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Volumn 201, Issue 7, 2013, Pages 1037-1051

Cyclin-dependent kinases regulate splice-specific targeting of dynamin-related protein 1 to microtubules

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; DYNAMIN; STAUROSPORINE; SYNAPSIN I;

EID: 84880008164     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201210045     Document Type: Article
Times cited : (98)

References (54)
  • 1
    • 79959318254 scopus 로고    scopus 로고
    • Isoform-specific dephosphorylation of dynamin1 by calcineurin couples neurotrophin receptor endocytosis to axonal growth
    • Bodmer, D., M. Ascaño, and R. Kuruvilla. 2011. Isoform-specific dephosphorylation of dynamin1 by calcineurin couples neurotrophin receptor endocytosis to axonal growth. Neuron. 70:1085-1099. http://dx.doi.org/10.1016/j.neuron.2011.04.025
    • (2011) Neuron. , vol.70 , pp. 1085-1099
    • Bodmer, D.1    Ascaño, M.2    Kuruvilla, R.3
  • 2
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and F.P. Cordelières. 2006. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224:213-232. http://dx.doi.org/10.1111/j.1365-2818.2006.01706.x
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 3
    • 52049109163 scopus 로고    scopus 로고
    • Novel mitochondrial extensions provide evidence for a link between microtubule-directed movement and mitochondrial fission
    • Bowes, T., and R.S. Gupta. 2008. Novel mitochondrial extensions provide evidence for a link between microtubule-directed movement and mitochondrial fission. Biochem. Biophys. Res. Commun. 376:40-45. http://dx.doi.org/10.1016/j.bbrc.2008.08.120
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 40-45
    • Bowes, T.1    Gupta, R.S.2
  • 5
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang, C.R., and C. Blackstone. 2007. Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J. Biol. Chem. 282:21583-21587. http://dx.doi.org/10.1074/jbc.C700083200
    • (2007) J. Biol. Chem. , vol.282 , pp. 21583-21587
    • Chang, C.R.1    Blackstone, C.2
  • 6
    • 77957798188 scopus 로고    scopus 로고
    • A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division
    • Chang, C.R., C.M. Manlandro, D. Arnoult, J. Stadler, A.E. Posey, R.B. Hill, and C. Blackstone. 2010. A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division. J. Biol. Chem. 285:32494-32503. http://dx.doi.org/10.1074/jbc.M110.142430
    • (2010) J. Biol. Chem. , vol.285 , pp. 32494-32503
    • Chang, C.R.1    Manlandro, C.M.2    Arnoult, D.3    Stadler, J.4    Posey, A.E.5    Hill, R.B.6    Blackstone, C.7
  • 7
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen, H., S.A. Detmer, A.J. Ewald, E.E. Griffin, S.E. Fraser, and D.C. Chan. 2003. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160: 189-200. http://dx.doi.org/10.1083/jcb.200211046
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 8
    • 36048945922 scopus 로고    scopus 로고
    • ImageJ for microscopy
    • Collins, T.J. 2007. ImageJ for microscopy. Biotechniques. 43:25-30. http://dx.doi.org/10.2144/000112517
    • (2007) Biotechniques. , vol.43 , pp. 25-30
    • Collins, T.J.1
  • 9
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs, J.T., and S. Strack. 2007. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 8:939-944. http://dx.doi.org/10.1038/sj.embor.7401062
    • (2007) EMBO Rep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 10
    • 65449187907 scopus 로고    scopus 로고
    • Functional characterization of phosphorylation sites in dynamin-related protein 1
    • Cribbs, J.T., and S. Strack. 2009. Functional characterization of phosphorylation sites in dynamin-related protein 1. Methods Enzymol. 457:231-253. http://dx.doi.org/10.1016/S0076-6879(09)05013-7
    • (2009) Methods Enzymol. , vol.457 , pp. 231-253
    • Cribbs, J.T.1    Strack, S.2
  • 11
    • 34447314190 scopus 로고    scopus 로고
    • Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function
    • Davies, V.J., A.J. Hollins, M.J. Piechota, W. Yip, J.R. Davies, K.E. White, P.P. Nicols, M.E. Boulton, and M. Votruba. 2007. Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function. Hum. Mol. Genet. 16:1307-1318. http://dx.doi.org/10.1093/hmg/ddm079
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1307-1318
    • Davies, V.J.1    Hollins, A.J.2    Piechota, M.J.3    Yip, W.4    Davies, J.R.5    White, K.E.6    Nicols, P.P.7    Boulton, M.E.8    Votruba, M.9
  • 12
    • 84855602576 scopus 로고    scopus 로고
    • Interplay between microtubule dynamics and intracellular organization
    • de Forges, H., A. Bouissou, and F. Perez. 2012. Interplay between microtubule dynamics and intracellular organization. Int. J. Biochem. Cell Biol. 44:266-274. http://dx.doi.org/10.1016/j.biocel.2011.11.009
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 266-274
    • de Forges, H.1    Bouissou, A.2    Perez, F.3
  • 13
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubuleassociated proteins
    • Dehmelt, L., and S. Halpain. 2005. The MAP2/Tau family of microtubuleassociated proteins. Genome Biol. 6:204. http://dx.doi.org/10.1186/gb-2004-6-1-204
    • (2005) Genome Biol. , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 14
    • 0034518173 scopus 로고    scopus 로고
    • Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics
    • Downing, K.H. 2000. Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu. Rev. Cell Dev. Biol. 16:89-111. http://dx.doi.org/10.1146/annurev.cellbio.16.1.89
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 89-111
    • Downing, K.H.1
  • 16
    • 80053376521 scopus 로고    scopus 로고
    • The crystal structure of dynamin
    • Ford, M.G., S. Jenni, and J. Nunnari. 2011. The crystal structure of dynamin. Nature. 477:561-566. http://dx.doi.org/10.1038/nature10441
    • (2011) Nature. , vol.477 , pp. 561-566
    • Ford, M.G.1    Jenni, S.2    Nunnari, J.3
  • 18
    • 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. http://dx.doi.org/10.1016/j.ceb.2007.11.010
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 19
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins, S., L. Lackner, and J. Nunnari. 2007. The machines that divide and fuse mitochondria. Annu. Rev. Biochem. 76:751-780. http://dx.doi.org/10.1146/annurev.biochem.76.071905.090048
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 20
    • 1642538446 scopus 로고    scopus 로고
    • Genomic organization, alternative splicing, and promoter analysis of human dynamin-like protein gene
    • Howng, S.L., W.D. Sy, T.S. Cheng, A.S. Lieu, C. Wang, W.S. Tzou, C.L. Cho, and Y.R. Hong. 2004. Genomic organization, alternative splicing, and promoter analysis of human dynamin-like protein gene. Biochem. Biophys. Res. Commun. 314:766-772. http://dx.doi.org/10.1016/j.bbrc.2003.12.172
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 766-772
    • Howng, S.L.1    Sy, W.D.2    Cheng, T.S.3    Lieu, A.S.4    Wang, C.5    Tzou, W.S.6    Cho, C.L.7    Hong, Y.R.8
  • 22
    • 80052759856 scopus 로고    scopus 로고
    • Dynamin 2 associates with microtubules at mitosis and regulates cell cycle progression
    • Ishida, N., Y. Nakamura, K. Tanabe, S.A. Li, and K. Takei. 2011. Dynamin 2 associates with microtubules at mitosis and regulates cell cycle progression. Cell Struct. Funct. 36:145-154. http://dx.doi.org/10.1247/csf.10016
    • (2011) Cell Struct. Funct. , vol.36 , pp. 145-154
    • Ishida, N.1    Nakamura, Y.2    Tanabe, K.3    Li, S.A.4    Takei, K.5
  • 24
    • 67749133987 scopus 로고    scopus 로고
    • The dynamin related protein Dnm1 fragments mitochondria in a microtubule-dependent manner during the fission yeast cell cycle
    • Jourdain, I., Y. Gachet, and J.S. Hyams. 2009. The dynamin related protein Dnm1 fragments mitochondria in a microtubule-dependent manner during the fission yeast cell cycle. Cell Motil. Cytoskeleton. 66:509-523. http://dx.doi.org/10.1002/cm.20351
    • (2009) Cell Motil. Cytoskeleton. , vol.66 , pp. 509-523
    • Jourdain, I.1    Gachet, Y.2    Hyams, J.S.3
  • 25
    • 79959655354 scopus 로고    scopus 로고
    • Mitochondrial division: molecular machinery and physiological functions
    • Kageyama, Y., Z. Zhang, and H. Sesaki. 2011. Mitochondrial division: molecular machinery and physiological functions. Curr. Opin. Cell Biol. 23:427-434. http://dx.doi.org/10.1016/j.ceb.2011.04.009
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 427-434
    • Kageyama, Y.1    Zhang, Z.2    Sesaki, H.3
  • 27
    • 37249044282 scopus 로고    scopus 로고
    • Quantitative FRAP in analysis of molecular binding dynamics in vivo
    • McNally, J.G. 2008. Quantitative FRAP in analysis of molecular binding dynamics in vivo. Methods Cell Biol. 85:329-351. http://dx.doi.org/10.1016/S0091-679X(08)85014-5
    • (2008) Methods Cell Biol. , vol.85 , pp. 329-351
    • McNally, J.G.1
  • 29
    • 84869115074 scopus 로고    scopus 로고
    • Microtubule assembly during mitosis - from distinct origins to distinct functions? J
    • Meunier, S., and I. Vernos. 2012. Microtubule assembly during mitosis - from distinct origins to distinct functions? J. Cell Sci. 125:2805-2814. http://dx.doi.org/10.1242/jcs.092429
    • (2012) Cell Sci. , vol.125 , pp. 2805-2814
    • Meunier, S.1    Vernos, I.2
  • 30
    • 78049461959 scopus 로고    scopus 로고
    • Proline-rich domain in dynamin-2 has a low microtubulebinding activity: how is this activity controlled during mitosis in HeLa cells?
    • Morita, M., K. Hamao, S. Izumi, E. Okumura, K. Tanaka, T. Kishimoto, and H. Hosoya. 2010. Proline-rich domain in dynamin-2 has a low microtubulebinding activity: how is this activity controlled during mitosis in HeLa cells? J. Biochem. 148:533-538. http://dx.doi.org/10.1093/jb/mvq116
    • (2010) J. Biochem. , vol.148 , pp. 533-538
    • Morita, M.1    Hamao, K.2    Izumi, S.3    Okumura, E.4    Tanaka, K.5    Kishimoto, T.6    Hosoya, H.7
  • 31
    • 84877781381 scopus 로고    scopus 로고
    • Mechanics of Dynamin-Mediated Membrane Fission
    • Morlot, S., and A. Roux. 2013. Mechanics of Dynamin-Mediated Membrane Fission. Annu Rev Biophys.
    • (2013) Annu Rev Biophys.
    • Morlot, S.1    Roux, A.2
  • 32
    • 0025006964 scopus 로고
    • Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
    • Obar, R.A., C.A. Collins, J.A. Hammarback, H.S. Shpetner, and R.B. Vallee. 1990. Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature. 347:256-261. http://dx.doi.org/10.1038/347256a0
    • (1990) Nature. , vol.347 , pp. 256-261
    • Obar, R.A.1    Collins, C.A.2    Hammarback, J.A.3    Shpetner, H.S.4    Vallee, R.B.5
  • 33
    • 33947434544 scopus 로고    scopus 로고
    • OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis
    • Olichon, A., G. Elachouri, L. Baricault, C. Delettre, P. Belenguer, and G. Lenaers. 2007. OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis. Cell Death Differ. 14:682-692. http://dx.doi.org/10.1038/sj.cdd.4402048
    • (2007) Cell Death Differ. , vol.14 , pp. 682-692
    • Olichon, A.1    Elachouri, G.2    Baricault, L.3    Delettre, C.4    Belenguer, P.5    Lenaers, G.6
  • 34
    • 84875273810 scopus 로고    scopus 로고
    • New insights into the function and regulation of mitochondrial fission
    • Otera, H., N. Ishihara, and K. Mihara. 2013. New insights into the function and regulation of mitochondrial fission. Biochim. Biophys. Acta. 1833:1256- 1268. http://dx.doi.org/10.1016/j.bbamcr.2013.02.002
    • (2013) Biochim. Biophys. Acta. , vol.1833 , pp. 1256-1268
    • Otera, H.1    Ishihara, N.2    Mihara, K.3
  • 35
    • 0032734577 scopus 로고    scopus 로고
    • The dynaminlike protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells
    • Pitts, K.R., Y. Yoon, E.W. Krueger, and M.A. McNiven. 1999. The dynaminlike protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells. Mol. Biol. Cell. 10:4403-4417.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 4403-4417
    • Pitts, K.R.1    Yoon, Y.2    Krueger, E.W.3    McNiven, M.A.4
  • 36
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton, W.M., and P.J. Hollenbeck. 2012. The axonal transport of mitochondria. J. Cell Sci. 125:2095-2104. http://dx.doi.org/10.1242/jcs.053850
    • (2012) J. Cell Sci. , vol.125 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 37
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., W.S. Rasband, and K.W. Eliceiri. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods. 9:671-675. http://dx.doi.org/10.1038/nmeth.2089
    • (2012) Nat. Methods. , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 38
    • 0024342278 scopus 로고
    • Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules
    • Shpetner, H.S., and R.B. Vallee. 1989. Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Cell. 59:421-432. http://dx.doi.org/10.1016/0092-8674(89)90027-5
    • (1989) Cell. , vol.59 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 39
    • 4644314874 scopus 로고    scopus 로고
    • Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrinmediated endocytosis
    • Song, B.D., M. Leonard, and S.L. Schmid. 2004. Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrinmediated endocytosis. J. Biol. Chem. 279:40431-40436. http://dx.doi.org/10.1074/jbc.M407007200
    • (2004) J. Biol. Chem. , vol.279 , pp. 40431-40436
    • Song, B.D.1    Leonard, M.2    Schmid, S.L.3
  • 40
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • Song, Z., H. Chen, M. Fiket, C. Alexander, and D.C. Chan. 2007. OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J. Cell Biol. 178:749-755. http://dx.doi.org/10.1083/jcb.200704110
    • (2007) J. Cell Biol. , vol.178 , pp. 749-755
    • Song, Z.1    Chen, H.2    Fiket, M.3    Alexander, C.4    Chan, D.C.5
  • 41
    • 84858434492 scopus 로고    scopus 로고
    • Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain
    • Strack, S., and J.T. Cribbs. 2012. Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain. J. Biol. Chem. 287:10990-11001. http://dx.doi.org/10.1074/jbc.M112.342105
    • (2012) J. Biol. Chem. , vol.287 , pp. 10990-11001
    • Strack, S.1    Cribbs, J.T.2
  • 42
    • 80555122785 scopus 로고    scopus 로고
    • Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin
    • Szyk, A., A.M. Deaconescu, G. Piszczek, and A. Roll-Mecak. 2011. Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin. Nat. Struct. Mol. Biol. 18:1250-1258. http://dx.doi.org/10.1038/nsmb.2148
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1250-1258
    • Szyk, A.1    Deaconescu, A.M.2    Piszczek, G.3    Roll-Mecak, A.4
  • 43
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • Taguchi, N., N. Ishihara, A. Jofuku, T. Oka, and K. Mihara. 2007. Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J. Biol. Chem. 282:11521-11529. http://dx.doi.org/10.1074/jbc.M607279200
    • (2007) J. Biol. Chem. , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 44
    • 67449124363 scopus 로고    scopus 로고
    • Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant
    • Tanabe, K., and K. Takei. 2009. Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant. J. Cell Biol. 185:939-948. http://dx.doi.org/10.1083/jcb.200803153
    • (2009) J. Cell Biol. , vol.185 , pp. 939-948
    • Tanabe, K.1    Takei, K.2
  • 45
    • 2342574188 scopus 로고    scopus 로고
    • Dynamin 2 binds gamma-tubulin and participates in centrosome cohesion
    • Thompson, H.M., H. Cao, J. Chen, U. Euteneuer, and M.A. McNiven. 2004. Dynamin 2 binds gamma-tubulin and participates in centrosome cohesion. Nat. Cell Biol. 6:335-342. http://dx.doi.org/10.1038/ncb1112
    • (2004) Nat. Cell Biol. , vol.6 , pp. 335-342
    • Thompson, H.M.1    Cao, H.2    Chen, J.3    Euteneuer, U.4    McNiven, M.A.5
  • 46
    • 67649786569 scopus 로고    scopus 로고
    • Drp1 levels constitutively regulate mitochondrial dynamics and cell survival in cortical neurons
    • Uo, T., J. Dworzak, C. Kinoshita, D.M. Inman, Y. Kinoshita, P.J. Horner, and R.S. Morrison. 2009. Drp1 levels constitutively regulate mitochondrial dynamics and cell survival in cortical neurons. Exp. Neurol. 218:274- 285. http://dx.doi.org/10.1016/j.expneurol.2009.05.010
    • (2009) Exp. Neurol. , vol.218 , pp. 274-285
    • Uo, T.1    Dworzak, J.2    Kinoshita, C.3    Inman, D.M.4    Kinoshita, Y.5    Horner, P.J.6    Morrison, R.S.7
  • 47
    • 5444236916 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1
    • Varadi, A., L.I. Johnson-Cadwell, V. Cirulli, Y. Yoon, V.J. Allan, and G.A. Rutter. 2004. Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1. J. Cell Sci. 117:4389-4400. http://dx.doi.org/10.1242/jcs.01299
    • (2004) J. Cell Sci. , vol.117 , pp. 4389-4400
    • Varadi, A.1    Johnson-Cadwell, L.I.2    Cirulli, V.3    Yoon, Y.4    Allan, V.J.5    Rutter, G.A.6
  • 49
    • 77955336327 scopus 로고    scopus 로고
    • A MAP for bundling microtubules
    • Walczak, C.E., and S.L. Shaw. 2010. A MAP for bundling microtubules. Cell. 142:364-367. http://dx.doi.org/10.1016/j.cell.2010.07.023
    • (2010) Cell. , vol.142 , pp. 364-367
    • Walczak, C.E.1    Shaw, S.L.2
  • 51
    • 84872686195 scopus 로고    scopus 로고
    • Cell signaling and mitochondrial dynamics: Implications for neuronal function and neurodegenerative disease
    • Wilson, T.J., A.M. Slupe, and S. Strack. 2013. Cell signaling and mitochondrial dynamics: Implications for neuronal function and neurodegenerative disease. Neurobiol. Dis. 51:13-26. http://dx.doi.org/10.1016/j.nbd.2012.01.009
    • (2013) Neurobiol. Dis. , vol.51 , pp. 13-26
    • Wilson, T.J.1    Slupe, A.M.2    Strack, S.3
  • 52
    • 80052193534 scopus 로고    scopus 로고
    • Calcineurin selectively docks with the dynamin Ixb splice variant to regulate activity-dependent bulk endocytosis
    • Xue, J., M.E. Graham, A.E. Novelle, N. Sue, N. Gray, M.A. McNiven, K.J. Smillie, M.A. Cousin, and P.J. Robinson. 2011. Calcineurin selectively docks with the dynamin Ixb splice variant to regulate activity-dependent bulk endocytosis. J. Biol. Chem. 286:30295-30303. http://dx.doi.org/10.1074/jbc.M111.273110
    • (2011) J. Biol. Chem. , vol.286 , pp. 30295-30303
    • Xue, J.1    Graham, M.E.2    Novelle, A.E.3    Sue, N.4    Gray, N.5    McNiven, M.A.6    Smillie, K.J.7    Cousin, M.A.8    Robinson, P.J.9
  • 53
    • 0032559599 scopus 로고    scopus 로고
    • A novel dynaminlike protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells
    • Yoon, Y., K.R. Pitts, S. Dahan, and M.A. McNiven. 1998. A novel dynaminlike protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. J. Cell Biol. 140:779-793. http://dx.doi.org/10.1083/jcb.140.4.779
    • (1998) J. Cell Biol. , vol.140 , pp. 779-793
    • Yoon, Y.1    Pitts, K.R.2    Dahan, S.3    McNiven, M.A.4
  • 54
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • Youle, R.J., and A.M. van der Bliek. 2012. Mitochondrial fission, fusion, and stress. Science. 337:1062-1065. http://dx.doi.org/10.1126/science.1219855
    • (2012) Science. , vol.337 , pp. 1062-1065
    • Youle, R.J.1    van der Bliek, A.M.2


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