173. Yap AS, Crampton MS, Hardin J. 2007 Making and breaking contacts: the cellular biology of cadherin regulation. Curr. Opin. Cell Biol. 19, 508-514. (doi:10.1016/j.ceb.2007.09.008) (Pubitemid 350016859)
174. Wirtz-Peitz F, Zallen JA. 2009 Junctional trafficking and epithelial morphogenesis. Curr. Opin. Genet. Dev. 19, 350-356. (doi:10.1016/j.gde.2009.04. 011)
175. de Beco S, Gueudry C, Amblard F, Coscoy S. 2009 Endocytosis is required for E-cadherin redistribution at mature adherens junctions. Proc. Natl Acad. Sci. USA 106, 7010-7015. (doi:10.1073/pnas.0811253106)
176. Nejsum LN, Nelson WJ. 2009 Epithelial cell surface polarity: the early steps. Front. Biosci. 14, 1088-1098. (doi:10.2741/3295)
177. Guo W, He B. 2009 The exocyst complex in polarized exocytosis. Curr. Opin. Cell Biol. 21, 537-542. (doi:10.1016/j.ceb.2009.04.007)
178. Schmid SL, Frolov VA. 2011 Dynamin: functional design of a membrane fission catalyst. Annu. Rev. Cell. Dev. Biol. 27, 79-105. (doi:10.1146/ annurevcellbio-100109-104016)
179. McCullough J, Colf LA, Sundquist WI. 2013 Membrane fission reactions of the mammalian ESCRT pathway. Annu. Rev. Biochem. 82, 663-692. (doi:10.1146/annurev-biochem-072909-101058)
180. Doyle ET, Burns SM, Contag CH. 2004 In vivo bioluminescence imaging for integrated studies of infection. Cell. Microbiol. 6, 303-317. (doi:10.1111/j.1462-5822.2004.00378.x) (Pubitemid 38379814)