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Volumn 185, Issue 7, 2009, Pages 1159-1166

Motor-dependent microtubule disassembly driven by tubulin tyrosination

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; CARBOXYPEPTIDASE; NOCODAZOLE;

EID: 67649580185     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200902142     Document Type: Article
Times cited : (261)

References (32)
  • 3
    • 59449100831 scopus 로고    scopus 로고
    • CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
    • Bieling, P., S. Kandels-Lewis, I.A. Telley, J. van Dijk, C. Janke, and T. Surrey. 2008. CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites. J. Cell Biol. 183:1223-1233.
    • (2008) J. Cell Biol. , vol.183 , pp. 1223-1233
    • Bieling, P.1    Kandels-Lewis, S.2    Telley, I.A.3    Van Dijk, J.4    Janke, C.5    Surrey, T.6
  • 5
    • 0021169663 scopus 로고
    • Microfilament-organizing centers in areas of cell contact: Cytoskeletal interactions during cell attachment and locomotion
    • Geiger, B., Z. Avnur, G. Rinnerthaler, H. Hinssen, and V.J. Small. 1984. Microfilament-organizing centers in areas of cell contact: cytoskeletal interactions during cell attachment and locomotion. J. Cell Biol. 99:83s-91s. (Pubitemid 14030782)
    • (1984) Journal of Cell Biology , vol.99 , Issue.1 II
    • Geiger, B.1    Avnur, Z.2    Rinnerthaler, G.3
  • 6
    • 33748158378 scopus 로고    scopus 로고
    • Plus end-specific depolymerase activity of Kip3, a kinesin-8 protein, explains its role in positioning the yeast mitotic spindle
    • DOI 10.1038/ncb1457, PII NCB1457
    • Gupta, M.L. Jr., P. Carvalho, D.M. Roof, and D. Pellman. 2006. Plus end-specific depolymerase activity of Kip3, a kinesin-8 protein, explains its role in positioning the yeast mitotic spindle. Nat. Cell Biol. 8:913-923. (Pubitemid 44314722)
    • (2006) Nature Cell Biology , vol.8 , Issue.9 , pp. 913-923
    • Gupta Jr., M.L.1    Carvalho, P.2    Roof, D.M.3    Pellman, D.4
  • 7
    • 39149121834 scopus 로고    scopus 로고
    • Tubulin modifications and their cellular functions
    • Hammond, J.W., D. Cai, and K.J. Verhey. 2008. Tubulin modifications and their cellular functions. Curr. Opin. Cell Biol. 20:71-76.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 8
    • 47749138578 scopus 로고    scopus 로고
    • Effects of anti-microtubule agents on microtubule organization in cells lacking the kinesin-13 MCAK
    • Hedrick, D.G., J.R. Stout, and C.E. Walczak. 2008. Effects of anti-microtubule agents on microtubule organization in cells lacking the kinesin-13 MCAK. Cell Cycle. 7:2146-2156. (Pubitemid 352031517)
    • (2008) Cell Cycle , vol.7 , Issue.14 , pp. 2146-2156
    • Hedrick, D.G.1    Stout, J.R.2    Walczak, C.E.3
  • 9
    • 33646950699 scopus 로고    scopus 로고
    • The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends
    • DOI 10.1038/nature04736, PII N04736
    • Helenius, J., G. Brouhard, Y. Kalaidzidis, S. Diez, and J. Howard. 2006. The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends. Nature. 441:115-119. (Pubitemid 43827962)
    • (2006) Nature , vol.441 , Issue.1 , pp. 115-119
    • Helenius, J.1    Brouhard, G.2    Kalaidzidis, Y.3    Diez, S.4    Howard, J.5
  • 10
    • 0043199576 scopus 로고    scopus 로고
    • Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension
    • DOI 10.1016/S0092-8674(03)00522-1
    • Homma, N., Y. Takei, Y. Tanaka, T. Nakata, S. Terada, M. Kikkawa, Y. Noda, and N. Hirokawa. 2003. Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension. Cell. 114:229-239. (Pubitemid 36936916)
    • (2003) Cell , vol.114 , Issue.2 , pp. 229-239
    • Homma, N.1    Takei, Y.2    Tanaka, Y.3    Nakata, T.4    Terada, S.5    Kikkawa, M.6    Noda, Y.7    Hirokawa, N.8
  • 11
    • 44349151502 scopus 로고    scopus 로고
    • Mitotic centromere-associated kinesin is a novel marker for prognosis and lymph node metastasis in colorectal cancer
    • DOI 10.1038/sj.bjc.6604379, PII 6604379
    • Ishikawa, K., Y. Kamohara, F. Tanaka, N. Haraguchi, K. Mimori, H. Inoue, and M. Mori. 2008. Mitotic centromere-associated kinesin is a novel marker for prognosis and lymph node metastasis in colorectal cancer. Br. J. Cancer. 98:1824-1829. (Pubitemid 351748844)
    • (2008) British Journal of Cancer , vol.98 , Issue.11 , pp. 1824-1829
    • Ishikawa, K.1    Kamohara, Y.2    Tanaka, F.3    Haraguchi, N.4    Mimori, K.5    Inoue, H.6    Mori, M.7
  • 12
    • 0023877365 scopus 로고
    • Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level
    • Khawaja, S., G.G. Gundersen, and J.C. Bulinski. 1988. Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level. J. Cell Biol. 106:141-149. (Pubitemid 18051401)
    • (1988) Journal of Cell Biology , vol.106 , Issue.1 , pp. 141-149
    • Khawaja, S.1    Gundersen, G.G.2    Bulinski, J.C.3
  • 13
    • 0036678201 scopus 로고    scopus 로고
    • The microtubule-destabilizing kinesin XKCM1 regulates microtubule dynamic instability in cells
    • DOI 10.1091/mbc.E01-12-0143
    • Kline-Smith, S.L., and C.E. Walczak. 2002. The microtubule-destabilizing kinesin XKCM1 regulates microtubule dynamic instability in cells. Mol. Biol. Cell. 13:2718-2731. (Pubitemid 34907098)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.8 , pp. 2718-2731
    • Kline-Smith, S.L.1    Walczak, C.E.2
  • 15
    • 0035860717 scopus 로고    scopus 로고
    • Molecular Dissection of the Microtubule Depolymerizing Activity of Mitotic Centromere-associated Kinesin
    • DOI 10.1074/jbc.M106626200
    • Maney, T., M. Wagenbach, and L. Wordeman. 2001. Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin. J. Biol. Chem. 276:34753-34758. (Pubitemid 37384474)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.37 , pp. 34753-34758
    • Maney, T.1    Wagenbach, M.2    Wordeman, L.3
  • 16
    • 34547726131 scopus 로고    scopus 로고
    • The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells
    • DOI 10.1091/mbc.E07-02-0110
    • Manning, A.L., N.J. Ganem, S.F. Bakhoum, M. Wagenbach, L. Wordeman, and D.A. Compton. 2007. The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells. Mol. Biol. Cell. 18:2970-2979. (Pubitemid 47235304)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.8 , pp. 2970-2979
    • Manning, A.L.1    Ganem, N.J.2    Bakhoum, S.F.3    Wagenbach, M.4    Wordeman, L.5    Compton, D.A.6
  • 17
    • 14744287039 scopus 로고    scopus 로고
    • Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase
    • DOI 10.1038/ncb1222
    • Mennella, V., G.C. Rogers, S.L. Rogers, D.W. Buster, R.D. Vale, and D.J. Sharp. 2005. Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase. Nat. Cell Biol. 7:235-245. (Pubitemid 40331124)
    • (2005) Nature Cell Biology , vol.7 , Issue.3 , pp. 235-245
    • Mennella, V.1    Rogers, G.C.2    Rogers, S.L.3    Buster, D.W.4    Vale, R.D.5    Sharp, D.J.6
  • 19
    • 4644339944 scopus 로고    scopus 로고
    • C-terminus of mitotic centromere-associated kinesin (MCAK) inhibits its lattice-stimulated ATPase activity
    • DOI 10.1042/BJ20040736
    • Moore, A., and L. Wordeman. 2004. C-terminus of mitotic centromere-associated kinesin (MCAK) inhibits its lattice-stimulated ATPase activity. Biochem. J. 383:227-235. (Pubitemid 39446683)
    • (2004) Biochemical Journal , vol.383 , Issue.2 , pp. 227-235
    • Moore, A.1    Wordeman, L.2
  • 21
    • 33846999330 scopus 로고    scopus 로고
    • Action and interactions at microtubule ends
    • DOI 10.1007/s00018-007-6360-3
    • Morrison, E.E. 2007. Action and interactions at microtubule ends. Cell. Mol. Life Sci. 64:307-317. (Pubitemid 46440204)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.3 , pp. 307-317
    • Morrison, E.E.1
  • 22
    • 4143095005 scopus 로고    scopus 로고
    • MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro
    • DOI 10.1016/j.febslet.2004.06.093, PII S0014579304008695
    • Newton, C.N., M. Wagenbach, Y. Ovechkina, L. Wordeman, and L. Wilson. 2004. MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro. FEBS Lett. 572:80-84. (Pubitemid 39092517)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 80-84
    • Newton, C.N.1    Wagenbach, M.2    Ovechkina, Y.3    Wordeman, L.4    Wilson, L.5
  • 23
    • 34249655122 scopus 로고    scopus 로고
    • Nonredundant Functions of Kinesin-13s during Meiotic Spindle Assembly
    • DOI 10.1016/j.cub.2007.04.057, PII S0960982207013371
    • Ohi, R., K. Burbank, Q. Liu, and T.J. Mitchison. 2007. Nonredundant functions of Kinesin-13s during meiotic spindle assembly. Curr. Biol. 17:953-959. (Pubitemid 46829840)
    • (2007) Current Biology , vol.17 , Issue.11 , pp. 953-959
    • Ohi, R.1    Burbank, K.2    Liu, Q.3    Mitchison, T.J.4
  • 24
    • 0024583552 scopus 로고
    • Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography
    • DOI 10.1021/bi00432a050
    • Paturle, L., J. Wehland, R.L. Margolis, and D. Job. 1989. Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography. Biochemistry. 28:2698-2704. (Pubitemid 19094391)
    • (1989) Biochemistry , vol.28 , Issue.6 , pp. 2698-2704
    • Paturle, L.1    Wehland, J.2    Margolis, R.L.3    Job, D.4
  • 25
    • 33847358842 scopus 로고    scopus 로고
    • Cell biology: Aneuploidy and cancer
    • DOI 10.1038/446038a, PII 446038A
    • Pellman, D. 2007. Cell biology: aneuploidy and cancer. Nature. 446:38-39. (Pubitemid 46348036)
    • (2007) Nature , vol.446 , Issue.7131 , pp. 38-39
    • Pellman, D.1
  • 27
    • 0028887946 scopus 로고
    • Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins
    • Saoudi, Y., I. Paintrand, L. Multigner, and D. Job. 1995. Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins. J. Cell Sci. 108:357-367.
    • (1995) J. Cell Sci. , vol.108 , pp. 357-367
    • Saoudi, Y.1    Paintrand, I.2    Multigner, L.3    Job, D.4
  • 28
  • 29
    • 54249131103 scopus 로고    scopus 로고
    • Capturing protein tails by CAP-Gly domains
    • Steinmetz, M.O., and A. Akhmanova. 2008. Capturing protein tails by CAP-Gly domains. Trends Biochem. Sci. 33:535-545.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 535-545
    • Steinmetz, M.O.1    Akhmanova, A.2
  • 30
    • 33749506269 scopus 로고    scopus 로고
    • Genome-wide genetic analysis of polyploidy in yeast
    • DOI 10.1038/nature05178, PII NATURE05178
    • Storchova, Z., A. Breneman, J. Cande, J. Dunn, K. Burbank, E. O'Toole, and D. Pellman. 2006. Genome-wide genetic analysis of polyploidy in yeast. Nature. 443:541-547. (Pubitemid 44527285)
    • (2006) Nature , vol.443 , Issue.7111 , pp. 541-547
    • Storchova, Z.1    Breneman, A.2    Cande, J.3    Dunn, J.4    Burbank, K.5    O'Toole, E.6    Pellman, D.7
  • 31
    • 58149203506 scopus 로고    scopus 로고
    • A kinesin-13 mutant catalytically depolymerizes microtubules in ADP
    • Wagenbach, M., S. Domnitz, L. Wordeman, and J. Cooper. 2008. A kinesin-13 mutant catalytically depolymerizes microtubules in ADP. J. Cell Biol. 183:617-623.
    • (2008) J. Cell Biol. , vol.183 , pp. 617-623
    • Wagenbach, M.1    Domnitz, S.2    Wordeman, L.3    Cooper, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.