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Volumn 115, Issue 21, 2002, Pages 4053-4059

The mitotic-spindle-associated protein astrin is essential for progression through mitosis

Author keywords

Astrin; Coiled coil; Microtubules; Mitotic spindle; RNA interference

Indexed keywords

ASTRIN; BUFFER; CELL CYCLE PROTEIN; RECOMBINANT PROTEIN; RNA; UNCLASSIFIED DRUG; SPAG5 PROTEIN, HUMAN;

EID: 0036860494     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00088     Document Type: Review
Times cited : (73)

References (42)
  • 1
    • 0034664766 scopus 로고    scopus 로고
    • CENP-E as an essential component of the mitotic checkpoint in vitro
    • Abrieu, A., Kahana, J. A., Wood, K. W. and Cleveland, D. W. (2000). CENP-E as an essential component of the mitotic checkpoint in vitro. Cell 102, 817-826.
    • (2000) Cell , vol.102 , pp. 817-826
    • Abrieu, A.1    Kahana, J.A.2    Wood, K.W.3    Cleveland, D.W.4
  • 2
    • 0028915798 scopus 로고
    • Proline-rich sequences that bind to Src homology 3 domains with individual specificities
    • Alexandropoulos, K., Cheng, G. and Baltimore, D. (1995). Proline-rich sequences that bind to Src homology 3 domains with individual specificities. Proc. Natl. Acad. Sci. USA 92, 3110-3114.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3110-3114
    • Alexandropoulos, K.1    Cheng, G.2    Baltimore, D.3
  • 3
    • 0019023345 scopus 로고
    • Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA
    • Auffrey, C. and Rougeon, F. (1980). Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur J. Cell Biol. 107, 303-314.
    • (1980) Eur J. Cell Biol. , vol.107 , pp. 303-314
    • Auffrey, C.1    Rougeon, F.2
  • 4
    • 0035916323 scopus 로고    scopus 로고
    • Chromosome movement: Dynein-out at the kinetochore
    • Banks, J. D. and Heald, R. (2001). Chromosome movement: dynein-out at the kinetochore. Curr. Biol. 11, R128-R131.
    • (2001) Curr. Biol. , vol.11
    • Banks, J.D.1    Heald, R.2
  • 5
    • 0029449733 scopus 로고
    • Motor proteins 1: Kinesins
    • Bloom, G. S. and Endow, S. A. (1995). Motor proteins 1: kinesins. Protein Profile 2, 1105-1171.
    • (1995) Protein Profile , vol.2 , pp. 1105-1171
    • Bloom, G.S.1    Endow, S.A.2
  • 7
    • 0033782853 scopus 로고    scopus 로고
    • Spindle assembly in animal cells
    • Compton, D. A. (2000). Spindle assembly in animal cells. Annu. Rev. Biochem. 69, 95-114.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 95-114
    • Compton, D.A.1
  • 8
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 9
    • 0035694237 scopus 로고    scopus 로고
    • Identification of essential genes in cultured mammalian cells using small interfering RNAs
    • Harborth, J., Elbashir, S. M., Bechert, K., Tuschl, T. and Weber, K. (2001). Identification of essential genes in cultured mammalian cells using small interfering RNAs. J. Cell Sci. 114, 4557-4565.
    • (2001) J. Cell Sci. , vol.114 , pp. 4557-4565
    • Harborth, J.1    Elbashir, S.M.2    Bechert, K.3    Tuschl, T.4    Weber, K.5
  • 10
    • 0025239701 scopus 로고
    • The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins; use of site-specific mutagenesis and recombinant protein expression
    • Hatzfeld, M. and Weber, K. (1990). The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins; use of site-specific mutagenesis and recombinant protein expression. J. Cell Biol. 110, 1199-1210.
    • (1990) J. Cell Biol. , vol.110 , pp. 1199-1210
    • Hatzfeld, M.1    Weber, K.2
  • 11
    • 0029836330 scopus 로고    scopus 로고
    • Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts
    • Heald, R., Tournebize, R., Blank, T., Sandaltzopoulos, R., Becker, P., Hyman, A. and Karsenti, E. (1996). Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts. Nature 382, 420-425.
    • (1996) Nature , vol.382 , pp. 420-425
    • Heald, R.1    Tournebize, R.2    Blank, T.3    Sandaltzopoulos, R.4    Becker, P.5    Hyman, A.6    Karsenti, E.7
  • 12
    • 0032005975 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins in organelle transport and cell division
    • Hirokawa, N., Noda, Y. and Okada, Y. (1998a). Kinesin and dynein superfamily proteins in organelle transport and cell division. Curr. Opin. Cell Biol. 10, 60-73.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 60-73
    • Hirokawa, N.1    Noda, Y.2    Okada, Y.3
  • 13
    • 0032005975 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins in organelle transport and cell division
    • Hirokawa, N., Noda, Y. and Okada, Y. (1998b). Kinesin and dynein superfamily proteins in organelle transport and cell division. Curr. Opin. Cell Biol. 10, 60-73.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 60-73
    • Hirokawa, N.1    Noda, Y.2    Okada, Y.3
  • 14
    • 0033569597 scopus 로고    scopus 로고
    • Three-dimensional structure of motor molecules
    • Hirose, K. and Amos, L. A. (1999). Three-dimensional structure of motor molecules. Cell Mol. Life Sci. 56, 184-199.
    • (1999) Cell Mol. Life Sci. , vol.56 , pp. 184-199
    • Hirose, K.1    Amos, L.A.2
  • 15
    • 0035945356 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin drives kinetochore protein transport to the spindle poles and has a role in mitotic spindle checkpoint inactivation
    • Howell, B. J., McEwen, B. F., Canman, J. C., Hoffman, D. B., Farrar, E. M., Rieder, C. L. and Salmon, E. D. (2001). Cytoplasmic dynein/dynactin drives kinetochore protein transport to the spindle poles and has a role in mitotic spindle checkpoint inactivation. J. Cell Biol. 155, 1159-1172.
    • (2001) J. Cell Biol. , vol.155 , pp. 1159-1172
    • Howell, B.J.1    McEwen, B.F.2    Canman, J.C.3    Hoffman, D.B.4    Farrar, E.M.5    Rieder, C.L.6    Salmon, E.D.7
  • 16
    • 0032006024 scopus 로고    scopus 로고
    • Microtubule dynamics in living cells
    • Joshi, H. C. (1998). Microtubule dynamics in living cells. Curr Opin. Cell Biol. 10, 35-44.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 35-44
    • Joshi, H.C.1
  • 17
    • 0035913964 scopus 로고    scopus 로고
    • The mitotic spindle: A self-made machine
    • Karsenti, E. and Vernos, I. (2001). The mitotic spindle: a self-made machine. Science 294, 543-547.
    • (2001) Science , vol.294 , pp. 543-547
    • Karsenti, E.1    Vernos, I.2
  • 18
    • 0033693656 scopus 로고    scopus 로고
    • A kinesin family tree
    • Kim, A. J. and Endow, S. A. (2000). A kinesin family tree. J. Cell Sci. 113, 3681-3682.
    • (2000) J. Cell Sci. , vol.113 , pp. 3681-3682
    • Kim, A.J.1    Endow, S.A.2
  • 19
    • 0032854874 scopus 로고    scopus 로고
    • Universal and unique features of kinesin motors: Insights from a comparison of fungal and animal conventional kinesins
    • Kirchner, J., Woehlke, G. and Schliwa, M. (1999). Universal and unique features of kinesin motors: insights from a comparison of fungal and animal conventional kinesins. Biol. Chem. 380, 915-921.
    • (1999) Biol. Chem. , vol.380 , pp. 915-921
    • Kirchner, J.1    Woehlke, G.2    Schliwa, M.3
  • 20
    • 0028891856 scopus 로고
    • Antibodies to the kinesin motor domain and CENP-E inhibit microtubule depolymerization-dependent movement of chromosomes in vitro
    • Lombillo, V. A., Nislow, C., Yen, T. J., Gelfand, V. I. and McIntosh, J. R. (1995). Antibodies to the kinesin motor domain and CENP-E inhibit microtubule depolymerization-dependent movement of chromosomes in vitro. J. Cell Biol. 128, 107-115.
    • (1995) J. Cell Biol. , vol.128 , pp. 107-115
    • Lombillo, V.A.1    Nislow, C.2    Yen, T.J.3    Gelfand, V.I.4    McIntosh, J.R.5
  • 21
    • 0035807883 scopus 로고    scopus 로고
    • Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein
    • Mack, G. J. and Compton, D. A. (2001). Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein. Proc. Natl. Acad Sci. USA 98, 14434-14439.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14434-14439
    • Mack, G.J.1    Compton, D.A.2
  • 22
    • 0032857015 scopus 로고    scopus 로고
    • The kinetochore of higher eucaryotes: A molecular view
    • Maney, T., Ginkel, L. M., Hunter, A. W. and Wordeman, L. (2000). The kinetochore of higher eucaryotes: a molecular view. Int. Rev. Cytol. 194, 67-131.
    • (2000) Int. Rev. Cytol. , vol.194 , pp. 67-131
    • Maney, T.1    Ginkel, L.M.2    Hunter, A.W.3    Wordeman, L.4
  • 23
    • 0035912738 scopus 로고    scopus 로고
    • All kinesin superfamily protein, KIF, genes in mouse and human
    • Miki, H., Setou, M., Kaneshiro, K. and Hirokawa, N. (2001). All kinesin superfamily protein, KIF, genes in mouse and human. Proc. Natl. Acad. Sci. USA 98, 7004-7011.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7004-7011
    • Miki, H.1    Setou, M.2    Kaneshiro, K.3    Hirokawa, N.4
  • 24
    • 0030111466 scopus 로고    scopus 로고
    • Kinesin proteins: A phylum of motors for microtubule-based motility
    • Moore, J. D. and Endow, S. A. (1996). Kinesin proteins: a phylum of motors for microtubule-based motility. Bioessays 18, 207-219.
    • (1996) Bioessays , vol.18 , pp. 207-219
    • Moore, J.D.1    Endow, S.A.2
  • 25
    • 0037813094 scopus 로고    scopus 로고
    • Self-organization of microtubules and motors
    • Nedelec, E. J., Surrey, T., Maggs, A. C. and Leibler, S. (1997). Self-organization of microtubules and motors. Nature 389, 305-308.
    • (1997) Nature , vol.389 , pp. 305-308
    • Nedelec, E.J.1    Surrey, T.2    Maggs, A.C.3    Leibler, S.4
  • 26
    • 0029294109 scopus 로고
    • YAC/P1 contigs defining the location of 56 microsatellite markers and several genes across 3.4cM interval on mouse chromosome 11
    • Nehls, M., Luno, K., Schorpp, M., Pfeifer, D., Krause, S., Matysiak-Scholze, U., Dierbach, H. and Boehm, T. (1995). YAC/P1 contigs defining the location of 56 microsatellite markers and several genes across 3.4cM interval on mouse chromosome 11. Mamm. Genome 6, 321-331.
    • (1995) Mamm. Genome , vol.6 , pp. 321-331
    • Nehls, M.1    Luno, K.2    Schorpp, M.3    Pfeifer, D.4    Krause, S.5    Matysiak-Scholze, U.6    Dierbach, H.7    Boehm, T.8
  • 27
    • 0029146196 scopus 로고
    • Kinetochore chemistry is sensitive to tension and may link mitotic forces to a cell cycle checkpoint
    • Nicklas, R. B., Ward, S. C. and Gorbsky, G. J. (1995). Kinetochore chemistry is sensitive to tension and may link mitotic forces to a cell cycle checkpoint. J. Cell Biol. 130, 929-939.
    • (1995) J. Cell Biol. , vol.130 , pp. 929-939
    • Nicklas, R.B.1    Ward, S.C.2    Gorbsky, G.J.3
  • 28
    • 0021125661 scopus 로고
    • Monoclonal antibodies specific for vimentin
    • Osborn, M., Debus, E. and Weber, K. (1984). Monoclonal antibodies specific for vimentin. Eur. J. Cell Biol. 34, 137-143.
    • (1984) Eur. J. Cell Biol. , vol.34 , pp. 137-143
    • Osborn, M.1    Debus, E.2    Weber, K.3
  • 29
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers, S. W. (1996). PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 30
    • 0029160299 scopus 로고
    • The checkpoint delaying anaphase in response to chormosome monoorientation is mediated by an inhibitory signal produced by unattached kinetochores
    • Rieder, C. L., Cole, R. W., Khodjakov, A. and Sluder, G. (1995). The checkpoint delaying anaphase in response to chormosome monoorientation is mediated by an inhibitory signal produced by unattached kinetochores. J. Cell Biol. 130, 941-948.
    • (1995) J. Cell Biol. , vol.130 , pp. 941-948
    • Rieder, C.L.1    Cole, R.W.2    Khodjakov, A.3    Sluder, G.4
  • 31
    • 0032146974 scopus 로고    scopus 로고
    • The vertebrate cell kinetochore and its roles during mitosis
    • Rieder, C. L. and Salmon, E. D. (1998). The vertebrate cell kinetochore and its roles during mitosis. Trends Cell Biol. 8, 310-318.
    • (1998) Trends Cell Biol. , vol.8 , pp. 310-318
    • Rieder, C.L.1    Salmon, E.D.2
  • 32
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., Wells, R. and Rechsteiner, M. (1986). Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234, 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 34
    • 0034949962 scopus 로고    scopus 로고
    • Testicular protein Spag5 has similarity to mitotic spindle protein Deepest and binds outer dense fiber protein Odf1
    • Shao, X., Xue, J. and van der Hoorn, F. A. (2001). Testicular protein Spag5 has similarity to mitotic spindle protein Deepest and binds outer dense fiber protein Odf1. Mol. Reprod. Dev. 59, 410-416.
    • (2001) Mol. Reprod. Dev. , vol.59 , pp. 410-416
    • Shao, X.1    Xue, J.2    van der Hoorn, F.A.3
  • 36
    • 0032795910 scopus 로고    scopus 로고
    • Phosphorylation by CDK1 regulates XMAP215 function in vitro
    • Vasquez, R. J., Gard, D. L. and Cassimeris, L. (1999). Phosphorylation by CDK1 regulates XMAP215 function in vitro. Cell Motil. Cytoskeleton 43, 310-321.
    • (1999) Cell Motil. Cytoskeleton , vol.43 , pp. 310-321
    • Vasquez, R.J.1    Gard, D.L.2    Cassimeris, L.3
  • 37
    • 13144251122 scopus 로고    scopus 로고
    • A model for the proposed roles of different microtubule-based motor proteins in establishing spindle bipolarity
    • Walczak, C. E., Vernos, I., Mitchison, T. J., Karsenti, E. and Heald, R. (1998). A model for the proposed roles of different microtubule-based motor proteins in establishing spindle bipolarity. Curr Biol. 8, 903-913.
    • (1998) Curr. Biol. , vol.8 , pp. 903-913
    • Walczak, C.E.1    Vernos, I.2    Mitchison, T.J.3    Karsenti, E.4    Heald, R.5
  • 38
    • 0035146128 scopus 로고    scopus 로고
    • The spindle: A dynamic assembly of microtubules and motors
    • Wittmann, T., Hyman, A. and Desai, A. (2001). The spindle: a dynamic assembly of microtubules and motors. Nat. Cell Biol. 3, E28-E34.
    • (2001) Nat. Cell Biol. , vol.3
    • Wittmann, T.1    Hyman, A.2    Desai, A.3
  • 39
    • 0036118383 scopus 로고    scopus 로고
    • Targeted disruption of the testicular SPAG5/deepest protein does not affect spermatogenesis or fertility
    • Xue, J., Tarnasky, H. A., Rancourt, D. E. and van Der Hoorn, F. A. (2002). Targeted disruption of the testicular SPAG5/deepest protein does not affect spermatogenesis or fertility. Mol. Cell Biol. 22, 1993-1997.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 1993-1997
    • Xue, J.1    Tarnasky, H.A.2    Rancourt, D.E.3    van Der Hoorn, F.A.4
  • 40
    • 0001665802 scopus 로고    scopus 로고
    • CENP-E forms a link between attachment of spindle microtubules to kinetochores and the mitotic checkpoint
    • Yao, X., Abrieu, A., Zheng, Y., Sullivan, K. F. and Cleveland, D. W. (2000). CENP-E forms a link between attachment of spindle microtubules to kinetochores and the mitotic checkpoint. Nat. Cell Biol. 2, 484-491.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 484-491
    • Yao, X.1    Abrieu, A.2    Zheng, Y.3    Sullivan, K.F.4    Cleveland, D.W.5
  • 41
    • 0026767624 scopus 로고
    • CENP-E is a putative kinetochore motor that accumulates just before mitosis
    • Yen, T. J., Li, G., Schaar, B. T., Szilak, I. and Cleveland, D. W. (1992). CENP-E is a putative kinetochore motor that accumulates just before mitosis. Nature 359, 536-539.
    • (1992) Nature , vol.359 , pp. 536-539
    • Yen, T.J.1    Li, G.2    Schaar, B.T.3    Szilak, I.4    Cleveland, D.W.5
  • 42
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu, H., Chen, Y. K., Feng, S., Dalgarno, D. C., Salmon, E. D. and Bloom, K. (1994). Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76, 933-945.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, Y.K.2    Feng, S.3    Dalgarno, D.C.4    Salmon, E.D.5    Bloom, K.6


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