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Volumn 22, Issue 1, 2010, Pages 88-95

Structural and mechanistic insights into microtubule end-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; BINDING PROTEIN; CYTOSKELETAL ASSOCIATED PROTEIN GLYCINE; END BINDING 1 PROTEIN; GLYCINE; NUCLEOTIDYLTRANSFERASE; PROTEIN CLIP 170; PROTEIN SKIP; PROTEIN XMAP215; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 75749107871     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2009.10.009     Document Type: Review
Times cited : (72)

References (47)
  • 2
    • 0141480958 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)
    • Hayashi I., and Ikura M. Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1). J Biol Chem 278 (2003) 36430-36434
    • (2003) J Biol Chem , vol.278 , pp. 36430-36434
    • Hayashi, I.1    Ikura, M.2
  • 4
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre P., Scheel J., Rickard J.E., and Kreis T.E. CLIP-170 links endocytic vesicles to microtubules. Cell 70 (1992) 887-900
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.E.3    Kreis, T.E.4
  • 5
    • 13944255721 scopus 로고    scopus 로고
    • Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end
    • Slep K.C., Rogers S.L., Elliott S.L., Ohkura H., Kolodziej P.A., and Vale R.D. Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end. J Cell Biol 168 (2005) 587-598
    • (2005) J Cell Biol , vol.168 , pp. 587-598
    • Slep, K.C.1    Rogers, S.L.2    Elliott, S.L.3    Ohkura, H.4    Kolodziej, P.A.5    Vale, R.D.6
  • 6
    • 67650627616 scopus 로고    scopus 로고
    • An EB1-binding motif acts as a microtubule tip localization signal
    • This study refines the determinants for EB1-SKIP-motif binding, reconstitutes EB1-depedent SKIP-motif plus end tracking in vitro and determines the structure of the MACF2 SKIP motif and the APC SKIP motif bound to the EB1 C-terminal dimerization domain using X-ray crystallography and NMR, respectively.
    • Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., et al. An EB1-binding motif acts as a microtubule tip localization signal. Cell 138 (2009) 366-376. This study refines the determinants for EB1-SKIP-motif binding, reconstitutes EB1-depedent SKIP-motif plus end tracking in vitro and determines the structure of the MACF2 SKIP motif and the APC SKIP motif bound to the EB1 C-terminal dimerization domain using X-ray crystallography and NMR, respectively.
    • (2009) Cell , vol.138 , pp. 366-376
    • Honnappa, S.1    Gouveia, S.M.2    Weisbrich, A.3    Damberger, F.F.4    Bhavesh, N.S.5    Jawhari, H.6    Grigoriev, I.7    van Rijssel, F.J.8    Buey, R.M.9    Lawera, A.10
  • 7
    • 0034617195 scopus 로고    scopus 로고
    • The interaction of TOGp with microtubules and tubulin
    • Spittle C., Charrasse S., Larroque C., and Cassimeris L. The interaction of TOGp with microtubules and tubulin. J Biol Chem 275 (2000) 20748-20753
    • (2000) J Biol Chem , vol.275 , pp. 20748-20753
    • Spittle, C.1    Charrasse, S.2    Larroque, C.3    Cassimeris, L.4
  • 9
    • 0030668145 scopus 로고    scopus 로고
    • BIM1 encodes a microtubule-binding protein in yeast
    • Schwartz K., Richards K., and Botstein D. BIM1 encodes a microtubule-binding protein in yeast. Mol Biol Cell 8 (1997) 2677-2691
    • (1997) Mol Biol Cell , vol.8 , pp. 2677-2691
    • Schwartz, K.1    Richards, K.2    Botstein, D.3
  • 11
    • 33846100785 scopus 로고    scopus 로고
    • The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment
    • Wei R.R., Al-Bassam J., and Harrison S.C. The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment. Nat Struct Mol Biol 14 (2007) 54-59
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 54-59
    • Wei, R.R.1    Al-Bassam, J.2    Harrison, S.C.3
  • 14
    • 34748862943 scopus 로고    scopus 로고
    • Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1
    • Slep K.C., and Vale R.D. Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol Cell 27 (2007) 976-991
    • (2007) Mol Cell , vol.27 , pp. 976-991
    • Slep, K.C.1    Vale, R.D.2
  • 15
    • 68549121078 scopus 로고    scopus 로고
    • Phosphoregulation of the budding yeast EB1 homologue Bim1p by Aurora/Ipl1p
    • This study reconstitutes Bim1p plus end tracking in vitro and delineates Aurora B kinase regulatory elements in the central linker region that modulate plus end tracking activity. The central linker region is required for plus end tracking activity though little structure/function information is known of its mechanism or regulation. The authors show that cell-cycle-dependent Aurora B activity causes phosphorylation of the central linker, thus abrogating Bim1p plus end localization.
    • Zimniak T., Stengl K., Mechtler K., and Westermann S. Phosphoregulation of the budding yeast EB1 homologue Bim1p by Aurora/Ipl1p. J Cell Biol 186 (2009) 379-391. This study reconstitutes Bim1p plus end tracking in vitro and delineates Aurora B kinase regulatory elements in the central linker region that modulate plus end tracking activity. The central linker region is required for plus end tracking activity though little structure/function information is known of its mechanism or regulation. The authors show that cell-cycle-dependent Aurora B activity causes phosphorylation of the central linker, thus abrogating Bim1p plus end localization.
    • (2009) J Cell Biol , vol.186 , pp. 379-391
    • Zimniak, T.1    Stengl, K.2    Mechtler, K.3    Westermann, S.4
  • 16
    • 37249075604 scopus 로고    scopus 로고
    • Reconstitution of a microtubule plus-end tracking system in vitro
    • This study is the first to show in vitro reconstituted microtubule plus end tracking activity. Using time-lapse total internal reflection fluorescence microscopy, the authors reconstitute Mal3 plus end tracking activity and show the dependence of Tip1 (CLIP-170) plus end tracking activity on Mal3.
    • Bieling P., Laan L., Schek H., Munteanu E.L., Sandblad L., Dogterom M., Brunner D., and Surrey T. Reconstitution of a microtubule plus-end tracking system in vitro. Nature 450 (2007) 1100-1105. This study is the first to show in vitro reconstituted microtubule plus end tracking activity. Using time-lapse total internal reflection fluorescence microscopy, the authors reconstitute Mal3 plus end tracking activity and show the dependence of Tip1 (CLIP-170) plus end tracking activity on Mal3.
    • (2007) Nature , vol.450 , pp. 1100-1105
    • Bieling, P.1    Laan, L.2    Schek, H.3    Munteanu, E.L.4    Sandblad, L.5    Dogterom, M.6    Brunner, D.7    Surrey, T.8
  • 17
    • 33845683023 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam
    • Sandblad L., Busch K.E., Tittmann P., Gross H., Brunner D., and Hoenger A. The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam. Cell 127 (2006) 1415-1424
    • (2006) Cell , vol.127 , pp. 1415-1424
    • Sandblad, L.1    Busch, K.E.2    Tittmann, P.3    Gross, H.4    Brunner, D.5    Hoenger, A.6
  • 18
    • 53549133348 scopus 로고    scopus 로고
    • Mal3, the Schizosaccharomyces pombe homolog of EB1, changes the microtubule lattice
    • This cryo-EM reconstruction analysis of microtubules polymerized in the presence of Mal3 indicates that Mal3 promotes polymerization of the A-form microtubule lattice. Mal3 binding is localized to the protofilament groove, associated predominantly with alpha-tubulin.
    • des Georges A., Katsuki M., Drummond D.R., Osei M., Cross R.A., and Amos L.A. Mal3, the Schizosaccharomyces pombe homolog of EB1, changes the microtubule lattice. Nat Struct Mol Biol 15 (2008) 1102-1108. This cryo-EM reconstruction analysis of microtubules polymerized in the presence of Mal3 indicates that Mal3 promotes polymerization of the A-form microtubule lattice. Mal3 binding is localized to the protofilament groove, associated predominantly with alpha-tubulin.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1102-1108
    • des Georges, A.1    Katsuki, M.2    Drummond, D.R.3    Osei, M.4    Cross, R.A.5    Amos, L.A.6
  • 19
    • 43149111310 scopus 로고    scopus 로고
    • EB1 regulates microtubule dynamics and tubulin sheet closure in vitro
    • This study analyzes the effect of EB1 on microtubule polymerization and dynamics in vitro. Using electron cryomicroscopy, the authors find that EB1 promotes the polymerization of tubulin sheets by favoring the lateral association of free tubulin. Results also indicate that EB1 promotes tube closure and concomitantly, catastrophe.
    • Vitre B., Coquelle F.M., Heichette C., Garnier C., Chretien D., and Arnal I. EB1 regulates microtubule dynamics and tubulin sheet closure in vitro. Nat Cell Biol 10 (2008) 415-421. This study analyzes the effect of EB1 on microtubule polymerization and dynamics in vitro. Using electron cryomicroscopy, the authors find that EB1 promotes the polymerization of tubulin sheets by favoring the lateral association of free tubulin. Results also indicate that EB1 promotes tube closure and concomitantly, catastrophe.
    • (2008) Nat Cell Biol , vol.10 , pp. 415-421
    • Vitre, B.1    Coquelle, F.M.2    Heichette, C.3    Garnier, C.4    Chretien, D.5    Arnal, I.6
  • 22
    • 33846950044 scopus 로고    scopus 로고
    • Discrete states of a protein interaction network govern interphase and mitotic microtubule dynamics
    • Niethammer P., Kronja I., Kandels-Lewis S., Rybina S., Bastiaens P., and Karsenti E. Discrete states of a protein interaction network govern interphase and mitotic microtubule dynamics. PLoS Biol 5 (2007) e29
    • (2007) PLoS Biol , vol.5
    • Niethammer, P.1    Kronja, I.2    Kandels-Lewis, S.3    Rybina, S.4    Bastiaens, P.5    Karsenti, E.6
  • 23
    • 52249087768 scopus 로고    scopus 로고
    • Orientation and structure of the Ndc80 complex on the microtubule lattice
    • This EM reconstruction of microtubules decorated with the Ndc80/Nuf2 kinetochore component reveals intriguing interaction modes between the heterodimer's calponin homology domains and inter-tubulin contacts on the microtubule, potentially representative of the EB1-microtubule interaction.
    • Wilson-Kubalek E.M., Cheeseman I.M., Yoshioka C., Desai A., and Milligan R.A. Orientation and structure of the Ndc80 complex on the microtubule lattice. J Cell Biol 182 (2008) 1055-1061. This EM reconstruction of microtubules decorated with the Ndc80/Nuf2 kinetochore component reveals intriguing interaction modes between the heterodimer's calponin homology domains and inter-tubulin contacts on the microtubule, potentially representative of the EB1-microtubule interaction.
    • (2008) J Cell Biol , vol.182 , pp. 1055-1061
    • Wilson-Kubalek, E.M.1    Cheeseman, I.M.2    Yoshioka, C.3    Desai, A.4    Milligan, R.A.5
  • 24
    • 23744433896 scopus 로고    scopus 로고
    • Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex
    • Hayashi I., Wilde A., Mal T.K., and Ikura M. Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex. Mol Cell 19 (2005) 449-460
    • (2005) Mol Cell , vol.19 , pp. 449-460
    • Hayashi, I.1    Wilde, A.2    Mal, T.K.3    Ikura, M.4
  • 26
    • 33746903069 scopus 로고    scopus 로고
    • Microtubule plus-end loading of p150(Glued) is mediated by EB1 and CLIP-170 but is not required for intracellular membrane traffic in mammalian cells
    • Watson P., and Stephens D.J. Microtubule plus-end loading of p150(Glued) is mediated by EB1 and CLIP-170 but is not required for intracellular membrane traffic in mammalian cells. J Cell Sci 119 (2006) 2758-2767
    • (2006) J Cell Sci , vol.119 , pp. 2758-2767
    • Watson, P.1    Stephens, D.J.2
  • 27
    • 59449100831 scopus 로고    scopus 로고
    • CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
    • This study uses in vitro total internal reflection fluorescence plus end tracking reconstitution assays to demonstrate the EB1-dependent plus end tracking activity of CLIP-170, confirming earlier studies showing the same dependency with S. pombe counterparts.
    • Bieling P., Kandels-Lewis S., Telley I.A., van Dijk J., Janke C., and Surrey T. CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites. J Cell Biol 183 (2008) 1223-1233. This study uses in vitro total internal reflection fluorescence plus end tracking reconstitution assays to demonstrate the EB1-dependent plus end tracking activity of CLIP-170, confirming earlier studies showing the same dependency with S. pombe counterparts.
    • (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
  • 28
    • 38849159958 scopus 로고    scopus 로고
    • Suppression of microtubule dynamic instability by the +TIP protein EB1 and its modulation by the CAP-Gly domain of p150glued
    • Manna T., Honnappa S., Steinmetz M.O., and Wilson L. Suppression of microtubule dynamic instability by the +TIP protein EB1 and its modulation by the CAP-Gly domain of p150glued. Biochemistry 47 (2008) 779-786
    • (2008) Biochemistry , vol.47 , pp. 779-786
    • Manna, T.1    Honnappa, S.2    Steinmetz, M.O.3    Wilson, L.4
  • 36
    • 34948902333 scopus 로고    scopus 로고
    • CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1
    • Hayashi I., Plevin M.J., and Ikura M. CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1. Nat Struct Mol Biol 14 (2007) 980-981
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 980-981
    • Hayashi, I.1    Plevin, M.J.2    Ikura, M.3
  • 38
    • 27544458296 scopus 로고    scopus 로고
    • Melanophilin and myosin Va track the microtubule plus end on EB1
    • Wu X.S., Tsan G.L., and Hammer III J.A. Melanophilin and myosin Va track the microtubule plus end on EB1. J Cell Biol 171 (2005) 201-207
    • (2005) J Cell Biol , vol.171 , pp. 201-207
    • Wu, X.S.1    Tsan, G.L.2    Hammer III, J.A.3
  • 40
    • 69949104631 scopus 로고    scopus 로고
    • Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics
    • Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., and Qi R.Z. Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics. Mol Biol Cell 20 (2009) 3660-3670
    • (2009) Mol Biol Cell , vol.20 , pp. 3660-3670
    • Fong, K.W.1    Hau, S.Y.2    Kho, Y.S.3    Jia, Y.4    He, L.5    Qi, R.Z.6
  • 41
    • 37649004096 scopus 로고    scopus 로고
    • XMAP215 is a processive microtubule polymerase
    • This study demonstrates the first in vitro reconstitution of XMAP215 plus end tracking activity. Using total internal reflection fluorescence microscopy, the authors find XMAP215 at the plus end of both growing and shrinking microtubules. Assays indicate a 1:1 XMAP215:tubulin-binding stoichiometry and negative stain EM reveals a large conformational change in XMAP215 upon binding a single tubulin heterodimer.
    • Brouhard G.J., Stear J.H., Noetzel T.L., Al-Bassam J., Kinoshita K., Harrison S.C., Howard J., and Hyman A.A. XMAP215 is a processive microtubule polymerase. Cell 132 (2008) 79-88. This study demonstrates the first in vitro reconstitution of XMAP215 plus end tracking activity. Using total internal reflection fluorescence microscopy, the authors find XMAP215 at the plus end of both growing and shrinking microtubules. Assays indicate a 1:1 XMAP215:tubulin-binding stoichiometry and negative stain EM reveals a large conformational change in XMAP215 upon binding a single tubulin heterodimer.
    • (2008) Cell , vol.132 , pp. 79-88
    • Brouhard, G.J.1    Stear, J.H.2    Noetzel, T.L.3    Al-Bassam, J.4    Kinoshita, K.5    Harrison, S.C.6    Howard, J.7    Hyman, A.A.8
  • 42
    • 0035901596 scopus 로고    scopus 로고
    • M phase-specific kinetochore proteins in fission yeast: microtubule-associating Dis1 and Mtc1 display rapid separation and segregation during anaphase
    • Nakaseko Y., Goshima G., Morishita J., and Yanagida M. M phase-specific kinetochore proteins in fission yeast: microtubule-associating Dis1 and Mtc1 display rapid separation and segregation during anaphase. Curr Biol 11 (2001) 537-549
    • (2001) Curr Biol , vol.11 , pp. 537-549
    • Nakaseko, Y.1    Goshima, G.2    Morishita, J.3    Yanagida, M.4
  • 43
    • 0030728492 scopus 로고    scopus 로고
    • Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body
    • Wang P.J., and Huffaker T.C. Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body. J Cell Biol 139 (1997) 1271-1280
    • (1997) J Cell Biol , vol.139 , pp. 1271-1280
    • Wang, P.J.1    Huffaker, T.C.2
  • 44
    • 33645306849 scopus 로고    scopus 로고
    • Stu2p binds tubulin and undergoes an open-to-closed conformational change
    • This study uses negative stain EM to show a dramatic conformational change in the Stu2p homodimer upon binding a single tubulin heterodimer. Analytic ultracentrifugation and gel filtration chromatography are used, indicating a 2:1 Stu2p:tubulin-binding stoichiometry.
    • Al-Bassam J., van Breugel M., Harrison S.C., and Hyman A. Stu2p binds tubulin and undergoes an open-to-closed conformational change. J Cell Biol 172 (2006) 1009-1022. This study uses negative stain EM to show a dramatic conformational change in the Stu2p homodimer upon binding a single tubulin heterodimer. Analytic ultracentrifugation and gel filtration chromatography are used, indicating a 2:1 Stu2p:tubulin-binding stoichiometry.
    • (2006) J Cell Biol , vol.172 , pp. 1009-1022
    • Al-Bassam, J.1    van Breugel, M.2    Harrison, S.C.3    Hyman, A.4
  • 45
    • 33847639293 scopus 로고    scopus 로고
    • Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding
    • Al-Bassam J., Larsen N.A., Hyman A.A., and Harrison S.C. Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding. Structure 15 (2007) 355-362
    • (2007) Structure , vol.15 , pp. 355-362
    • Al-Bassam, J.1    Larsen, N.A.2    Hyman, A.A.3    Harrison, S.C.4
  • 46
    • 0023589342 scopus 로고
    • A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end
    • Gard D.L., and Kirschner M.W. A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end. J Cell Biol 105 (1987) 2203-2215
    • (1987) J Cell Biol , vol.105 , pp. 2203-2215
    • Gard, D.L.1    Kirschner, M.W.2


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