Tts1, the fission yeast homologue of the TMEM33 family, functions in NE remodeling during mitosis

Molecular Biology of the Cell

Volumn 25, Issue 19, 2014, Pages 2970-2983

  Zhang, Dan ^a   Oliferenko, Snezhana ^a,b  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; TMEM33 PROTEIN; TTS1 PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; NUCLEOPORIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; TETRASPANIN; TTS1 PROTEIN, S POMBE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL EXPANSION; CELL NUCLEUS MEMBRANE; ENDOPLASMIC RETICULUM; MITOSIS; MITOSIS SPINDLE; NONHUMAN; NUCLEAR PORE COMPLEX; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; SCHIZOSACCHAROMYCES; SPINDLE POLE BODY; AMINO ACID SEQUENCE; CHROMOSOME SEGREGATION; DNA SEQUENCE; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; NUCLEAR PORE; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

EUKARYOTA; SCHIZOSACCHAROMYCES POMBE; SCHIZOSACCHAROMYCETACEAE;

AMINO ACID SEQUENCE; BASE SEQUENCE; CHROMOSOME SEGREGATION; ENDOPLASMIC RETICULUM; MEMBRANE TRANSPORT PROTEINS; MITOSIS; NUCLEAR ENVELOPE; NUCLEAR PORE; NUCLEAR PORE COMPLEX PROTEINS; PROTEIN STRUCTURE, TERTIARY; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; SEQUENCE ANALYSIS, DNA; SPINDLE POLE BODIES; STRUCTURE-ACTIVITY RELATIONSHIP; TETRASPANINS;

EID: 84921380035     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-12-0729     Document Type: Article

References (64)

1. Anderson DJ, Hetzer MW (2007). Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nat Cell Biol 9, 1160-1166.
2. Anderson DJ, Hetzer MW (2008). Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. J Cell Biol 182, 911-924.
3. Antonin W, Mattaj IW (2005). Nuclear pore complexes: round the bend? Nat Cell Biol 7, 10-12.
4. Bae JA, Moon D, Yoon JH (2009). Nup211, the fission yeast homolog of Mlp1/Tpr, is involved in mRNA export. J Microbiol 47, 337-343.
5. Bahler J, Steever AB, Wheatley S, Wang Y, Pringle JR, Gould KL, McCollum D (1998). Role of polo kinase and Mid1p in determining the site of cell division in fission yeast. J Cell Biol 143, 1603-1616.
6. Bailey TL, Boden M, Buske FA, Frith M, Grant CE, Clementi L, Ren J, Li WW, Noble WS (2009). MEME SUITE: tools for motif discovery and searching. Nucleic Acids Res 37, W202-W208.
7. Belgareh N, Doye V (1997). Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. J Cell Biol 136, 747-759.
8. Bridge AJ, Morphew M, Bartlett R, Hagan IM (1998). The fission yeast SPB component Cut12 links bipolar spindle formation to mitotic control. Genes Dev 12, 927-942.
9. Casey AK, Dawson TR, Chen J, Friederichs JM, Jaspersen SL, Wente SR (2012). Integrity and function of the Saccharomyces cerevisiae spindle pole body depends on connections between the membrane proteins Ndc1, Rtn1, and Yop1. Genetics 192, 441-455.
10. Chadrin A, Hess B, San Roman M, Gatti X, Lombard B, Loew D, Barral Y, Palancade B, Doye V (2010). Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution. J Cell Biol 189, 795-811.
11. Chernomordik LV, Kozlov MM (2003). Protein-lipid interplay in fusion and fission of biological membranes. Annu Rev Biochem 72, 175-207.
12. Chernomordik LV, Kozlov MM (2008). Mechanics of membrane fusion. Nat Struct Mol Biol 15, 675-683.
13. Contreras FX, Ernst AM, Wieland F, Brugger B (2011). Specificity of intramembrane protein-lipid interactions. Cold Spring Harb Perspect Biol 3, a004705.
14. Dawson TR, Lazarus MD, Hetzer MW, Wente SR (2009). ER membrane-bending proteins are necessary for de novo nuclear pore formation. J Cell Biol 184, 659-675.
15. Ding R, West RR, Morphew DM, Oakley BR, McIntosh JR (1997). The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds. Mol Biol Cell 8, 1461-1479.
16. Fath S, Mancias JD, Bi X, Goldberg J (2007). Structure and organization of coat proteins in the COPII cage. Cell 129, 1325-1336.
17. Flory MR, Morphew M, Joseph JD, Means AR, Davis TN (2002). Pcp1p, an Spc110p-related calmodulin target at the centrosome of the fission yeast Schizosaccharomyces pombe. Cell Growth Differ 13, 47-58.
18. Fong CS, Sato M, Toda T (2010). Fission yeast Pcp1 links polo kinase-mediated mitotic entry to gamma-tubulin-dependent spindle formation. EMBO J 29, 120-130.
19. Fotin A, Cheng Y, Sliz P, Grigorieff N, Harrison SC, Kirchhausen T, Walz T (2004). Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature 432, 573-579.
20. Gautier R, Douguet D, Antonny B, Drin G (2008). HELIQUEST: a web server to screen sequences with specific alpha-helical properties. Bioinformatics 24, 2101-2102.
21. Giddings TH Jr, O'Toole ET, Morphew M, Mastronarde DN, McIntosh JR, Winey M (2001). Using rapid freeze and freeze-substitution for the preparation of yeast cells for electron microscopy and three-dimensional analysis. Methods Cell Biol 67, 27-42.
22. Gonzalez Y, Meerbrey K, Chong J, Torii Y, Padte NN, Sazer S (2009). Nuclear shape, growth and integrity in the closed mitosis of fission yeast depend on the Ran-GTPase system, the spindle pole body and the endoplasmic reticulum. J Cell Sci 122, 2464-2472.
23. Gould KL (2004). Protocols for experimentation with Schizosaccharomyces pombe. Methods 33, 187-188.
24. Grallert A, Krapp A, Bagley S, Simanis V, Hagan IM (2004). Recruitment of NIMA kinase shows that maturation of the S. pombe spindle-pole body occurs over consecutive cell cycles and reveals a role for NIMA in modulating SIN activity. Genes Dev 18, 1007-1021.
25. Grigoriev I, Gouveia SM, van der Vaart B, Demmers J, Smyth JT, Honnappa S, Splinter D, Steinmetz MO, Putney JW Jr, Hoogenraad CC, et al. (2008). STIM1 is a MT-plus-end-tracking protein involved in remodeling of the ER. Curr Biol 18, 177-182.
26. Hetzer MW (2010). The nuclear envelope. Cold Spring Harb Perspect Biol 2, a000539.
27. Hodge CA, Choudhary V, Wolyniak MJ, Scarcelli JJ, Schneiter R, Cole CN (2010). Integral membrane proteins Brr6 and Apq12 link assembly of the nuclear pore complex to lipid homeostasis in the endoplasmic reticulum. J Cell Sci 123, 141-151.
28. Horio T, Uzawa S, Jung MK, Oakley BR, Tanaka K, Yanagida M (1991). The fission yeast gamma-tubulin is essential for mitosis and is localized at microtubule organizing centers. J Cell Sci 99, 693-700.
29. Hu J, Shibata Y, Voss C, Shemesh T, Li Z, Coughlin M, Kozlov MM, Rapoport TA, Prinz WA (2008). Membrane proteins of the endoplasmic reticulum induce high-curvature tubules. Science 319, 1247-1250.
30. Hu J, Shibata Y, Zhu PP, Voss C, Rismanchi N, Prinz WA, Rapoport TA, Blackstone C (2009). A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell 138, 549-561.
31. Jaspersen SL, Ghosh S (2012). Nuclear envelope insertion of spindle pole bodies and nuclear pore complexes. Nucleus 3, 226-236.
32. Lee C, Goldberg J (2010). Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats. Cell 142, 123-132.
33. Lim HWG, Huber G, Torii Y, Hirata A, Miller J, Sazer S (2007). Vesicle-like biomechanics governs important aspects of nuclear geometry in fission yeast. PLoS One 2, e948.
34. Liu TY, Bian X, Sun S, Hu X, Klemm RW, Prinz WA, Rapoport TA, Hu J (2012). Lipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion. Proc Natl Acad Sci USA 109, E2146-E2154.
35. McMahon HT, Gallop JL (2005). Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438, 590-596.
36. Moritz M, Agard DA (2001). Gamma-tubulin complexes and microtubule nucleation. Curr Opin Struct Biol 11, 174-181.
37. Ohkura H, Hagan IM, Glover DM (1995). The conserved Schizosaccharomyces pombe kinase plo1, required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells. Genes Dev 9, 1059-1073.
38. Orso G, Pendin D, Liu S, Tosetto J, Moss TJ, Faust JE, Micaroni M, Egorova A, Martinuzzi A, McNew JA, et al. (2009). Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 460, 978-983.
39. Palsdottir H, Hunte C (2004). Lipids in membrane protein structures. Biochim Biophys Acta 1666, 2-18.
40. Petersen B, Petersen TN, Andersen P, Nielsen M, Lundegaard C (2009). A generic method for assignment of reliability scores applied to solvent accessibility predictions. BMC Struct Biol 9, 51.
41. Rao Y, Haucke V (2011). Membrane shaping by the Bin/amphiphysin/Rvs (BAR) domain protein superfamily. Cell Mol Life Sci 68, 3983-3993.
42. Roux A, Cuvelier D, Nassoy P, Prost J, Bassereau P, Goud B (2005). Role of curvature and phase transition in lipid sorting and fission of membrane tubules. EMBO J 24, 1537-1545.
43. Sheetz MP (2001). Cell control by membrane-cytoskeleton adhesion. Nat Rev Mol Cell Biol 2, 392-396.
44. Shibata Y, Hu J, Kozlov MM, Rapoport TA (2009). Mechanisms shaping the membranes of cellular organelles. Annu Rev Cell Dev Biol 25, 329-354.
45. Shibata Y, Shemesh T, Prinz WA, Palazzo AF, Kozlov MM, Rapoport TA (2010). Mechanisms determining the morphology of the peripheral ER. Cell 143, 774-788.
46. Shibata Y, Voss C, Rist JM, Hu J, Rapoport TA, Prinz WA, Voeltz GK (2008). The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J Biol Chem 283, 18892-18904.
47. Sparkes I, Tolley N, Aller I, Svozil J, Osterrieder A, Botchway S, Mueller C, Frigerio L, Hawes C (2010). Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell 22, 1333-1343.
48. Stagg SM, LaPointe P, Razvi A, Gurkan C, Potter CS, Carragher B, Balch WE (2008). Structural basis for cargo regulation of COPII coat assembly. Cell 134, 474-484.
49. Strambio-de-Castillia C, Blobel G, Rout MP (1999). Proteins connecting the nuclear pore complex with the nuclear interior. J Cell Biol 144, 839-855.
50. Tallada VA, Tanaka K, Yanagida M, Hagan IM (2009). The S. pombe mitotic regulator Cut12 promotes spindle pole body activation and integration into the nuclear envelope. J Cell Biol 185, 875-888.
51. Tamm T, Grallert A, Grossman EP, Alvarez-Tabares I, Stevens FE, Hagan IM (2011). Brr6 drives the Schizosaccharomyces pombe spindle pole body nuclear envelope insertion/extrusion cycle. J Cell Biol 195, 467-484.
52. Tusnady GE, Simon I (2001). The HMMTOP transmembrane topology prediction server. Bioinformatics 17, 849-850.
53. Vardy L, Toda T (2000). The fission yeast gamma-tubulin complex is required in G(1) phase and is a component of the spindle assembly checkpoint. EMBO J 19, 6098-6111.
54. Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA (2006). A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573-586.
55. Voeltz GK, Rolls MM, Rapoport TA (2002). Structural organization of the endoplasmic reticulum. EMBO Rep 3, 944-950.
56. Wagner W, Brenowitz SD, Hammer JA 3rd (2011). Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons. Nat Cell Biol 13, 40-48.
57. West RR, Vaisberg EV, Ding R, Nurse P, McIntosh JR (1998). cut11(+): A gene required for cell cycle-dependent spindle pole body anchoring in the nuclear envelope and bipolar spindle formation in Schizosaccharomyces pombe. Mol Biol Cell 9, 2839-2855.
58. Witkin KL, Friederichs JM, Cohen-Fix O, Jaspersen SL (2010). Changes in the nuclear envelope environment affect spindle pole body duplication in Saccharomyces cerevisiae. Genetics 186, 867-883.
59. Yam C, Gu Y, Oliferenko S (2013). Partitioning and remodeling of the Schizo-saccharomyces japonicus mitotic nucleus require chromosome tethers. Curr Biol 23, 2303-2310.
60. Yam C, He Y, Zhang D, Chiam KH, Oliferenko S (2011). Divergent strategies for controlling the nuclear membrane satisfy geometric constraints during nuclear division. Curr Biol 21, 1314-1319.
61. Zhang D, Oliferenko S (2013). Remodeling the nuclear membrane during closed mitosis. Curr Opin Cell Biol 25, 142-148.
62. Zhang D, Vjestica A, Oliferenko S (2010). The cortical ER network limits the permissive zone for actomyosin ring assembly. Curr Biol 20, 1029-1034.
63. Zhang D, Vjestica A, Oliferenko S (2012). Plasma membrane tethering of the cortical ER necessitates its finely reticulated architecture. Curr Biol 22, 2048-2052.
64. Zheng Y, Wong ML, Alberts B, Mitchison T (1995). Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex. Nature 378, 578-583.