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Volumn 21, Issue 6, 2012, Pages 1299-1311

VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL PROTEIN; PEPTIDES AND PROTEINS; PROTEIN TYROSINE PHOSPHATASE INTERACTING PROTEIN 51; UNCLASSIFIED DRUG; VESICLE ASSOCIATED MEMBRANE PROTEIN ASSOCIATED PROTEIN B;

EID: 84863393591     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr559     Document Type: Article
Times cited : (408)

References (68)
  • 1
    • 79959763071 scopus 로고    scopus 로고
    • Keeping up with genetic discoveries in amyotrophic lateral sclerosis: The ALSoD and ALSGene databases
    • Lill, C.M., Abel, O., Bertram, L. and Al-Chalabi, A. (2011) Keeping up with genetic discoveries in amyotrophic lateral sclerosis: The ALSoD and ALSGene databases. Amyotroph. Lateral Scler., 12, 238-249.
    • (2011) Amyotroph. Lateral Scler. , vol.12 , pp. 238-249
    • Lill, C.M.1    Abel, O.2    Bertram, L.3    Al-Chalabi, A.4
  • 4
    • 0031898053 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism
    • Kagiwada, S., Hosaka, K., Murata, M., Nikawa, J. and Takatsuki, A. (1998) The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism. J. Bacteriol., 180, 1700-1708.
    • (1998) J. Bacteriol. , vol.180 , pp. 1700-1708
    • Kagiwada, S.1    Hosaka, K.2    Murata, M.3    Nikawa, J.4    Takatsuki, A.5
  • 6
    • 33749554133 scopus 로고    scopus 로고
    • Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8)
    • Kanekura, K., Nishimoto, I., Aiso, S. and Matsuoka, M. (2006) Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem., 28, 30223-30232.
    • (2006) J. Biol. Chem. , vol.28 , pp. 30223-30232
    • Kanekura, K.1    Nishimoto, I.2    Aiso, S.3    Matsuoka, M.4
  • 7
    • 0033967492 scopus 로고    scopus 로고
    • Mouse VAP33 is associated with the endoplasmic reticulum and microtubules
    • Skehel, P.A., Fabian-Fine, R. and Kandel, E.R. (2000) Mouse VAP33 is associated with the endoplasmic reticulum and microtubules. Proc. Natl Acad. Sci. USA, 97, 1101-1106.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1101-1106
    • Skehel, P.A.1    Fabian-Fine, R.2    Kandel, E.R.3
  • 8
    • 34848904785 scopus 로고    scopus 로고
    • Motor neuron disease-associated mutant vesicle-associated membrane protein-associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates
    • Teuling, E., Ahmed, S., Haasdijk, E., Demmers, J., Steinmetz, M.O., Akhmanova, A., Jaarsma, D. and Hoogenraad, C.C. (2007) Motor neuron disease-associated mutant vesicle-associated membrane protein-associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates. J. Neurosci., 27, 9801-9815.
    • (2007) J. Neurosci. , vol.27 , pp. 9801-9815
    • Teuling, E.1    Ahmed, S.2    Haasdijk, E.3    Demmers, J.4    Steinmetz, M.O.5    Akhmanova, A.6    Jaarsma, D.7    Hoogenraad, C.C.8
  • 9
    • 77952308995 scopus 로고    scopus 로고
    • A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum
    • Fasana, E., Fossati, M., Ruggiano, A., Brambillasca, S., Hoogenraad, C.C., Navone, F., Francolini, M. and Borgese, N. (2010) A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum. FASEB J., 24, 1419-1430.
    • (2010) FASEB J. , vol.24 , pp. 1419-1430
    • Fasana, E.1    Fossati, M.2    Ruggiano, A.3    Brambillasca, S.4    Hoogenraad, C.C.5    Navone, F.6    Francolini, M.7    Borgese, N.8
  • 11
    • 77954324616 scopus 로고    scopus 로고
    • AAV-mediated expression of wildtype and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca-dependent ER-associated pathway
    • Langou, K., Moumen, A., Pellegrino, C., Aebischer, J., Medina, I., Aebischer, P. and Raoul, C. (2010) AAV-mediated expression of wildtype and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca-dependent ER-associated pathway. J. Neurochem., 114, 795-809.
    • (2010) J. Neurochem. , vol.114 , pp. 795-809
    • Langou, K.1    Moumen, A.2    Pellegrino, C.3    Aebischer, J.4    Medina, I.5    Aebischer, P.6    Raoul, C.7
  • 12
    • 77951559589 scopus 로고    scopus 로고
    • Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity
    • Kim, S., Leal, S.S., Ben Halevy, D., Gomes, C.M. and Lev, S. (2010) Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity. J. Biol. Chem., 285, 13839-13849.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13839-13849
    • Kim, S.1    Leal, S.S.2    Ben Halevy, D.3    Gomes, C.M.4    Lev, S.5
  • 14
    • 0037130456 scopus 로고    scopus 로고
    • Drosophila VAP-33A directs bouton formation at neuromuscular junctions in a dosage-dependent manner
    • Pennetta, G., Hiesinger, P., Fabian-Fine, R., Meinertzhagen, I. and Bellen, H. (2002) Drosophila VAP-33A directs bouton formation at neuromuscular junctions in a dosage-dependent manner. Neuron, 35, 291-306.
    • (2002) Neuron , vol.35 , pp. 291-306
    • Pennetta, G.1    Hiesinger, P.2    Fabian-Fine, R.3    Meinertzhagen, I.4    Bellen, H.5
  • 15
    • 48449098142 scopus 로고    scopus 로고
    • A Drosophila model of ALS: human ALS-associated mutation in VAP33A suggests a dominant negative mechanism
    • Ratnaparkhi, A., Lawless, G.M., Schweizer, F.E., Golshani, P. and Jackson, G.R. (2008) A Drosophila model of ALS: human ALS-associated mutation in VAP33A suggests a dominant negative mechanism. PLoS ONE, 3, e2334.
    • (2008) PLoS ONE , vol.3
    • Ratnaparkhi, A.1    Lawless, G.M.2    Schweizer, F.E.3    Golshani, P.4    Jackson, G.R.5
  • 16
    • 55049136297 scopus 로고    scopus 로고
    • FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation
    • Prosser, D.C., Tran, D., Gougeon, P.Y., Verly, C. and Ngsee, J.K. (2008) FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation. J. Cell Sci., 121, 3052-3061.
    • (2008) J. Cell Sci. , vol.121 , pp. 3052-3061
    • Prosser, D.C.1    Tran, D.2    Gougeon, P.Y.3    Verly, C.4    Ngsee, J.K.5
  • 17
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP Proteins and is essential for Golgi-mediated transport
    • Peretti, D., Dahan, N., Shimoni, E., Hirschberg, K. and Lev, S. (2008) Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP Proteins and is essential for Golgi-mediated transport. Mol. Biol. Cell, 19, 3871-3884.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3871-3884
    • Peretti, D.1    Dahan, N.2    Shimoni, E.3    Hirschberg, K.4    Lev, S.5
  • 18
    • 58549088349 scopus 로고    scopus 로고
    • ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB
    • Suzuki, H., Kanekura, K., Levine, T.P., Kohno, K., Olkkonen, V.M., Aiso, S. and Matsuoka, M. (2009) ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB. J. Neurochem., 108, 973-985.
    • (2009) J. Neurochem. , vol.108 , pp. 973-985
    • Suzuki, H.1    Kanekura, K.2    Levine, T.P.3    Kohno, K.4    Olkkonen, V.M.5    Aiso, S.6    Matsuoka, M.7
  • 20
    • 14044268935 scopus 로고    scopus 로고
    • Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction
    • Amarilio, R., Ramachandran, S., Sabanay, H. and Lev, S. (2005) Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J. Biol. Chem., 280, 5934-5944.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5934-5944
    • Amarilio, R.1    Ramachandran, S.2    Sabanay, H.3    Lev, S.4
  • 21
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda, H., Han, S.M., Yang, Y., Tong, C., Lin, Y.Q., Mohan, K., Haueter, C., Zoghbi, A., Harati, Y., Kwan, J. et al. (2008) The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell, 133, 963-977.
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1    Han, S.M.2    Yang, Y.3    Tong, C.4    Lin, Y.Q.5    Mohan, K.6    Haueter, C.7    Zoghbi, A.8    Harati, Y.9    Kwan, J.10
  • 22
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E. and Caroni, P. (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci., 12, 627-636.
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 23
    • 66149156941 scopus 로고    scopus 로고
    • ER Stress and unfolded protein response in amyotrophic lateral sclerosis
    • Kanekura, K., Suzuki, H., Aiso, S. and Matsuoka, M. (2009) ER Stress and unfolded protein response in amyotrophic lateral sclerosis. Mol. Neurobiol., 39, 81-89.
    • (2009) Mol. Neurobiol. , vol.39 , pp. 81-89
    • Kanekura, K.1    Suzuki, H.2    Aiso, S.3    Matsuoka, M.4
  • 24
    • 79954633016 scopus 로고    scopus 로고
    • Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: mechanistic relationship and differential sensitivity to intervention
    • Tradewell, M.L., Cooper, L.A., Minotti, S. and Durham, H.D. (2011) Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: mechanistic relationship and differential sensitivity to intervention. Neurobiol. Dis., 42, 265-275.
    • (2011) Neurobiol. Dis. , vol.42 , pp. 265-275
    • Tradewell, M.L.1    Cooper, L.A.2    Minotti, S.3    Durham, H.D.4
  • 25
    • 77549088703 scopus 로고    scopus 로고
    • Calcium dysregulation in amyotrophic lateral sclerosis
    • Grosskreutz, J., Van Den Bosch, L. and Keller, B.U. (2010) Calcium dysregulation in amyotrophic lateral sclerosis. Cell Calcium, 47, 165-174.
    • (2010) Cell Calcium , vol.47 , pp. 165-174
    • Grosskreutz, J.1    Van Den Bosch, L.2    Keller, B.U.3
  • 27
    • 77955281658 scopus 로고    scopus 로고
    • PTPIP51-a myeloid lineage specific protein interacts with PTP1B in neutrophil granulocytes
    • Brobeil, A., Graf, M., Oeschger, S., Steger, K. and Wimmer, M. (2010) PTPIP51-a myeloid lineage specific protein interacts with PTP1B in neutrophil granulocytes. Blood Cells Mol. Dis., 45, 159-168.
    • (2010) Blood Cells Mol. Dis. , vol.45 , pp. 159-168
    • Brobeil, A.1    Graf, M.2    Oeschger, S.3    Steger, K.4    Wimmer, M.5
  • 28
    • 37249089881 scopus 로고    scopus 로고
    • RMD-1, a novel microtubule-associated protein, functions in chromosome segregation in Caenorhabditis elegans
    • Oishi, K., Okano, H. and Sawa, H. (2007) RMD-1, a novel microtubule-associated protein, functions in chromosome segregation in Caenorhabditis elegans. J. Cell Biol., 179, 1149-1162.
    • (2007) J. Cell Biol. , vol.179 , pp. 1149-1162
    • Oishi, K.1    Okano, H.2    Sawa, H.3
  • 29
    • 33747407345 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis
    • Lv, B.F., Yu, C.F., Chen, Y.Y., Lu, Y., Guo, J.H., Song, Q.S., Ma, D.L., Shi, T.P. and Wang, L. (2006) Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis. Apoptosis, 11, 1489-1501.
    • (2006) Apoptosis , vol.11 , pp. 1489-1501
    • Lv, B.F.1    Yu, C.F.2    Chen, Y.Y.3    Lu, Y.4    Guo, J.H.5    Song, Q.S.6    Ma, D.L.7    Shi, T.P.8    Wang, L.9
  • 30
    • 55049097922 scopus 로고    scopus 로고
    • PTPIP51, a novel 14-3-3 binding protein, regulates cell morphology and motility via Raf-ERK pathway
    • Yu, C., Han, W., Shi, T., Lv, B., He, Q., Zhang, Y., Li, T., Song, Q., Wang, L. and Ma, D. (2008) PTPIP51, a novel 14-3-3 binding protein, regulates cell morphology and motility via Raf-ERK pathway. Cell Signal., 20, 2208-2220.
    • (2008) Cell Signal , vol.20 , pp. 2208-2220
    • Yu, C.1    Han, W.2    Shi, T.3    Lv, B.4    He, Q.5    Zhang, Y.6    Li, T.7    Song, Q.8    Wang, L.9    Ma, D.10
  • 32
    • 0018331218 scopus 로고
    • Fractionation of human liver mitochondria: enzymic and morphological characterization of the inner and outer membranes as compared to rat liver mitochondria
    • Benga, G., Hodarnau, A., Tilinca, R., Porutiu, D., Dancea, S., Pop, V. and Wrigglesworth, J. (1979) Fractionation of human liver mitochondria: enzymic and morphological characterization of the inner and outer membranes as compared to rat liver mitochondria. J. Cell Sci., 35, 417-429.
    • (1979) J. Cell Sci. , vol.35 , pp. 417-429
    • Benga, G.1    Hodarnau, A.2    Tilinca, R.3    Porutiu, D.4    Dancea, S.5    Pop, V.6    Wrigglesworth, J.7
  • 33
    • 0035229003 scopus 로고    scopus 로고
    • Assaying protein import into mitochondria
    • Ryan, M.T., Voos, W. and Pfanner, N. (2001) Assaying protein import into mitochondria. Methods Cell Biol., 65, 189-215.
    • (2001) Methods Cell Biol. , vol.65 , pp. 189-215
    • Ryan, M.T.1    Voos, W.2    Pfanner, N.3
  • 35
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance, J.E. (1990) Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem., 265, 7248-7256.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 37
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito, O.M. and Scorrano, L. (2008) Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature, 456, 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 39
    • 68649116755 scopus 로고    scopus 로고
    • SR/ER-mitochondrial local communication: calcium and ROS
    • Csordas, G. and Hajnoczky, G. (2009) SR/ER-mitochondrial local communication: calcium and ROS. Biochim. Biophys. Acta, 1787, 1352-1362.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1352-1362
    • Csordas, G.1    Hajnoczky, G.2
  • 40
    • 37849053294 scopus 로고    scopus 로고
    • hVAPB, the causative gene of a heterogeneous group of motor neuron diseases in humans, is functionally interchangeable with its Drosophila homologue DVAP-33A at the neuromuscular junction
    • Chai, A., Withers, J., Koh, Y.H., Parry, K., Bao, H., Zhang, B., Budnik, V. and Pennetta, G. (2008) hVAPB, the causative gene of a heterogeneous group of motor neuron diseases in humans, is functionally interchangeable with its Drosophila homologue DVAP-33A at the neuromuscular junction. Hum. Mol. Genet., 17, 266-280.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 266-280
    • Chai, A.1    Withers, J.2    Koh, Y.H.3    Parry, K.4    Bao, H.5    Zhang, B.6    Budnik, V.7    Pennetta, G.8
  • 41
    • 0027973135 scopus 로고
    • A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusinol, A.E., Cui, Z., Chen, M.H. and Vance, J.E. (1994) A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J. Biol. Chem., 269, 27494-27502.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 42
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM)
    • Simmen, T., Lynes, E.M., Gesson, K. and Thomas, G. (2010) Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta, 1798, 1465-1473.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 44
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li, G., Mongillo, M., Chin, K.T., Harding, H., Ron, D., Marks, A.R. and Tabas, I. (2009) Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J. Cell Biol., 186, 783-792.
    • (2009) J. Cell Biol. , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 46
  • 47
    • 79959462293 scopus 로고    scopus 로고
    • The role of mitochondria in the pathogenesis of Amyotrophic Lateral Sclerosis
    • Duffy, L.M., Chapman, A.L., Shaw, P.J. and Grierson, A.J. (2011) The role of mitochondria in the pathogenesis of Amyotrophic Lateral Sclerosis. Neuropathol. Appl. Neurobiol., 37, 336-352.
    • (2011) Neuropathol. Appl. Neurobiol. , vol.37 , pp. 336-352
    • Duffy, L.M.1    Chapman, A.L.2    Shaw, P.J.3    Grierson, A.J.4
  • 48
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins, C.M., Jung, C., Ding, H. and Xu, Z. (2002) Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci., 22, RC215.
    • (2002) J. Neurosci. , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 50
    • 0037119407 scopus 로고    scopus 로고
    • Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice
    • Mattiazzi, M., D'Aurelio, M., Gajewski, C.D., Martushova, K., Kiaei, M., Beal, M.F. and Manfredi, G. (2002) Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J. Biol. Chem., 277, 29626-29633.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29626-29633
    • Mattiazzi, M.1    D'Aurelio, M.2    Gajewski, C.D.3    Martushova, K.4    Kiaei, M.5    Beal, M.F.6    Manfredi, G.7
  • 51
    • 3242703300 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria
    • Pasinelli, P., Belford, M.E., Lennon, N., Bacskai, B.J., Hyman, B.T., Trotti, D. and Brown, R.H. Jr. (2004) Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron, 43, 19-30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3    Bacskai, B.J.4    Hyman, B.T.5    Trotti, D.6    Brown Jr., R.H.7
  • 57
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan, X., Chiang, P.M., Price, D.L. and Wong, P.C. (2010) Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl Acad. Sci. USA, 107, 16325-16330.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 58
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice
    • Xu, Y.F., Gendron, T.F., Zhang, Y.J., Lin, W.L., D'Alton, S., Sheng, H., Casey, M.C., Tong, J., Knight, J., Yu, X. et al. (2010) Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J. Neurosci., 30, 10851-10859.
    • (2010) J. Neurosci. , vol.30 , pp. 10851-10859
    • Xu, Y.F.1    Gendron, T.F.2    Zhang, Y.J.3    Lin, W.L.4    D'Alton, S.5    Sheng, H.6    Casey, M.C.7    Tong, J.8    Knight, J.9    Yu, X.10
  • 59
    • 79953855830 scopus 로고    scopus 로고
    • TDP-43-induced death is associated with altered regulation of BIM and BCL-XL and attenuated by caspase-mediated TDP-43 cleavage
    • Suzuki, H., Lee, K. and Matsuoka, M. (2011) TDP-43-induced death is associated with altered regulation of BIM and BCL-XL and attenuated by caspase-mediated TDP-43 cleavage. J. Biol. Chem., 286, 13171-13183.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 63
    • 0030592773 scopus 로고    scopus 로고
    • The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine binding domain proteins in the yeast two-hybrid system
    • McLoughlin, D.M. and Miller, C.C.J. (1996) The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine binding domain proteins in the yeast two-hybrid system. FEBS Lett., 397, 197-200.
    • (1996) FEBS Lett , vol.397 , pp. 197-200
    • McLoughlin, D.M.1    Miller, C.C.J.2
  • 65
    • 17144429793 scopus 로고    scopus 로고
    • Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission
    • De Vos, K.J., Allan, V.J., Grierson, A.J. and Sheetz, M.P. (2005) Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission. Curr. Biol., 15, 678-683.
    • (2005) Curr. Biol. , vol.15 , pp. 678-683
    • De Vos, K.J.1    Allan, V.J.2    Grierson, A.J.3    Sheetz, M.P.4
  • 66
    • 0141521642 scopus 로고    scopus 로고
    • Expression of phosphatidylinositol (4,5) bisphosphate-specific pleckstrin homology domains alters direction but not the level of axonal transport of mitochondria
    • De Vos, K.J., Sable, J., Miller, K.E. and Sheetz, M.P. (2003) Expression of phosphatidylinositol (4,5) bisphosphate-specific pleckstrin homology domains alters direction but not the level of axonal transport of mitochondria. Mol. Biol. Cell, 14, 3636-3649.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3636-3649
    • De Vos, K.J.1    Sable, J.2    Miller, K.E.3    Sheetz, M.P.4
  • 67
    • 0034641135 scopus 로고    scopus 로고
    • Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria
    • De Vos, K., Severin, F., Van Herreweghe, F., Vancompernolle, K., Goossens, V., Hyman, A. and Grooten, J. (2000) Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria. J. Cell Biol., 149, 1207-1214.
    • (2000) J. Cell Biol. , vol.149 , pp. 1207-1214
    • De Vos, K.1    Severin, F.2    Van Herreweghe, F.3    Vancompernolle, K.4    Goossens, V.5    Hyman, A.6    Grooten, J.7
  • 68
    • 79953141458 scopus 로고    scopus 로고
    • Phosphorylation of kinesin light chain-1 at serine-460 modulates binding and trafficking of calsyntenin-1
    • Vagnoni, A., Rodriguez, L., Manser, C., De Vos, K.J. and Miller, C.C.J. (2011) Phosphorylation of kinesin light chain-1 at serine-460 modulates binding and trafficking of calsyntenin-1. J. Cell Sci., 124, 1032-1042.
    • (2011) J. Cell Sci. , vol.124 , pp. 1032-1042
    • Vagnoni, A.1    Rodriguez, L.2    Manser, C.3    De Vos, K.J.4    Miller, C.C.J.5


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