Actin Doesn’t Do the Locomotion: Secretion Drives Cell Polarization

Part of the Molecular Biology Intelligence Unit book series (MBIU)


Cell polarity refers to the asymmetry in cell shape resulting from asymmetrical protein distribution within a cell in order to serve a specialized cell function or directional cell division. Mechanisms of cell polarization are conserved through evolution and are achieved by conserved multiprotein complexes. Recent advances have revealed that protein transport plays a key role in both the mechanisms and the regulation of cell polarity.


Lipid Raft Cell Polarity Secretory Vesicle Septum Formation Actin Cable 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Nelson WJ. Adaptation of core mechanisms to generate cell polarity. Nature 2003; 422:766–74.PubMedGoogle Scholar
  2. 2.
    Madden K, Snyder M. Cell polarity and morphogenesis in budding yeast. Annu Rev Microbiol 1998; 52:687–744.PubMedGoogle Scholar
  3. 3.
    Johnson Dl. Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity. Micro Molec Biol Rev 1999; 63:54–105.Google Scholar
  4. 4.
    Chant J. Cell polarity in yeast. Annu Rev Cell Dev Biol 1999; 15:365–91.PubMedGoogle Scholar
  5. 5.
    Pruyne D, Bretscher A. Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states. J Cell Sci 2000; 113:365–75.PubMedGoogle Scholar
  6. 6.
    Pruyne D, Bretscher A. Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton. J Cell Sci 2000; 113:571–85.PubMedGoogle Scholar
  7. 7.
    Wodarz A. Establishing cell polarity in development. Nature Cell Biol 2002; 4:E39–44.Google Scholar
  8. 8.
    Johnson K, Wodarz A. A genetic hierarchy controlling cell polarity. Nature Cell Biol 2003; 5:12–4.PubMedGoogle Scholar
  9. 9.
    Dohlman HG, Thorner JW. Regulation of G protein-initiated signal transduction in yeast: Paradigms and principles. Annu Rev Biochem 2001; 70:703–54.PubMedGoogle Scholar
  10. 10.
    Casamayor A, Snyder M. Bud-site selection and cell polarity in budding yeast. Curr Opin Microbiol 2002; 5:179–86.PubMedGoogle Scholar
  11. 11.
    Chang F, Peter M. Yeasts make their mark. Nature Cell Biol 2003; 5:294–9.PubMedGoogle Scholar
  12. 12.
    Thompson CRL, Bretscher MS. Cell polarity and locomotion, as well as endocytosis, depend on NSF. Development 2002; 129:4185–92.PubMedGoogle Scholar
  13. 13.
    Bretscher MS, Aguado-Velasco C. Membrane traffic during cell locomotion. Curr Opin Cell Biol 1998; 10:537–41.PubMedGoogle Scholar
  14. 14.
    Chang F. Studies in fission yeast on mechanisms of cell division site placement. Cell Struct Funct 2001; 26:539–44.PubMedGoogle Scholar
  15. 15.
    Plusa B, Grabarek JB, Piotrowska K et al. Site of the previous meiotic division defines cleavage orientation in the mouse embryo. Nature Cell Biol 2002; 4:811–5.PubMedGoogle Scholar
  16. 16.
    Bisgrove SR, Henderson DC, Kropf DL. Asymmetric division in fucoid zygotes is positioned by telophase nuclei. Plant Cell 2003; 15:854–62.PubMedGoogle Scholar
  17. 17.
    Ahringer J. Control of cell polarity and mitotic spindle positioning in animal cells. Curr Opin Cell Biol 2003; 15:73–81.PubMedGoogle Scholar
  18. 18.
    Chant J. Septin scaffolds and cleavage planes in Saccharomyces. Cell 1996; 84:187–90.PubMedGoogle Scholar
  19. 19.
    Chant J, Herskowitz I. Genetic control of bud site selection in yeast by a set of gene products that comprise a morphogenetic pathway. Cell 1991; 65:1203–12.PubMedGoogle Scholar
  20. 20.
    Sanders SL, Fields C. Bud-site selection is only skin deep. Curr Biol 1995; 5:1213–5.PubMedGoogle Scholar
  21. 21.
    Osman MA, Konopka JB, Cerione RA. Iqglp links spatial and secretion landmarks to polarity and cytokinesis. J Cell Biol 2002; 159:601–11.PubMedGoogle Scholar
  22. 22.
    Chen T, Hiroko T, Chaudhuri A et al. Multigenerational cortical inheritance of the Rax2 protein in orienting polarity and division in yeast. Science 2000; 290:1975–8.PubMedGoogle Scholar
  23. 23.
    Harkins HA, Pagé N, Schenkman LR et al. Bud8p and Bud9p, proteins that may mark the sites for bipolar budding in yeast. Molec Biol Cell 2001; 12:2497–518.PubMedGoogle Scholar
  24. 24.
    Fujita A, Oka C, Arikawa Y et al. A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature 1994; 372:567–70.PubMedGoogle Scholar
  25. 25.
    Haarer BK, Corbett A, Kweon Y et al. SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud selection. Genetics 1996; 144:495–510.PubMedGoogle Scholar
  26. 26.
    Finger FP, Hughes TE, Novick P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 1998; 92:559–71.PubMedGoogle Scholar
  27. 27.
    Osman M, Cerione RA. Iqglp, a yeast homologue of the mammalian IQGAPs, mediates Cdc42p effects on the actin cytoskeleton. J Cell Biol 1998; 142:443–55.PubMedGoogle Scholar
  28. 28.
    Cabib E, Roh DH, Schmidt M et al. The yeast cell wall and septum as paradigms of cell growth and morphogenesis. J Biol Chem 2001; 276:19679–82.PubMedGoogle Scholar
  29. 29.
    Bi E. Cytokinesis in budding yeast: The relationship between actomyosin ring function and septum formation. Cell Struct Funct 2001; 26:529–37.PubMedGoogle Scholar
  30. 30.
    Guo W, Roth D, Walch-Solimena C et al. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 1999; 18:1071–80.PubMedGoogle Scholar
  31. 31.
    Wedlich-Soldner R, Li R. Spontaneous cell polarization: Undermining determinism. Nature Cell Biol 2003; 5:267–70.PubMedGoogle Scholar
  32. 32.
    Weiner OD, Neilsen PO, Prestwich GD et al. A PtdInsP3-and Rho GTPase-mediated positive feedback loop regulates neutrophil polarity. Nature Cell Biol 2002; 4:509–12.PubMedGoogle Scholar
  33. 33.
    Wedlich-Soldner R, Altschuler S, Wu L et al. Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science 2003; 299:1231–5.PubMedGoogle Scholar
  34. 34.
    Lippincott J, Li R. Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J Cell Biol 1998; 140:355–66.PubMedGoogle Scholar
  35. 35.
    Epp AJ, Chant J. An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Curr Biol 1997; 7:921–9.PubMedGoogle Scholar
  36. 36.
    Marston AL, Chen T, Yang MC et al. A localized GTPase exchange factor, Bud5, determines the orientation of division axes in yeast. Current Biol 2001; 11:803–7.Google Scholar
  37. 37.
    Lord M, Yang MC, Mischke M et al. Cell cycle programs of gene experssion control morphogenetic protein localization. J Cell Biol 2000; 151:1501–11.PubMedGoogle Scholar
  38. 38.
    Schenkman LR, Caruso C, Pagé N et al. The role of cell cycle-regulated expression in the localization of spatial landmark proteins in yeast. J Cell Biol 2002; 156:829–41.PubMedGoogle Scholar
  39. 39.
    Jin H, Amberg DC. The secretory pathway mediates localization of the cell polarity regulator Aip3p/Bud6p. Mol Biol Cell 2000; 11:647–61.PubMedGoogle Scholar
  40. 40.
    Johnson Dl, Pringle JR. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J Cell Biol 1990; 111:143–52.PubMedGoogle Scholar
  41. 41.
    Pringle JR, Bi E, Harkins HA et al. Establishment of cell polarity in yeast. Cold Spring Harb Symp Quant Biol 1995; 60:729–44.PubMedGoogle Scholar
  42. 42.
    Bretscher A. Polarized growth and organelle segregation in yeast: The tracks, motors, and recep-tors. J Cell Biol 2003; 160:811–6.PubMedGoogle Scholar
  43. 43.
    Kang PJ, Sanson A, Lee B et al. A GDP/GTP exchange factor involved in linking a spatial land-mark to cell polarity. Science 2001; 292:1376–8.PubMedGoogle Scholar
  44. 44.
    Nern A, Arkowitz RA. G Proteins mediate changes in cell shape by stabilizing the axis of polarity. Molec Cell 2000; 5:853–64.PubMedGoogle Scholar
  45. 45.
    Caviston JP, Tcheperegine SE, Bi E. Singularity in budding: A role for the evolutionary con-served small GTPase Cdc42p. PNAS 2002; 99:12185–90.PubMedGoogle Scholar
  46. 46.
    Lew DJ, Reed SI. Cell cycle control of morphogenesis in budding yeast. Curr Opin Genet Dev 1995; 5:17–23.PubMedGoogle Scholar
  47. 47.
    TerBush DR, Novick P. Sec6, Sec8, and Seel5 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae. J Cell Biol 1995; 130:299–312.PubMedGoogle Scholar
  48. 48.
    Grindstaff KK, Yeaman C, Anandasabapathy N et al. Sec6/8 complex is recruited to cell-cell con-tacts and specifies transport vesicle deliveryt to the basal-lateral membrane in epithelial cells. Cell 1998; 93:731–40.PubMedGoogle Scholar
  49. 49.
    Hsu SC, Hazuka CD, Roth R et al. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 1998; 20:1111–22.PubMedGoogle Scholar
  50. 50.
    Hsu SC, Hazuka CD, Foletti DL et al. Targeting vesicles to specific sites on the plasma mem-brane: The role of the sec6/8 complex. Trends Cell Biol 1999; 9:150–3.PubMedGoogle Scholar
  51. 51.
    Matern HT, Yeaman C, Nelson WJ et al. The Sec6/8 complex in mammalian cells: Characterization of mammalian Sec3, subunit interactions, and expression of subunits in polarized cells. PNAS 2001; 98:9648–53.PubMedGoogle Scholar
  52. 52.
    Bowser R, Muller H, Govidan B et al. Sec8p and Secl5p are components of a plasma membrane-associated 19.5 S particle that may function downstream of Sec4p to control exocytosis. J Cell Biol 1992; 118:1041–56.PubMedGoogle Scholar
  53. 53.
    Guo W, Tamanoi F, Novick P. Spatial regulation of the exocyst complex by Rhol GTPase. Nat Cell Biol 2001; 3:353–60.PubMedGoogle Scholar
  54. 54.
    Zhang X, Bi E, Novick P et al. Cdc42 interacts with the exocyst and regulates polarized secretion. J Biol Chem 2001; 276:46745–50.PubMedGoogle Scholar
  55. 55.
    Adamo JE, Moskow JJ, Gladfelter AS et al. Yeast Cdc42 functions at a late step in exocytosis, specifically during polarized growth of the emerging bud. J Cell Biol 2001; 155:581–92.PubMedGoogle Scholar
  56. 56.
    Muller O, Johnson DI, Mayer A. Cdc42p functions at the docking stage of yeast vacuole membrane fusion. EMBO J 2001; 20:5657–65.PubMedGoogle Scholar
  57. 57.
    Richman TJ, Sawyer MM, Johnson DL Saccharomyces cerevisiae Cdc42p localizes to cellular membranes and clusters at sites of polarized growth. Eukaryotic Cell 2002; 1:458–68.PubMedGoogle Scholar
  58. 58.
    Schott D, Huffaker T, Bretscher A. Microfilaments and microtubules: The news from yeast. Curr Opin Microbiol 2002; 5:564–74.PubMedGoogle Scholar
  59. 59.
    Evangelista M, Pruyne D, Amberg DC et al. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol 2002; 4:32–41.PubMedGoogle Scholar
  60. 60.
    Sagot I, Klee SK, Pellman D. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nature Cell Biol 2002; 4:42–50.PubMedGoogle Scholar
  61. 61.
    Pruyne D, Evangelista M, Yang C et al. Role of formins in actin assembly: Nucleation and barbed end association. Science 2002; 297:612–5.PubMedGoogle Scholar
  62. 62.
    Sheu YJ, Santos B, Fortin N et al. Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis. Molec Cell Biol 1998; 18:4053–69.PubMedGoogle Scholar
  63. 63.
    van Drogen F, Peter M. Spa2p functions as a scaffold-like protein to recruit the Mpklp MAP kinase module to sites of polarized growth. Curr Biol 2002; 12:1698–703.PubMedGoogle Scholar
  64. 64.
    Fujiwara T, Tanaka K, Mino A et al. Rholp-Bnilp-Spa2p interactions: Implication in localization of Bnilp at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae. Molec Biol Cell 1998; 9:1221–33.PubMedGoogle Scholar
  65. 65.
    Mino A, Tanaka K, Kamei T et al. Shslp: A novel member of septin that interacts with Spa2p, involved in polarized growth in Saccharomyces cerevisiae. Biochem Biophys Res Comm 1998; 251:732–6.PubMedGoogle Scholar
  66. 66.
    Faty M, Fink M, Barral Y. Septins: A ring to part mother and daughter. Curr Genet 2002; 41:123–31.PubMedGoogle Scholar
  67. 67.
    Barral Y, Parra M, Bidlingmaier S et al. Niml-related kinases coordinate cell cycle progression with organization of the peripheral cytoskeleton. Genes Dev 1999; 13:176–87.PubMedGoogle Scholar
  68. 68.
    Barral Y, Mermall V, Mooseker MS et al. Compartmentalization of the cell cortex by septins is required for maintenance of cell polarity in yeast. Mol Cell 2000; 5:841–51.PubMedGoogle Scholar
  69. 69.
    Takizawa PA, DeRisi JL, Wilhelm JE et al. Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 2000; 290:341–4.PubMedGoogle Scholar
  70. 70.
    Schmidt M, Bowers B, Varma A et al. In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other. J Cell Sci 2001; 115:293–302.Google Scholar
  71. 71.
    Field C, Li R, Oegema K. Cytokinesis in eukaryotes: A mechanistic comparison. Curr Opin Cell Biol 1999; 11:68–80.PubMedGoogle Scholar
  72. 72.
    Hales KG, Bi E, Wu JQ et al. Cytokinesis: An emerging unified theory for eukaryotes? Curr Opin Cell Biol 1999; 11:717–25.PubMedGoogle Scholar
  73. 73.
    Gould KL, Simanis V. The control of septum formation in fission yeast. Genes Dev 1997; 11:2939–51.PubMedGoogle Scholar
  74. 74.
    Bi E, Maddox P, Lew DJ et al. Involvement of an actomyosin ring in Saccharomyces cerevisiae. J Cell Biol 1998; 142:1301–12.PubMedGoogle Scholar
  75. 75.
    Korinek WS, Bi E, Epp JA et al. Cyk3, a novel SH3-domain protein, affects cytokinesis in yeast. Curr Biol 2000; 10:947–50.PubMedGoogle Scholar
  76. 76.
    Vallen EA, Caviston J, Bi E. Roles of Hoflp, Bnilp, Bnrlp, and Myolp in cytokinesis in Saccharomyces cerevisiae. Molec Biol Cell 2000; 11:593–611.PubMedGoogle Scholar
  77. 77.
    Tolliday N, Pitcher M, Li R. Direct evidence for a critical role of Myosin II in budding yeast cytokinesis and the evolvability of new cytokinetic mechanisms in the absence of Myosin II. Molec Biol Cell 2003; 14:798–809.PubMedGoogle Scholar
  78. 78.
    Flescher EG, Madden K, Snyder M. Components required for cytokinesis are important for bud site selection in yeast. J Cell Biol 1993; 122:373–86.PubMedGoogle Scholar
  79. 79.
    Wang H, Tang X, Liu J et al. The multiprotein exocyst complex is essential for cell separation in Schizosaccharomyces pombe. Molec Biol Cell 2002; 13:515–29.PubMedGoogle Scholar
  80. 80.
    Colman-Lerner A, Chin TE, Brent R. Yeast Cbkl and Mob2 activate daughter-specific genetic programs to induce asymmetric cell fates. Cell 2001; 107:739–50.PubMedGoogle Scholar
  81. 81.
    Ríos-Munoz W, Ramírez MI, Molina FR et al. Myosin II is important for maintaining regulated secretion and asymmetric localization of chitinase 1 in the budding yeast. Arch Biochem Biophys 2003; 409:411–3.PubMedGoogle Scholar
  82. 82.
    Wagner W, Bielli P, Wacha S et al. MIclp promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p. EMBO J 2002; 21:6397–408.PubMedGoogle Scholar
  83. 83.
    Boyne JR, Yosuf HM, Bieganowski P et al. Yeast myosin light chain Mlclp, interacts with both IQGAP and class II myosin to effect cytokinesis. J Cell Sci 2000; 113:4533–43.PubMedGoogle Scholar
  84. 84.
    Shannon KB, Li RA. Myosin light chain mediates the localization of the budding yeast IQGAP-like protein during contractile ring formation. Curr Biol 2000; 10:727–30.PubMedGoogle Scholar
  85. 85.
    Stevens RC, Davis TN. Mlclp is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae. J Cell Biol 1998; 142:711–22.PubMedGoogle Scholar
  86. 86.
    Johnston GC, Prendergast JA, Singer RA. The Saccharomyces cerevisiae MY02 gene encodes an essential myosin for vectorial transport of vesicles. J Cell Biol 1991; 113:539–51.PubMedGoogle Scholar
  87. 87.
    Pruyne DW, Schott DH, Bretscher A. Tropomyosin-containign actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J Cell Biol 1998; 143:1931–45.PubMedGoogle Scholar
  88. 88.
    Schott D, Ho J, Pruyne D et al. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J Cell Biol 1999; 147:791–808.PubMedGoogle Scholar
  89. 89.
    Burack WR, Shaw AS. Signal transduction: Hanging on a scaffold. Curr Opin Cell Biol 2000; 12:211–6.PubMedGoogle Scholar
  90. 90.
    Ferrell Jr JE. What do scaffold proteins really do? Sci STKE 2000; 52:1–3.Google Scholar
  91. 91.
    Hartwell LH. Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp Cell Res 1971; 69:265–76.PubMedGoogle Scholar
  92. 92.
    Hartwell L, Culotti J, Reid B. Genetic control of the cell-division cycle in yeast. I. Detection of mutants. PNAS 1970; 66:352–9.PubMedGoogle Scholar
  93. 93.
    Hartwell LH, Culotti J, Pringle JR et al. Genetic control of the cell division cycle in yeast. Science 1974; 183:46–51.PubMedGoogle Scholar
  94. 94.
    Carroll CW, Altman R, Schieltz D et al. The septins are required for the mitosis-specific activtion of the Gin4 kinase. J Cell Biol 1998; 143:709–17.Google Scholar
  95. 95.
    Field CM, Kellogg D. Septins: Cytoskeletal polymers or signaling GTPases? Trend Cell Biol 1999; 9:387–94.Google Scholar
  96. 96.
    Trimble WS. Septins: A highly conserved family of membrane-associated GTPases with functions in cell division and beyond. J Membrane Biol 1999; 169:75–81.Google Scholar
  97. 97.
    Gladfelter AS, Pringle JR, Lew DJ. The septin cortex at the yeast mother-bud neck. Curr Opin Micro 2001; 4:681–9.Google Scholar
  98. 98.
    Kinoshita M, Noda M. Roles of septins in the mammalian cytokinesis machinery. Cell Struct Funct 2001; 26:667–70.PubMedGoogle Scholar
  99. 99.
    Oegema K, Desai A, Wong ML et al. Purification and assay of a septin complex from Drosophila embryos. Meth Enzymol 1998; 298:279–95.PubMedGoogle Scholar
  100. 100.
    Frazier JA, Wong ML, Longtine MS et al. Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function. J Cell Biol 1998; 143:737–49.PubMedGoogle Scholar
  101. 101.
    DeMarini DJ, Adams AE, Fares H et al. A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall. J Cell Biol 1997; 139:75–93.PubMedGoogle Scholar
  102. 102.
    Longtine MS, DeMarini DJ, Valencik ML et al. The septins: Roles in cytokinesis and other pro-cesses. Curr Opin Cell Biol 1996; 8:106–19.PubMedGoogle Scholar
  103. 103.
    Longtine MS, Theesfeld CL, McMillan JN et al. Septin-dependent assembly of a cell cycle-regulatory module in Saccharomyces cerevisiae. Mol Cell Biol 2000; 20:4049–61.PubMedGoogle Scholar
  104. 104.
    Beites CL, Xie H, Bowser R et al. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nature Neurosci 1999; 2:434–9.PubMedGoogle Scholar
  105. 105.
    Hart MJ, Callow MG, Souza B et al. IQGAP 1, a calmodulin-binding protein with a RasGAP-related domain, is a potential effector for Cdc42Hs. EMBO J 1996; 15:2997–3005.PubMedGoogle Scholar
  106. 106.
    McCallum SJ, Wu WJ, Cerione RA. Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAP1 and a Cdc42Hs binding partner IQGAP2. J Biol Chem 1996; 271:21732–7.PubMedGoogle Scholar
  107. 107.
    Erickson JW, Cerione RA, Hart MJ. Identification of an actin cytoskeleton complex that includes IQGAP and the Cdc42 GTPase. J Biol Chem 1997; 272:24443–7.PubMedGoogle Scholar
  108. 108.
    Shannon KB, Li R. The multiple roles of Cyklp in the assembly and function of the actomyosin ring in budding yeast. Mol Biol Cell 1999; 10:283–96.PubMedGoogle Scholar
  109. 109.
    McCollum D, Gould KL. Timing is everything: Regulation of mitotic exit and cytokinesis by the MEN and SIN. Trends Cell Biol 2001; 11:89–95.PubMedGoogle Scholar
  110. 110.
    Melkonian KA, Ostermeyer AG, Chen JZ et al. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J Biol Chem 1999; 274:3910–7.PubMedGoogle Scholar
  111. 111.
    Bagnat M, Keränen S, Shevchenko A et al. Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. PNAS 2000; 97:3254–9.PubMedGoogle Scholar
  112. 112.
    Bagnat M, Simons K. Cell surface polarization during yeast mating. PNAS 2002; 99:14183–8.PubMedGoogle Scholar
  113. 113.
    Wachtler V, Rajagopalan S, Balasubramanian MK. Sterol-rich plasma membrane domains in the fission yeast Schizosaccharomyces pombe. J Cell Sci 2003; 116:867–74.PubMedGoogle Scholar
  114. 114.
    Dickson RC, Lester RL. Sphingolipid functions in Saccharomyces cerevisiae. Biochimica et Biophysica Acta 2002; 1583:13–25.PubMedGoogle Scholar
  115. 115.
    Horejsi W. The roles of membrane microdomains (rafts) in T cell activation. Immunol Rev 2003; 191:148–64.PubMedGoogle Scholar
  116. 116.
    Young RM, Holowka D, Baird B. A lipid raft environment promotes increased Lyn kinase specific activity by protecting its active site tyrosine from dephosphorylation. J Biol Chem 2003; 278(23):20746–52.PubMedGoogle Scholar
  117. 117.
    Moffett S, Brown DA, Linder ME. Lipid-dependent targeting of G proteins into rafts. J Biol Chem 2000; 275:2191–8.PubMedGoogle Scholar
  118. 118.
    David D, Sundarababu S, Gerst JE. Involvement of long fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 1998; 143:1167–82.PubMedGoogle Scholar
  119. 119.
    Wu W, Erickson J, Lin R et al. The y-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000; 405:800–4.PubMedGoogle Scholar
  120. 120.
    Symons M, Derry J, Karlak B et al. Wiskott-aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization. Cell 1996; 84:723–34.PubMedGoogle Scholar
  121. 121.
    Miki H, Sasaki T, Takai Y et al. Induction of fllopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 1998; 391:93–6.PubMedGoogle Scholar
  122. 122.
    Rohatgi R, Ma L, Miki H et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 1999; 97:221–31.PubMedGoogle Scholar
  123. 123.
    Joberty G, Peterson C, Gao L et al. The cell-polarity protein Par6 links Par3 and the atypical protein kinase C to Cdc42. Nat Cell Biol 2000; 2:531–9.PubMedGoogle Scholar
  124. 124.
    Lin D, Edwards A, Fawcett J et al. A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Racl and aPKC signalling and cell polarity. Nat Cell Biol 2000; 2:540–7.PubMedGoogle Scholar
  125. 125.
    Qiu R, Abo A, Martin G. A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PCkξ signaling and cell transformation. Curr Biol 2000; 10:697–707.PubMedGoogle Scholar
  126. 126.
    Kuroda S, Fukata M, Nakagawa M et al. Role of IQGAP 1, a target of the small GTPases Cdc42 and Racl, in regulation of E-cadherin-mediated cell-cell adhesion. Science 1998; 281:832–5.PubMedGoogle Scholar
  127. 127.
    Kroschewski R, Hall A, Mellman I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat Cell Biol 1999; 1:8–13.PubMedGoogle Scholar
  128. 128.
    Hussain NK, Jenna S, Glogauer M et al. Endocytic protein intersectin-I regulates actin assembly via Cdc42 and N-WASP. Nat Cell Biol 2001; 3:927–32.PubMedGoogle Scholar
  129. 129.
    Yang W, Lo CG, Dispenza T et al. The Cdc42-target ACK2 directly interacts with clathrin and influences clathrin assembly. J Biol Chem 2001; 276:17468–73.PubMedGoogle Scholar
  130. 130.
    Lin Q, Lo C, Cerione RA et al. The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. J Biol Chem 2002; 277:10134–8.PubMedGoogle Scholar

Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  1. 1.Department of Molecular Medicine, College of Veterinary MedicineCornell UniversityIthacaUSA
  2. 2.Institute for Biotechnology and Life SciencesCornell UniversityIthacaUSA

Personalised recommendations