Microfilaments and microtubules: The news from yeast

Current Opinion in Microbiology

Volumn 5, Issue 6, 2002, Pages 564-574

  Schott, Daniel ^a   Huffaker, Tim ^a   Bretscher, Anthony ^a  

^a Cornell University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BINDING PROTEIN; CELL PROTEIN; KINESIN; MUTANT PROTEIN;

ACTIN POLYMERIZATION; CELL BUDDING; CELL DIVISION; CELL KINETICS; CELL MOTILITY; CELL NUCLEUS; CELL ORGANELLE; CELL SEPARATION; CELL TRANSPORT; CENTROMERE; CYTOPLASM; FUNGAL CELL; MICROFILAMENT; MICROTUBULE; MICROTUBULE ORGANIZING CENTER; MITOSIS SPINDLE; NONHUMAN; PROTEIN EXPRESSION; REVIEW; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; SYNTHESIS; YEAST; YEAST CELL;

SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE;

EID: 0036899850     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(02)00369-7     Document Type: Review

References (127)

1. Adams AE, Pringle JR: Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J Cell Biol 1984, 98:934-945.
2. Amberg DC: Three-dimensional imaging of the yeast actin cytoskeleton through the budding cell cycle. Mol Biol Cell 1998, 9:3259-3262.
3. Kilmartin JV, Adams AE: Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J Cell Biol 1984, 98:922-933.
4. Marks J, Hagan IM, Hyams JS: Growth polarity and cytokinesis in fission yeast: The role of the cytoskeleton. J Cell Sci 1986, 5(Suppl):229-241.
5. Gladfelter AS, Pringle JR, Lew DJ: The septin cortex at the yeast mother-bud neck. Curr Opin Microbiol 2001, 4:681-689.
6. Faty M, Fink M, Barral Y: Septins: A ring to part mother and daughter. Curr Genet 2002, 41:123-131.
7. Pruyne D, Bretscher A: Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton. J Cell Sci 2000, 113:571-585.
8. Winter D, Podtelejnikov AV, Mann M, Li R: The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches [Erratum: Curr Biol 1997, 7:R593]. Curr Biol 1997, 7:519-529.
9. Winter DC, Choe EY, Li R: Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits. Proc Natl Acad Sci USA 1999, 96:7288-7293.
10. Volkmann N, Amann KJ, Stoilova-McPhie S, Egile C, Winter DC, Hazelwood L, Heuser JE, Li R, Pollard TD, Hanein D: Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 2001, 293:2456-2459. The authors present beautiful electron micrographs of branched microfilaments containing the Arp2/3 complex.
11. Smith MG, Swamy SR, Pon LA: The life cycle of actin patches in mating yeast. J Cell Sci 2001, 114:1505-1513. Labeling Abp1p and Sac6p with green fluorescent protein (GFP) reveals patches that form in the mating projection and last 5-10 s. Most move randomly, while some move linearly away from the mating projection tip.
12. Warren DT, Andrews PD, Gourlay CW, Ayscough KR: Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. J Cell Sci 2002, 115:1703-1715. The actin-patch component Sla1p is found to bind the Arp2/3 activator Abp1p, but Sla1p and Abp1p are not in all yeast actin patches and those that contain only Sla1p move more slowly. SLA1 is needed for efficient endocytosis and rapid actin patch disassembly.
13. Lappalainen P, Drubin DG: Cofilin promotes rapid actin filament turnover in vivo. Nature 1997, 388:78-82.
14. Iida K, Yahara I: Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells 1999, 4:21-32.
15. Rodal AA, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC: Aip1p interacts with cofilin to disassemble actin filaments. J Cell Biol 1999, 145:1251-1264.
16. Watson HA, Cope MJ, Groen AC, Drubin DG, Wendland B: In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol Biol Cell 2001, 12:3668-3679. Prk1p is able to phosphorylate the epsin Ent1p, and the phenotypes and genetic interactions of mutants that mimic Ent1p phosphorylation or dephosphorylation are consistent with a role for Ark1p and Prk1p in negatively regulating the binding of Pan1p to Ent1p.
17. Cope MJ, Yang S, Shang C, Drubin DG: Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast. J Cell Biol 1999, 144:1203-1218.
18. Zeng G, Yu X, Cai M: Regulation of yeast actin cytoskeleton regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p. Mol Biol Cell 2001, 12:3759-3772. Prk1p is able to form a complex with the actin-patch components Sla1p and Pan1p, and can phosphorylate Sla1p. Sla1p phosphorylation may be one of several ways Prk1p regulates components involved in actin patches and endocytosis.
19. Kubler E, Riezman H: Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J 1993, 12:2855-2862.
20. Geli MI, Riezman H: Endocytic internalization in yeast and animal cells: Similar and different. J Cell Sci 1998, 111:1031-1037.
21. Mulholland J, Preuss D, Moon A, Wong A, Drubin D, Botstein D: Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J Cell Biol 1994, 125:381-391.
22. Merrifield CJ, Moss SE, Ballestrem C, Imhof BA, Giese G, Wunderlich I, Almers W: Endocytic vesicles move at the tips of actin tails in cultured mast cells. Nat Cell Biol 1999, 1:72-74.
23. May RC, Caron E, Hall A, Machesky LM: Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3. Nat Cell Biol 2000, 2:246-248.
24. Frischknecht F, Moreau V, Rottger S, Gonfloni S, Reckmann I, Superti-Furga G, Way M: Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Nature 1999, 401:926-929.
25. Doyle T, Botstein D: Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc Natl Acad Sci USA 1996, 93:3886-3891.
26. Waddle JA, Karpova TS, Waterston RH, Cooper JA: Movement of cortical actin patches in yeast. J Cell Biol 1996, 132:861-870.
27. Pelham RJ Jr, Chang F: Role of actin polymerization and actin cables in actin-patch movement in Schizosaccharomyces pombe. Nat Cell Biol 2001, 3:235-244. Labeling the actin cytoskeleton with green fluorescent protein (GFP)-tagged coronin shows that most actin patches move randomly at about 0.3 pm/s while others move along actin cables away from growth sites. Movement is dependent on Arp3p and profilin, implicating a role for polymerization in patch movement.
28. Carlsson AE, Shah AD, Eiking D, Karpova TS, Cooper JA: Quantitative analysis of actin patch movement in yeast. Biophys J 2002, 82:2333-2343. Most patches move randomly, while others show directed movement. Actin polymerization is suggested to be important for patch movement.
29. Utsugi T, Minemura M, Hirata A, Abe M, Watanabe D, Ohya Y: Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell wall synthesis. Genes Cells 2002, 7:1-9. The glucan synthase Fks1p tagged with green fluorescent protein is enriched on actin patches and moves like actin patches during the medium-budded cell cycle stage. Since las17 and arc18 mutants reduce patch and glucan synthase movement, an important function of actin patches may be to distribute cell wall synthesis evenly in the maturing bud.
30. Howard RJ: Ultrastructural analysis of hyphal tip cell growth in fungi: Spitzenkörper, cytoskeleton and endomembranes after freeze-substitution. J Cell Sci 1981, 48:89-103.
31. Baba M, Baba N, Ohsumi Y, Kanaya K, Osumi M: Three-dimensional analysis of morphogenesis induced by mating pheromone alpha factor in Saccharomyces cerevisiae. J Cell Sci 1989, 94:207-216.
32. Howard JP, Hutton JL, Olson JM, Payne GS: Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. J Cell Biol 2002, 157:315-326. Sla1p may target specific transmembrane proteins for endocytosis by physically linking them to clathrin-coated pits or actin or both.
33. Winter D, Lechler T, Li R: Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr Biol 1999, 9:501-504.
34. Goode BL, Rodal AA, Barnes G, Drubin DG: Activation of the Arp2/3 complex by the actin filament binding protein abp1p. J Cell Biol 2001, 153:627-634. In vitro experiments show that the actin patch component Abp1p binds and activates the Arp2/3 complex. Since Abp1p binds microfilaments, it may recruit Arp2/3 to the sides of filaments.
35. Duncan MC, Cope MJ, Goode BL, Wendland B, Drubin DG: Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex. Nat Cell Biol 2001, 3:687-690. The first evidence is presented for a direct link by Pan1p between the endocytic machinery (the clathrin coat), and an actin polymerization machinery (the Arp2/3 complex).
36. Wendland B, Emr SD: Pan1p, yeast Eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis. J Cell Biol 1998, 141:71-84.
37. Wendland B, Steece KE, Emr SD: Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J 1999, 18:4383-4393.
38. Wendland B, McCaffery JM, Xiao Q, Emr SD: A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J Cell Biol 1996, 135:1485-1500.
39. Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T, Leberer E, Whiteway M, Thomas DY, Boone C: A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J Cell Biol 2000, 148:353-362.
40. Lee WL, Bezanilla M, Pollard TD: Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASP. J Cell Biol 2000, 151:789-800.
41. Lechler T, Jonsdottir GA, Klee SK, Pellman D, Li R: A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J Cell Biol 2001, 155:261-270. In vitro, the Saccharomyces WASP-interacting protein/verprolin homolog and actin-patch component Vrp1p complexes with the Arp2/3 activators Las17p (WASP homolog) and myosin-I, and assists activation of the Arp2/3 complex by myosin-I.
42. Matile P, Moor H, Robinow CF: Yeast cytology. In The Yeasts, vol 1. Edited by Rose AH, Harrison JS. Academic Press, London; 1969:219-302.
43. Mulholland J, Konopka J, Singer-Kruger B, Zerial M, Botstein D: Visualization of receptor-mediated endocytosis in yeast. Mol Biol Cell 1999, 10:799-817.
44. Kobori H, Yamada N, Taki A, Osumi M: Actin is associated with the formation of the cell wall in reverting protoplasts of the fission yeast Schizosaccharomyces pombe. J Cell Sci 1989, 94:635-646.
45. Mulholland J, Wesp A, Riezman H, Botstein D: Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretary vesicle. Mol Biol Cell 1997, 8:1481-1499.
46. Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA: Synthetic lethality screen identifies a novel yeast myosin-I gene (MYO5): Myosin-I proteins are required for polarization of the actin cytoskeleton. J Cell Biol 1996, 133:1277-1291.
47. Ayscough KR, Eby JJ, Lila T, Dewar H, Kozminski KG, Drubin DG: Sia1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1 p-GTPase and Sla2p, a protein with talin homology. Mol Biol Cell 1999, 10:1061-1075.
48. Belmont LD, Drubin DG: The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J Cell Biol 1998, 142:1289-1299.
49. Johnston GC, Prendergast JA, Singer RA: The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J Cell Biol 1991, 113:539-551.
50. Pruyne DW, Schott DH, Bretscher A: Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J Cell Biol 1998, 143:1931-1945.
51. Govindan B, Bowser R, Novick P: The role of Myo2, a yeast class V myosin, in vesicular transport. J Cell Biol 1995, 128:1055-1068.
52. Karpova TS, Reck-Peterson SL, Elkind NB, Mooseker MS, Novick PJ, Cooper JA: Role of actin and Myo2p in polarized secretion and growth of Saccharomyces cerevisiae. Mol Biol Cell 2000, 11:1727-1737.
53. Schott D, Ho J, Pruyne D, Bretscher A: 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.
54. Schott DH, Collins RN, Bretscher A: Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length. J Cell Biol 2002, 156:35-39. Tagging the secretory vesicle marker Sec4p with green fluorescent protein in Saccharomyces reveals transit across the cell to exocytosis sites. Varying the number of light-chain-binding repeats in the myosin-V Myo2p demonstrates that Myo2p is the motor for Sec4p movement, and provides in vivo evidence for the lever arm model of myosin.
55. Reck-Peterson SL, Tyska MJ, Novick PJ, Mooseker MS: The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actinbased motors. J Cell Biol 2001, 153:1121-1126. The first in vitro motility assays for the two class-V myosins in Saccharomyces are described.
56. Uyeda TQ, Abramson PD, Spudich JA: The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc Natl Acad Sci USA 1996, 93:4459-4464.
57. Catlett NL, Duex JE, Tang F, Weisman LS: Two distinct regions in a yeast myosin-V tall domain are required for the movement of different cargoes. J Cell Biol 2000, 150:513-526.
58. Hoepfner D, van den Berg M, Philippsen P, Tabak HF, Hettema EH: A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J Cell Biol 2001, 155:979-990. Peroxisomes line up along actin cables and show gradual, MYO2-dependent movement into the bud.
59. Rossanese OW, Reinke CA, Bevis BJ, Hammond AT, Sears IB, O'Connor J, Glick BS: A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J Cell Biol 2001, 153:47-62. Visualization of Sec7p-GFP-labeled particles, presumably late Golgi cisternae, suggests that Myo2p can transport some of the Golgi cisternae into the bud.
60. Yin H, Pruyne D, Huffaker TC, Bretscher A: Myosin V orientates the mitotic spindle in yeast. Nature 2000, 406:1013-1015.
61. Beach DL, Thibodeaux J, Maddox P, Yeh E, Bloom K: The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast. Curr Biol 2000, 10:1497-1506.
62. Kusch J, Meyer A, Snyder MP, Barral Y: Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Genes Dev 2002, 16:1627-1639. Microtubule capture at the bud neck is mediated by Kar9p, but, interestingly, capture may be partially independent of actin or myosin.
63. Kwon S, Schnapp BJ: RNA localization: SHEdding light on the RNA-motor linkage. Curr Biol 2001, 11:R166-168.
64. Yang HC, Pon LA: Actin cable dynamics in budding yeast. Proc Natl Acad Sci USA 2002, 99:751-756. Using Abp140-GFP to label actin cables, elongating actin cables are shown to translocate at 0.3 μm/s away from the bud while new material is added at the same pace at the proximal end. Actin cables not anchored show directed translocation, presumably driven by myosin, and fail to elongate.
65. Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A: Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol 2002, 4:32-41. Assembly of actin cables is shown to be dependent on the formins Bni1p and Bnr1p and independent of the Arp2/3 complex.
66. Feierbach B, Chang F: Roles of the fission yeast formin For3p in cell polarity, actin cable formation and symmetric cell division. Curr Biol 2001, 11:1656-1665. Cells lacking the formin For3p lack detectable actin cables, have a depolarized myosin-V distribution and show partial defects in polarized growth.
67. Ozaki-Kuroda K, Yamamoto Y, Nohara H, Kinoshita M, Fujiwara T, Irie K, Takai Y: Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae. Mol Cell Biol 2001, 21:827-839. A remarkable correlation between regions of cell expansion with the minuteto-minute distribution of GFP-Bni1p is demonstrated.
68. Imamura H, Tanaka K, Hihara T, Umikawa M, Kamei T, Takahashi K, Sasaki T, Takai Y: Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J 1997, 16:2745-2755.
69. Kohno H, Tanaka K, Mino A, Umikawa M, Imamura H, Fujiwara T, Fujita Y, Hotta K, Qadota H, Watanabe T et al.: Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J 1996, 15:6060-6068.
70. Evangelista M, Blundell K, Longtine MS, Chow CJ, Adames N, Pringle J R, Peter M, Boone C: Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 1997, 276:118-122.
71. Sagot I, Klee SK, Pellman D: Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat Cell Biol 2002, 4:42-50.
72. Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, Bretscher A, Boone C: Role of formins in actin assembly: Nucleation and barbed-end association. Science 2002, 297:612-615. The Saccharomyces formin Bni1p is shown to nucleate actin polymerization and remain bound to the growing barbed ends of microfilaments. This work provides a molecular mechanism for the assembly of unbranched polarized microfilaments.
73. Sagot I, Rodal AA, Moseley J, Goode BL, Pellman D: An actin nucleation mechanism mediated by Bni1 and Profilin. Nat Cell Biol 2002, 4:626-631.
74. Adams AE, Botstein D, Drubin DG: Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature 1991, 354:404-408.
75. Balasubramanian MK, Helfman DM, Hemmingsen SM: A new tropomyosin essential for cytokinesis in the fission yeast S. pombe. Nature 1992, 360:84-87.
76. 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, 140:355-366.
77. Rodriguez JR, Paterson BM: Yeast myosin heavy chain mutant: Maintenance of the cell type specific budding pattern and the normal deposition of chitin and cell wall components requires an intact myosin heavy chain gene. Cell Motil Cytoskeleton 1990, 17:301-308.
78. Schmidt M, Bowers B, Varma A, Roh DH, Cabib E: In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other. J Cell Sci 2002, 115:293-302. Chitin synthase and myosin-I mutants show similar defects in actomyosin ring contraction, and primary septum (a chitin disc) formation, and orderly plasma membrane invagination during cytokinesis, which raises the possibility that chitin synthesis might provide part of the force for actomyosin ring contraction.
79. Vallen EA, Caviston J, Bi E: Roles of Hof1p, Bni1p, Bnr1p, and Myo1p in cytokinesis in Saccharomyces cerevisiae. Mol Biol Cell 2000, 11:593-611.
80. Heitz MJ, Petersen J, Valovin S, Hagan IM: MTOC formation during mitotic exit in fission yeast. J Cell Sci 2001, 114:4521-4532. The actin ring recruits the microtubule nucleator γ-tubulin to maintain a cytoplasmic equatorial microtubule-organizing-centre.
81. Chang F, Woollard A, Nurse P: Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring. J Cell Sci 1996, 109:131-142.
82. Chang F, Drubin D, Nurse P: cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J Cell Biol 1997, 137:169-182.
83. Pelham RJ, Chang F: Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 2002, 419:82-86. Results are presented to indicate that two actin nucleators, the Arp2/3 complex and formins, are involved in actin-ring formation and maintenance.
84. Motegi F, Nakano K, Mabuchi I: Molecular mechanism of myosin-II assembly at the division site in Schizosaccharomyces pombe. J Cell Sci 2000, 113:1813-1825.
85. Arai R, Mabuchi I: F-actin ring formation and the role of F-actin cables in the fission yeast Schizosaccharomyces pombe. J Cell Sci 2002, 115:887-898. Observation of actin cables suggest that they might be involved in the initial formation of the ring.
86. Wong KC, D'Souza VM, Naqvi NI, Motegi F, Mabuchi I, Balasubramanian MK: Importance of a Myosin II-containing progenitor for actomyosin ring assembly in fission yeast. Curr Biol 2002, 12:724-729. By observing the distribution of myosin-II or myosin regulatory light chain, it is proposed that a remnant of the myosin ring from a previous cell cycle might normally serve as a template for the formation of a new actin ring.
87. Palmer RE, Sullivan DS, Huffaker T, Koshland D: Role of astral microtubules and actin in spindle orientation and migration in the budding yeast, Saccharomyces cerevisiae. J Cell Biol 1992, 119:583-593.
88. Fehrenbacher KL, Davis D, Wu M, Boldogh I, Pon LA: Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol Biol Cell 2002, 13:854-865. Both microtubules and actin might contribute to the endoplasmic reticulum distribution during different parts of the cell cycle.
89. Motegi F, Arai R, Mabuchi I: Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell. Mol Biol Cell 2001, 12:1367-1380. Unlike in Saccharomyces, polarized growth in Schizosaccharomyces does not absolutely require myosin-V, suggesting that this yeast has additional mechanisms for targeting secretion to growth sites.
90. Win TZ, Gachet Y, Mulvihill DP, May KM, Hyams JS: Two type V myosins with non-overlapping functions in the fission yeast Schizosaccharomyces pombe: Myo52 is concerned with growth polarity and cytokinesis, Myo51 is a component of the cytokinetic actin ring. J Cell Sci 2001, 114:69-79. Unlike in Saccharomyces, polarized growth in Schizosaccharomyces does not absolutely require myosin-V, suggesting that this yeast has additional mechanisms for targeting secretion to growth sites. Interestingly, the myosin-V that is unimportant for polarized growth concentrates on the cytokinetic ring.
91. Wedlich-Soldner R, Straube A, Friedrich MW, Steinberg G: A balance of KIF1A-like kinesin and dynein organizes early endosomes in the fungus Ustilago maydis. EMBO J 2002, 21:2946-2957. By analysing the dynamics of Kin3, it is proposed that dynein and kinesin carry the endosomes in opposite directions along microtubules.
92. Wedlich-Soldner R, Schulz I, Straube A, Steinberg G: Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis. Mol Biol Cell 2002, 13:965-977. Motility of the endoplasmic reticulum along microtubules in Ustilago maydis is disrupted in a temperature-sensitive dynein mutant.
93. Desai A, Mitchison TJ: Microtubule polymerization dynamics. Annu Rev Cell Dev Biol 1997, 13:83-117.
94. Dougherty CA, Sage CR, Davis A, Farrell KW: Mutation in the beta tubulin signature motif suppresses microtubule GTPase activity and dynamics, and slows mitosis. Biochemistry 2001, 40:15725-15732. GTP binding and hydrolysis by β-tubulin is important for microtubule dynamics and for spindle function.
95. Anders KR, Botstein D: Dominant-lethal alpha-tubulin mutants defective in microtubule depolymerization in yeast. Mol Biol Cell 2001, 12:3973-3986. The prediction from structural data that dynamic instability is due to GTPase activation between neighbouring tubulin heterodimers is supported by mutagenesis studies.
96. Kosco KA, Pearson CG, Maddox PS, Wang PJ, Adams IR, Salmon ED, Bloom K, Huffaker TC: Control of microtubule dynamics by Stu2p is essential for spindle orientation and metaphase chromosome alignment in yeast. Mol Biol Cell 2001, 12:2870-2880. Saccharomyces Stu2p, a member of a conserved microtubule-binding protein family, is shown to promote microtubule dynamics in both the cytoplasm and the spindle and is needed for proper spindle orientation and chromosome alignment.
97. Severin F, Habermann B, Huffaker T, Hyman T: Stu2 promotes mitotic spindle elongation in anaphase. J Cell Biol 2001, 153:435-442. Since Stu2p stabilizes microtubules during anaphase and its activity in vivo is opposed by Kip3p, a homologue of microtubule-destabilizing kinesins, proper spindle elongation may require a balance among conserved microtubule-stabilizing and -destabilizing factors.
98. Caron JM, Vega LR, Fleming J, Bishop R, Solomon F: Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: Possible role for palmitoylation of alpha-tubulin. Mol Biol Cell 2001, 12:2672-2687. A mutation in α-tubulin that increases cytoplasmic microtubule number and length in dividing cells also reduces α-tubulin palmitoylation, hinting that palmitoylation of this cysteine residue stimulates microtubule depolymerization during nuclear migration.
99. Knop M, Schiebel E: Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to the spindle pole-body via their interaction with Spc110p. EMBO J 1997, 16:6985-6995.
100. Vinh DB, Kern JW, Hancock WO, Howard J, Davis TN: Reconstitution and characterization of budding yeast gamma-tubulin complex. Mol Biol Cell 2002, 13:1144-1157. Reconstitution of a Saccharomyces γ-tubulin complex from purified recombinant Tub4p (γ-tubulin), Spc97p and Spc98p is reported and shown to bind to the spindle pole body docking protein Spc110p (bearing Cmd1p, calmodulin).
101. Vogel J, Drapkin B, Oomen J, Beach D, Bloom K, Snyder M: Phosphorylation of gamma-tubulin regulates microtubule organization in budding yeast. Dev Cell 2001, 1:621-631. The authors show that Saccharomyces γ-tubulin (Tub4p) is particularly phosphorylated in the G1 phase of the cell cycle. Mutation of an amino acid needed for phosphorylation affects the number of microtubules in the cell, suggesting that phosphorylation regulates the microtubule nucleation activity of Tub4p.
102. Maddox PS, Bloom KS, Salmon ED: The polarity and dynamics of microtubule assembly in the budding yeast Saccharomyces cerevisiae. Nat Cell Biol 2000, 2:36-41.
103. Van Hooser AA, Heald R: Kinetochore function: The complications of becoming attached. Curr Biol 2001, 11:R855-857.
104. Cheeseman IM, Drubin DG, Barnes G: Simple centromere, complex kinetochore: Linking spindle microtubules and centromeric DNA in budding yeast. J Cell Biol 2002, 157:199-203.
105. Hofmann C, Cheeseman IM, Goode BL, McDonald KL, Barnes G, Drubin DG: Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in mitotic spindle function. J Cell Biol 1998, 143:1029-1040.
106. Cheeseman IM, Brew C, Wolyniak M, Desai A, Anderson S, Muster N, Yates JR, Huffaker TC, Drubin DG, Barnes G: Implication of a novel multiprotein Dam1p complex in outer kinetochore function. J Cell Biol 2001, 155:1137-1145. In vitro and in vivo evidence is provided for a complex of Dam1p, Duo1p, Dad1p, Spc19p, Spc34p, Dad2p and Ask1p that binds microtubules and functions at the kinetochore.
107. Janke C, Ortiz J, Tanaka TU, Lechner J, Schiebel E: Four new subunits of the Dam1-Duo1 complex reveal novel functions in sister kinetochore biorientation. EMBO J 2002, 21:181-193. Ask1p, Dad2p, Spc19p and Spc34p are identified as components of the Dam1p kinetochore complex and Spc34p, and analysis of spc34 mutants suggests that the two spindle pole bodies are normally unequal.
108. Li Y, Bachant J, Alcasabas AA, Wang Y, Qin J, Elledge SJ: The mitotic spindle is required for loading of the DASH complex onto the kinetochore. Genes Dev 2002, 16:183-197. The Saccharomyces kinetochore protein Ask1 p is shown to be a component of the Dam1 p complex, which is important for sister chromatid separation and spindle integrity. Interestingly, treatment with the microtubule-depolymerizing drug nocodazole prevents the association of Ask1p with centromeres, suggesting that spindle microtubules may help load components onto the kinetochore.
109. He X, Rines DR, Espelin CW, Sorger PK: Molecular analysis of kinetochore-microtubule attachment in budding yeast. Cell 2001, 106:195-206. Ten kinetochore proteins are identified, some of which are microtubule-associated proteins, suggesting possible physical links between microtubules and kinetochores, which so far have been elusive.
110. Enquist-Newman M, Cheeseman IM, Van Goor D, Drubin DG, Meluh PB, Barnes G: Dad1p, third component of the duo1p/dam1p complex involved in kinetochore function and mitotic spindle integrity. Mol Biol Cell 2001, 12:2601-2613. A new component of the Dam1p kinetochore complex is identified and characterized.
111. Jones MH, He X, Giddings TH, Winey M: Yeast Dam1p has a role at the kinetochore in assembly of the mitotic spindle. Proc Natl Acad Sci USA 2001, 98:13675-13680. Dam1p is shown to be an important part of the kinetochore in Saccharomyces.
112. Cheeseman IM, Enquist-Newman M, Muller-Reichert T, Drubin DG, Barnes G: Mitotic spindle integrity and kinetochore function linked by the Duo1p/Dam1p complex. J Cell Biol 2001, 152:197-212. Biochemical and genetic data showing that Duo1 p and Dam1p are part of an important complex in the kinetochore.
113. Hoyt MA, He L, Loo KK, Saunders WS: Two Saccharomyces cerevisiae kinesin-related gene products required for mitotic spindle assembly. J Cell Biol 1992, 118:109-120.
114. West RR, Malmstrom T, McIntosh JR: Kinesins Klp5(+) and Klp6(+) are required for normal chromosome movement in mitosis. J Cell Sci 2002, 115:931-940. The role of two kinetochore-associated kinesins in chromosome movement is discussed.
115. Garcia MA, Koonrugsa N, Toda T: Two kinesin-like Kln I family proteins in fission yeast regulate the establishment of metaphase and the onset of anaphase A. Curr Biol 2002, 12:610-621. Kinl-family kinesin homologs Klp5 and Klp6, which are often microtubule-disassembling enzymes, are needed for efficient chromosome movement, suggesting they might contribute to pole-ward force on kinetochores.
116. Lin H, de Carvalho P, Kho D, Tai CY, Pierre P, Fink GR, Pellman D: Polyploids require Bik1 for kinetochore-microtubule attachment. J Cell Biol 2001, 155:1173-1184. Bik1p, the yeast CLIP170 homologue, is found to be essential in polyploids and to contribute to the pole-ward force on sister chromatids. This suggests that Bik1p is involved in the microtubule-kinetochore linkage.
117. He X, Asthana S, Sorger PK: Transient sister chromatid separation and elastic deformation of chromosomes during mitosis in budding yeast. Cell 2000, 101:763-775.
118. Garcia MA, Vardy L, Koonrugsa N, Toda T: Fission yeast ch TOG/XMAP215 homologue Alp14 connects mitotic spindles with the kinetochore and is a component of the Mad2-dependent spindle checkpoint. EMBO J 2001, 20:3389-3401. Alp14, a Schizosaccharomyces homologue of Saccharomyces Stu2p, is found at kinetochores and may bridge them to the plus end of microtubules.
119. Nakaseko Y, Goshima G, Morishita J, Yanagida M: M phase-specific kinetochore proteins in fission yeast: Microtubule-associating Dis1 and Mtc1 display rapid separation and segregation during anaphase. Curr Biol 2001, 11:537-549. Evidence is presented that Dis1p and Mtc1p, members of a conserved microtubule-binding protein family that includes frog XMAP215, may provide a physical linkage between microtubules and the kinetochore.
120. Biggins S, Severin FF, Bhalla N, Sassoon I, Hyman AA, Murray AW: The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast. Genes Dev 1999, 13:532-544.
121. Kang J, Cheeseman IM, Kallstrom G, Velmurugan S, Barnes G, Chan CS: Functional cooperation of Dam1, Ipl1, and the inner centromere protein (INCENP)-related protein Sli15 during chromosome segregation. J Cell Biol 2001, 155:763-774. The protein kinase Ipl1p and its activator Sli1p bind microtubules and the Dam1p-Duo1p complex. Since Sli1p and Ipl1p are located at the kinetochore, the results suggest that phosphorylation by Ipl1p might regulate kinetochore function.
122. Tanaka TU, Rachidi N, Janke C, Pereira G, Galova M, Schiebel E, Stark MJ, Nasmyth K: Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections. Cell 2002, 108:317-329. Ipl1p-Sli1p, the Saccharomyces homologue of the Aurora-INCENP complex, is needed for bipolar orientation of sister kinetochores, and kinetochores in ipl1 mutants stay attached to old spindle pole bodies suggesting a model where Ipl1p causes kinetochore-microtubule connection turnover until sister kinetochores pull toward opposite spindle poles.
123. Yin H, You L, Pasqualone D, Kopski KM, Huffaker TC: Stu1p Is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle. Mol Biol Cell 2002, 13:1881-1892. Genetic and localization data suggest that Stu1p participates in providing an outward force on spindle poles during anaphase.
124. Troxell CL, Sweezy MA, West RR, Reed KD, Carson BD, Pidoux AL, Cande WZ, McIntosh JR: Pkl1(+)and Klp2(+): Two kinesins of the Kar3 subfamily in fission yeast perform different functions in both mitosis and meiosis. Mol Biol Cell 2001, 12:3476-3488. The authors investigate the roles of two Kar3-subfamily kinesin-like proteins in Schizosaccharomyces mitosis and meiosis.
125. van Hemert MJ, Lamers GE, Klein DC, Oosterkamp TH, Steensma HY, van Heusden GP: The Saccharomyces cerevisiae Fin1 protein forms cell cycle-specific filaments between spindle pole bodies. Proc Natl Acad Sci USA 2002, 99:5390-5393. The Fin1 p protein polymerizes into filaments in vitro and concentrates on late mitotic spindles in vivo, suggesting that it forms part of a filamentous non-microtubule spindle matrix.
126. Schafer DA, Welch MD, Machesky LM, Bridgman PC, Meyer SM, Cooper JA: Visualization and molecular analysis of actin assembly in living cells. J Cell Biol 1998, 143:1919-1930.
127. Li R: Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J Cell Biol 1997,136:649-658.