메뉴 건너뛰기




Volumn 443, Issue 7110, 2006, Pages 466-469

Structural insights into yeast septin organization from polarized fluorescence microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; CELL MEMBRANES; ENZYME KINETICS; MICROSCOPIC EXAMINATION; YEAST;

EID: 33749165924     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05109     Document Type: Article
Times cited : (193)

References (29)
  • 1
    • 0029982293 scopus 로고    scopus 로고
    • A purified Drosophila septin complex forms filaments and exhibits GTPase activity
    • Field, C. M. et al. A purified Drosophila septin complex forms filaments and exhibits GTPase activity. J. Cell Biol. 133, 605-616 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 605-616
    • Field, C.M.1
  • 2
    • 0030943556 scopus 로고    scopus 로고
    • Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures
    • Kinoshita, M. et al. Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev. 11, 1535-1547 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 1535-1547
    • Kinoshita, M.1
  • 3
    • 0028175009 scopus 로고
    • The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins
    • Neufeld, T. P. & Rubin, G. M. The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins. Cell 77, 371-379 (1994).
    • (1994) Cell , vol.77 , pp. 371-379
    • Neufeld, T.P.1    Rubin, G.M.2
  • 4
    • 0015193588 scopus 로고
    • Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis
    • Hartwell, L. H. Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp. Cell Res. 69, 265-276 (1971).
    • (1971) Exp. Cell Res. , vol.69 , pp. 265-276
    • Hartwell, L.H.1
  • 5
    • 3142729153 scopus 로고    scopus 로고
    • Spatial coordination of cytokinetic events by compartmentalization of the cell cortex
    • Dobbelaere, J. & Barral, Y. Spatial coordination of cytokinetic events by compartmentalization of the cell cortex. Science 305, 393-396 (2004).
    • (2004) Science , vol.305 , pp. 393-396
    • Dobbelaere, J.1    Barral, Y.2
  • 6
    • 0035030209 scopus 로고    scopus 로고
    • The Tem1 small GTPase controls actomyosin and septin dynamics during cytokinesis
    • Lippincott, J., Shannon, K. B., Shou, W., Deshaies, R. J. & Li, R. The Tem1 small GTPase controls actomyosin and septin dynamics during cytokinesis. J. Cell Sci. 114, 1379-1386 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 1379-1386
    • Lippincott, J.1    Shannon, K.B.2    Shou, W.3    Deshaies, R.J.4    Li, R.5
  • 7
    • 0034965127 scopus 로고    scopus 로고
    • Cell cycle control of septin ring dynamics in the budding yeast
    • Cid, V. J., Adamikova, L., Sanchez, M., Molina, M. & Nombela, C. Cell cycle control of septin ring dynamics in the budding yeast. Microbiology 147, 1437-1450 (2001).
    • (2001) Microbiology , vol.147 , pp. 1437-1450
    • Cid, V.J.1    Adamikova, L.2    Sanchez, M.3    Molina, M.4    Nombela, C.5
  • 8
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function
    • Frazier, J. A. et al. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J. Cell Biol. 143, 737-749 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 737-749
    • Frazier, J.A.1
  • 10
    • 0017153996 scopus 로고
    • A highly ordered ring of membrane-associated filaments in budding yeast
    • Byers, B. & Goetsch, L. A highly ordered ring of membrane-associated filaments in budding yeast. J. Cell Biol. 69, 717-721 (1976).
    • (1976) J. Cell Biol. , vol.69 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 11
    • 0024572299 scopus 로고
    • Fluorescence polarization microscopy
    • Axelrod, D. Fluorescence polarization microscopy. Methods Cell Biol. 30, 333-352 (1989).
    • (1989) Methods Cell Biol. , vol.30 , pp. 333-352
    • Axelrod, D.1
  • 12
    • 3042722112 scopus 로고    scopus 로고
    • Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae
    • Sheff, M. A. & Thorn, K. S. Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae. Yeast 21, 661-670 (2004).
    • (2004) Yeast , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 13
    • 0021530625 scopus 로고
    • Model-independent fluorescence polarization for measuring order in a biological assembly
    • Burghardt, T. P. Model-independent fluorescence polarization for measuring order in a biological assembly. Biopolymers 23, 2383-2406 (1984).
    • (1984) Biopolymers , vol.23 , pp. 2383-2406
    • Burghardt, T.P.1
  • 14
    • 0033029278 scopus 로고    scopus 로고
    • Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers
    • Dale, R. E. et al. Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers. Biophys. J. 76, 1606-1618 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 1606-1618
    • Dale, R.E.1
  • 15
    • 0347171399 scopus 로고
    • Mathematics of the polarized-fluorescence experiment
    • Desper, C. R. & Kimura, I. Mathematics of the polarized-fluorescence experiment. J. Appl. Phys. 38, 4225-4233 (1967).
    • (1967) J. Appl. Phys. , vol.38 , pp. 4225-4233
    • Desper, C.R.1    Kimura, I.2
  • 17
    • 0018389150 scopus 로고
    • Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization
    • Axelrod, D. Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization. Biophys. J. 26, 557-573 (1979).
    • (1979) Biophys. J. , vol.26 , pp. 557-573
    • Axelrod, D.1
  • 18
    • 0034053143 scopus 로고    scopus 로고
    • One- and two-photon excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins
    • Volkmer, A., Subramaniam, V., Birch, D. J. & Jovin, T. M. One- and two-photon excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins. Biophys. J. 78, 1589-1598 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 1589-1598
    • Volkmer, A.1    Subramaniam, V.2    Birch, D.J.3    Jovin, T.M.4
  • 19
    • 0033615015 scopus 로고    scopus 로고
    • Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
    • Corrie, J. E. et al. Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction. Nature 400, 425-430 (1999).
    • (1999) Nature , vol.400 , pp. 425-430
    • Corrie, J.E.1
  • 20
    • 0037763890 scopus 로고    scopus 로고
    • Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment
    • Rocheleau, J. V., Edidin, M. & Piston, D. W. Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment. Biophys. J. 84, 4078-4086 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 4078-4086
    • Rocheleau, J.V.1    Edidin, M.2    Piston, D.W.3
  • 21
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M. & Stock, J. Predicting coiled coils from protein sequences. Science 252, 1162-1164 (1991).
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 22
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G. & Phillips, G. N. Jr. The molecular structure of green fluorescent protein. Nature Biotechnol. 14, 1246-1251 (1996).
    • (1996) Nature Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 23
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M. et al. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395 (1996).
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1
  • 24
    • 0030661707 scopus 로고    scopus 로고
    • Deletions of the Aequorea victoria green fluorescent protein define the minimal domain required for fluorescence
    • Li, X. et al. Deletions of the Aequorea victoria green fluorescent protein define the minimal domain required for fluorescence. J. Biol. Chem. 272, 28545-28549 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28545-28549
    • Li, X.1
  • 25
    • 0037345639 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of septin dynamics during the cell cycle
    • Dobbelaere, J., Gentry, M. S., Hallberg, R. L. & Barral, Y. Phosphorylation-dependent regulation of septin dynamics during the cell cycle. Dev. Cell 4, 345-357 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 345-357
    • Dobbelaere, J.1    Gentry, M.S.2    Hallberg, R.L.3    Barral, Y.4
  • 26
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • Caviston, J. P., Longtine, M., Pringle, J. R. & Bi, E. The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol. Biol. Cell 14, 4051-4066 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4051-4066
    • Caviston, J.P.1    Longtine, M.2    Pringle, J.R.3    Bi, E.4
  • 27
    • 0037081643 scopus 로고    scopus 로고
    • In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other
    • Schmidt, M., Bowers, B., Varma, A., Roh, D. H. & 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. 115, 293-302 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 293-302
    • Schmidt, M.1    Bowers, B.2    Varma, A.3    Roh, D.H.4    Cabib, E.5
  • 28
    • 0032774449 scopus 로고    scopus 로고
    • Actin protofilament orientation at the erythrocyte membrane
    • Picart, C. & Discher, D. E. Actin protofilament orientation at the erythrocyte membrane. Biophys. J. 77, 865-878 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 865-878
    • Picart, C.1    Discher, D.E.2
  • 29
    • 0036270970 scopus 로고    scopus 로고
    • Use of green fluorescent protein in living yeast cells
    • Tatchell, K. & Robinson, L. C. Use of green fluorescent protein in living yeast cells. Methods Enzymol. 351, 661-683 (2002)
    • (2002) Methods Enzymol. , vol.351 , pp. 661-683
    • Tatchell, K.1    Robinson, L.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.