메뉴 건너뛰기




Volumn 111, Issue 16, 2014, Pages 5860-5865

Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin

Author keywords

Cytoskeletal regulation; TIRF microscopy; Tubulin polymerization

Indexed keywords

BINDING PROTEIN; CALMODULIN REGULATED SPECTRIN ASSOCIATED PROTEIN; CALMODULIN REGULATED SPECTRIN ASSOCIATED PROTEIN 2; CALMODULIN REGULATED SPECTRIN ASSOCIATED PROTEIN 3; KINESIN; KINESIN 13; PATRONIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 84899072470     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1404133111     Document Type: Article
Times cited : (129)

References (39)
  • 1
    • 0027527453 scopus 로고
    • Localization of an exchangeable GTP binding site at the plus end of microtubules
    • Mitchison TJ (1993) Localization of an exchangeable GTP binding site at the plus end of microtubules. Science 261(5124):1044-1047.
    • (1993) Science , vol.261 , Issue.5124 , pp. 1044-1047
    • Mitchison, T.J.1
  • 2
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T, Kirschner M (1984) Dynamic instability of microtubule growth. Nature 312(5991):237-242.
    • (1984) Nature , vol.312 , Issue.5991 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 4
    • 41149156427 scopus 로고    scopus 로고
    • Tracking the ends: A dynamic protein network controls the fate of microtubule tips
    • DOI 10.1038/nrm2369, PII NRM2369
    • Akhmanova A, Steinmetz MO (2008) Tracking the ends: A dynamic protein network controls the fate of microtubule tips. Nat Rev Mol Cell Biol 9(4):309-322. (Pubitemid 351430849)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 309-322
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 5
    • 0035906940 scopus 로고    scopus 로고
    • Microtubule "plus-end-tracking proteins": The end is just the beginning
    • DOI 10.1016/S0092-8674(01)00364-6
    • Schuyler SC, Pellman D (2001) Microtubule "plus-end-tracking proteins": The end is just the beginning. Cell 105(4):421-424. (Pubitemid 32520848)
    • (2001) Cell , vol.105 , Issue.4 , pp. 421-424
    • Schuyler, S.C.1    Pellman, D.2
  • 6
    • 43149111310 scopus 로고    scopus 로고
    • EB1 regulates microtubule dynamics and tubulin sheet closure in vitro
    • Vitre B, et al. (2008) EB1 regulates microtubule dynamics and tubulin sheet closure in vitro. Nat Cell Biol 10(4):415-421.
    • (2008) Nat Cell Biol , vol.10 , Issue.4 , pp. 415-421
    • Vitre, B.1
  • 7
    • 77953515706 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics by Bim1 and Bik1, the budding yeast members of the EB1 and CLIP-170 families of plus-end tracking proteins
    • Blake-Hodek KA, Cassimeris L, Huffaker TC (2010) Regulation of microtubule dynamics by Bim1 and Bik1, the budding yeast members of the EB1 and CLIP-170 families of plus-end tracking proteins. Mol Biol Cell 21(12):2013-2023.
    • (2010) Mol Biol Cell , vol.21 , Issue.12 , pp. 2013-2023
    • Blake-Hodek, K.A.1    Cassimeris, L.2    Huffaker, T.C.3
  • 8
    • 84859736946 scopus 로고    scopus 로고
    • EBs recognize a nucleotide-dependent structural cap at growing microtubule ends
    • Maurer SP, Fourniol FJ, Bohner G, Moores CA, Surrey T (2012) EBs recognize a nucleotide-dependent structural cap at growing microtubule ends. Cell 149(2):371-382.
    • (2012) Cell , vol.149 , Issue.2 , pp. 371-382
    • Maurer, S.P.1    Fourniol, F.J.2    Bohner, G.3    Moores, C.A.4    Surrey, T.5
  • 9
    • 67650627616 scopus 로고    scopus 로고
    • An EB1-binding motif acts as a microtubule tip localization signal
    • Honnappa S, et al. (2009) An EB1-binding motif acts as a microtubule tip localization signal. Cell 138(2):366-376.
    • (2009) Cell , vol.138 , Issue.2 , pp. 366-376
    • Honnappa, S.1
  • 10
    • 0033792092 scopus 로고    scopus 로고
    • Control of microtubule dynamics by the antagonistic activities of XMAP215 and XKCM1 in Xenopus egg extracts
    • Tournebize R, et al. (2000) Control of microtubule dynamics by the antagonistic activities of XMAP215 and XKCM1 in Xenopus egg extracts. Nat Cell Biol 2(1):13-19.
    • (2000) Nat Cell Biol , vol.2 , Issue.1 , pp. 13-19
    • Tournebize, R.1
  • 11
    • 37649004096 scopus 로고    scopus 로고
    • XMAP215 is a processive microtubule polymerase
    • Brouhard GJ, et al. (2008) XMAP215 is a processive microtubule polymerase. Cell 132(1):79-88.
    • (2008) Cell , vol.132 , Issue.1 , pp. 79-88
    • Brouhard, G.J.1
  • 12
    • 0037292454 scopus 로고    scopus 로고
    • The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends
    • DOI 10.1016/S1097-2765(03)00049-2
    • Hunter AW, et al. (2003) The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. Mol Cell 11(2):445-457. (Pubitemid 36293838)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 445-457
    • Hunter, A.W.1    Caplow, M.2    Coy, D.L.3    Hancock, W.O.4    Diez, S.5    Wordeman, L.6    Howard, J.7
  • 15
    • 0037452096 scopus 로고    scopus 로고
    • Dynamics and mechanics of the microtubule plus end
    • DOI 10.1038/nature01600
    • Howard J, Hyman AA (2003) Dynamics and mechanics of the microtubule plus end. Nature 422(6933):753-758. (Pubitemid 36514118)
    • (2003) Nature , vol.422 , Issue.6933 , pp. 753-758
    • Howard, J.1    Hyman, A.A.2
  • 17
    • 0030727892 scopus 로고    scopus 로고
    • Actomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling
    • DOI 10.1083/jcb.139.2.417
    • Waterman-Storer CM, Salmon ED (1997) Actomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling. J Cell Biol 139(2):417-434. (Pubitemid 27459314)
    • (1997) Journal of Cell Biology , vol.139 , Issue.2 , pp. 417-434
    • Waterman-Storer, C.M.1    Salmon, E.D.2
  • 18
    • 0000885332 scopus 로고    scopus 로고
    • Non-centrosomal microtubule formation and measurement of minus end microtubule dynamics in A498 cells
    • Yvon AM, Wadsworth P (1997) Non-centrosomal microtubule formation and measurement of minus end microtubule dynamics in A498 cells. J Cell Sci 110(pt 19):2391-2401.
    • (1997) J Cell Sci , vol.110 , Issue.PART 19 , pp. 2391-2401
    • Yvon, A.M.1    Wadsworth, P.2
  • 20
    • 0032803940 scopus 로고    scopus 로고
    • Contribution of plus and minus end pathways to microtubule turnover
    • Vorobjev IA, Rodionov VI, Maly IV, Borisy GG (1999) Contribution of plus and minus end pathways to microtubule turnover. J Cell Sci 112(pt 14):2277-2289. (Pubitemid 29381019)
    • (1999) Journal of Cell Science , vol.112 , Issue.14 , pp. 2277-2289
    • Vorobjev, I.A.1    Rodionov, V.I.2    Maly, I.V.3    Borisy, G.G.4
  • 22
    • 77957817006 scopus 로고    scopus 로고
    • Patronin regulates the microtubule network by protecting microtubule minus ends
    • Goodwin SS, Vale RD (2010) Patronin regulates the microtubule network by protecting microtubule minus ends. Cell 143(2):263-274.
    • (2010) Cell , vol.143 , Issue.2 , pp. 263-274
    • Goodwin, S.S.1    Vale, R.D.2
  • 23
    • 84886894587 scopus 로고    scopus 로고
    • Patronin mediates a switch from kinesin-13-dependent poleward flux to anaphase B spindle elongation
    • Wang H, Brust-Mascher I, Civelekoglu-Scholey G, Scholey JM (2013) Patronin mediates a switch from kinesin-13-dependent poleward flux to anaphase B spindle elongation. J Cell Biol 203(1):35-46.
    • (2013) J Cell Biol , vol.203 , Issue.1 , pp. 35-46
    • Wang, H.1    Brust-Mascher, I.2    Civelekoglu-Scholey, G.3    Scholey, J.M.4
  • 24
    • 56349123945 scopus 로고    scopus 로고
    • Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts
    • Meng W, Mushika Y, Ichii T, Takeichi M (2008) Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts. Cell 135(5):948-959.
    • (2008) Cell , vol.135 , Issue.5 , pp. 948-959
    • Meng, W.1    Mushika, Y.2    Ichii, T.3    Takeichi, M.4
  • 25
    • 84897925038 scopus 로고    scopus 로고
    • CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions
    • Shahbazi MN, et al. (2013) CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions. J Cell Biol 203(6):1043-1061.
    • (2013) J Cell Biol , vol.203 , Issue.6 , pp. 1043-1061
    • Shahbazi, M.N.1
  • 26
    • 68949211177 scopus 로고    scopus 로고
    • The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins
    • Baines AJ, et al. (2009) The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins. Mol Biol Evol 26(9):2005-2014.
    • (2009) Mol Biol Evol , vol.26 , Issue.9 , pp. 2005-2014
    • Baines, A.J.1
  • 27
    • 84897019937 scopus 로고    scopus 로고
    • A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth
    • King MD, et al. (2014) A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth. J Neurochem 128(3):391-402.
    • (2014) J Neurochem , vol.128 , Issue.3 , pp. 391-402
    • King, M.D.1
  • 28
    • 84870587308 scopus 로고    scopus 로고
    • Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of noncentrosomal microtubules
    • Tanaka N, Meng W, Nagae S, Takeichi M (2012) Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of noncentrosomal microtubules. Proc Natl Acad Sci USA 109(49):20029-20034.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.49 , pp. 20029-20034
    • Tanaka, N.1    Meng, W.2    Nagae, S.3    Takeichi, M.4
  • 29
    • 84877001696 scopus 로고    scopus 로고
    • Non-centrosomal microtubules regulate F-actin organization through the suppression of GEF-H1 activity
    • Nagae S, Meng W, Takeichi M (2013) Non-centrosomal microtubules regulate F-actin organization through the suppression of GEF-H1 activity. Genes Cells 18(5):387-396.
    • (2013) Genes Cells , vol.18 , Issue.5 , pp. 387-396
    • Nagae, S.1    Meng, W.2    Takeichi, M.3
  • 30
    • 84898754062 scopus 로고    scopus 로고
    • The Caenorhabditis elegans microtubule minus-end binding homolog PTRN-1 stabilizes synapses and neurites
    • Marcette JD, Chen JJ, Nonet ML (2014) The Caenorhabditis elegans microtubule minus-end binding homolog PTRN-1 stabilizes synapses and neurites. Elife 3:e01637.
    • (2014) Elife , vol.3
    • Marcette, J.D.1    Chen, J.J.2    Nonet, M.L.3
  • 31
    • 84898723545 scopus 로고    scopus 로고
    • PTRN-1, a microtubule minus end-binding CAMSAP homolog, promotes microtubule function in Caenorhabditis elegans neurons
    • Richardson CE, et al. (2014) PTRN-1, a microtubule minus end-binding CAMSAP homolog, promotes microtubule function in Caenorhabditis elegans neurons. Elife 3:e01498.
    • (2014) Elife , vol.3
    • Richardson, C.E.1
  • 32
    • 84893542408 scopus 로고    scopus 로고
    • Microtubule minus-end stabilization by polymerization-driven CAMSAP deposition
    • Jiang K, et al. (2014) Microtubule minus-end stabilization by polymerization-driven CAMSAP deposition. Dev Cell 28(3):295-309.
    • (2014) Dev Cell , vol.28 , Issue.3 , pp. 295-309
    • Jiang, K.1
  • 33
    • 77955657138 scopus 로고    scopus 로고
    • Microtubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry
    • Kollman JM, Polka JK, Zelter A, Davis TN, Agard DA (2010) Microtubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry. Nature 466(7308):879-882.
    • (2010) Nature , vol.466 , Issue.7308 , pp. 879-882
    • Kollman, J.M.1    Polka, J.K.2    Zelter, A.3    Davis, T.N.4    Agard, D.A.5
  • 34
    • 0037138396 scopus 로고    scopus 로고
    • Functional plasticity of CH domains
    • DOI 10.1016/S0014-5793(01)03240-9, PII S0014579301032409
    • Gimona M, Djinovic-Carugo K, Kranewitter WJ, Winder SJ (2002) Functional plasticity of CH domains. FEBS Lett 513(1):98-106. (Pubitemid 34242985)
    • (2002) FEBS Letters , vol.513 , Issue.1 , pp. 98-106
    • Gimona, M.1    Djinovic-Carugo, K.2    Kranewitter, W.J.3    Winder, S.J.4
  • 36
    • 77955301639 scopus 로고    scopus 로고
    • Microtubule dynamics reconstituted in vitro and imaged by single-molecule fluorescence microscopy
    • Gell C, et al. (2010) Microtubule dynamics reconstituted in vitro and imaged by single-molecule fluorescence microscopy. Methods Cell Biol 95:221-245.
    • (2010) Methods Cell Biol , vol.95 , pp. 221-245
    • Gell, C.1
  • 37
    • 41449108157 scopus 로고    scopus 로고
    • An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments
    • Aitken CE, Marshall RA, Puglisi JD (2008) An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments. Biophys J 94(5):1826-1835.
    • (2008) Biophys J , vol.94 , Issue.5 , pp. 1826-1835
    • Aitken, C.E.1    Marshall, R.A.2    Puglisi, J.D.3
  • 38
    • 67649580185 scopus 로고    scopus 로고
    • Motor-dependent microtubule disassembly driven by tubulin tyrosination
    • Peris L, et al. (2009) Motor-dependent microtubule disassembly driven by tubulin tyrosination. J Cell Biol 185(7):1159-1166.
    • (2009) J Cell Biol , vol.185 , Issue.7 , pp. 1159-1166
    • Peris, L.1
  • 39
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: An open-source platform for biological-image analysis
    • Schindelin J, et al. (2012) Fiji: An open-source platform for biological-image analysis. Nat Methods 9(7):676-682.
    • (2012) Nat Methods , vol.9 , Issue.7 , pp. 676-682
    • Schindelin, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.