메뉴 건너뛰기




Volumn 6, Issue 13, 1997, Pages 2205-2212

Huntingtin-associated protein 1 (HAP1) interacts with the p150(Glued) subunit of dynactin

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHROMOSOME PROTEIN; CYTOSKELETON PROTEIN; DYNACTIN; HUNTINGTIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 0030726894     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/6.13.2205     Document Type: Article
Times cited : (287)

References (62)
  • 3
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • HD Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell, 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 5
    • 0027377151 scopus 로고
    • Correlation between the onset age of Huntington's disease and length of the trinucleotide repeat in IT-15
    • Stine,O.C., Pleasant,N., Franz,M.L., Abbott,M.H., Folstein,S.E. and Ross.C.A. (1993) Correlation between the onset age of Huntington's disease and length of the trinucleotide repeat in IT-15. Hum. Mol. Genet., 2, 1547-1549.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1547-1549
    • Stine, O.C.1    Pleasant, N.2    Franz, M.L.3    Abbott, M.H.4    Folstein, S.E.5    Ross, C.A.6
  • 16
    • 0029899868 scopus 로고    scopus 로고
    • Huntingtin-associated protein (HAP1): Discrete neuronal localizations in the brain resemble nitric oxide synthase
    • Li,X.-J., Sharp,A.H., Li,S.-H., Dawson,T.M., Snyder,S.H. and Ross,C.A. (1996) Huntingtin-associated protein (HAP1): discrete neuronal localizations in the brain resemble nitric oxide synthase. Proc. Natl. Acad. Sci. USA, 93, 4839-4844.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4839-4844
    • Li, X.-J.1    Sharp, A.H.2    Li, S.-H.3    Dawson, T.M.4    Snyder, S.H.5    Ross, C.A.6
  • 17
    • 0030767266 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 (HAP1) binds to a trio-like polypeptide, with a rac1 guanine nucleotide exchange factor domain
    • Colomer,V., Engelender,E., Sharp,A.H., Duan,K., Cooper,J.K., Lanahan,A., Lyford,G., Worley,P. and Ross,C.A. (1997) Huntingtin-associated protein 1 (HAP1) binds to a trio-like polypeptide, with a rac1 guanine nucleotide exchange factor domain. Hum. Mol. Genet., 6, 1519-1525.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1519-1525
    • Colomer, V.1    Engelender, E.2    Sharp, A.H.3    Duan, K.4    Cooper, J.K.5    Lanahan, A.6    Lyford, G.7    Worley, P.8    Ross, C.A.9
  • 18
    • 0025891138 scopus 로고
    • Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued
    • Holzbaur,E.L., Hammarback,J.A., Paschal,B.M., Kravit,N.G., Pfister,K.K. and Vallee,R.B. (1991) Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued. Nature, 351, 579-583.
    • (1991) Nature , vol.351 , pp. 579-583
    • Holzbaur, E.L.1    Hammarback, J.A.2    Paschal, B.M.3    Kravit, N.G.4    Pfister, K.K.5    Vallee, R.B.6
  • 19
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill,S.R., Schroer,T.A., Szilak,I., Steuer,E.R., Sheetz,M.P. and Cleveland,D.W. (1991) Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol., 6, 1639-1650.
    • (1991) J. Cell Biol. , vol.6 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 20
    • 0029742626 scopus 로고    scopus 로고
    • Functionally distinct isoforms of dynactin are expressed in human neurons
    • Tokito,M.K., Howland,D.S., Lee,V.M.-Y. and Holzbaur,E.L.F̀. (1996) Functionally distinct isoforms of dynactin are expressed in human neurons. Mol. Biol. Cell, 7, 1167-1180.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1167-1180
    • Tokito, M.K.1    Howland, D.S.2    Lee, V.M.-Y.3    Holzbaur, E.L.F.4
  • 21
    • 0028353367 scopus 로고
    • PCM-1, a 228-kD centrosome autoantigen with a distinct cell cycle distribution
    • Balczon,R., Bao,L. and Zimmer,W.E. (1994) PCM-1, a 228-kD centrosome autoantigen with a distinct cell cycle distribution. J. Cell Biol., 124, 783-794.
    • (1994) J. Cell Biol. , vol.124 , pp. 783-794
    • Balczon, R.1    Bao, L.2    Zimmer, W.E.3
  • 22
    • 0023357815 scopus 로고
    • The human mid-size neurofilament subunit: A repeated protein sequence and the relationship of its gene to the intermediate filament gene family
    • Myers,M.W., Lazzarini,R.A., Lee,V.M., Schlaepfer,W.W. and Nelson,D.L. (1987) The human mid-size neurofilament subunit: a repeated protein sequence and the relationship of its gene to the intermediate filament gene family. EMBO J., 6, 1617-1626.
    • (1987) EMBO J. , vol.6 , pp. 1617-1626
    • Myers, M.W.1    Lazzarini, R.A.2    Lee, V.M.3    Schlaepfer, W.W.4    Nelson, D.L.5
  • 23
    • 0030903317 scopus 로고    scopus 로고
    • Retroactive motors
    • Schnapp,B.J. (1997) Retroactive motors. Neuron, 18, 523-526.
    • (1997) Neuron , vol.18 , pp. 523-526
    • Schnapp, B.J.1
  • 24
    • 0026728645 scopus 로고
    • Molecular cloning of human CREB-2: An ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element
    • Karpinski,B.A., Morle,G.D., Huggenvik,J., Uhler,M.D. and Leiden,J.M. (1992) Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element. Proc. Natl. Acad. Sci. USA, 89, 4820-4824.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4820-4824
    • Karpinski, B.A.1    Morle, G.D.2    Huggenvik, J.3    Uhler, M.D.4    Leiden, J.M.5
  • 26
    • 0030459738 scopus 로고    scopus 로고
    • Transcriptional repression by RING finger protein TIF1β that interacts with the KRAB repressor domain of KOX1
    • Moosman,P., Georgiev,O., Le Douarin,B., Bourquin,J.-P. and Schaffner,W. (1996) Transcriptional repression by RING finger protein TIF1β that interacts with the KRAB repressor domain of KOX1. Nucleic Acids Res., 24, 4859-4867.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4859-4867
    • Moosman, P.1    Georgiev, O.2    Le Douarin, B.3    Bourquin, J.-P.4    Schaffner, W.5
  • 27
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas,A. (1996) Prediction and analysis of coiled-coil structures. Methods Enzymol., 266, 513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 29
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas,A. (1996) Coiled coils: new structures and new functions. Trends Biochem. Sci., 21, 357-406.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 357-406
    • Lupas, A.1
  • 30
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey,S.R. and Snyder,S.H. (1996) PIN: an associated protein inhibitor of neuronal nitric oxide synthase. Science, 274, 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 32
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran,E.A., Tokito,M.K., Karki,S. and Holzbaur,E.L.F. (1996) Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J. Cell Biol., 135, 1815-1829.
    • (1996) J. Cell Biol. , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 33
    • 0020955120 scopus 로고
    • Synapsin (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation
    • Huttner,W.B., Schiebler,W., Greengard,P. and Camilli,P. (1983) Synapsin (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation. J. Cell Biol., 96, 1374-1388.
    • (1983) J. Cell Biol. , vol.96 , pp. 1374-1388
    • Huttner, W.B.1    Schiebler, W.2    Greengard, P.3    Camilli, P.4
  • 34
    • 0344237032 scopus 로고
    • A 30,000-dalton membrane protein (p38) present in synaptic vesicles
    • Jahn,R., Schiebler,W., Ouimet,C. and Greengard,P. (1985) A 30,000-dalton membrane protein (p38) present in synaptic vesicles. Proc. Natl. Acad. Sci. USA, 82, 4137-4141.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4137-4141
    • Jahn, R.1    Schiebler, W.2    Ouimet, C.3    Greengard, P.4
  • 35
    • 0019851385 scopus 로고
    • Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue
    • Matthew,W.D., Tsaveler,L. and Reichardt,L.F. (1981) Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue. J. Cell Biol., 91, 257-269.
    • (1981) J. Cell Biol. , vol.91 , pp. 257-269
    • Matthew, W.D.1    Tsaveler, L.2    Reichardt, L.F.3
  • 36
    • 0345704610 scopus 로고
    • Establishment of noradrenergic clonal line of rat adrenal pheocromocytoma cells which respond to nerve growth factor
    • Green,L.A. and Tischler,A.S. (1976) Establishment of noradrenergic clonal line of rat adrenal pheocromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. USA, 73, 2424-2428.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2424-2428
    • Green, L.A.1    Tischler, A.S.2
  • 37
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea,E.K., Klemm,J.D., Kim,P.S. and Alber,T. (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science, 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 38
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer,D.A., Gill,S.R., Cooper,J.A., Heuser,J.E. and Schroer,T.A. (1994) Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J. Cell Biol., 126, 403-412.
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 39
  • 41
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki,S. and Holzbaur,E.L.F. (1995) Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. Biol. Chem., 270, 28806-28811.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.F.2
  • 44
    • 0020469397 scopus 로고
    • Genetic analysis of mutations at the Glued locus and interacting loci in Drosophila melanogaster
    • Harte,P.J., Kankel,D.R. (1982) Genetic analysis of mutations at the Glued locus and interacting loci in Drosophila melanogaster. Genetics, 101, 477-501.
    • (1982) Genetics , vol.101 , pp. 477-501
    • Harte, P.J.1    Kankel, D.R.2
  • 45
    • 0020743637 scopus 로고
    • Golgi and genetic mosaic analyses of visual system mutants in Drosophila melanogaster
    • Garen,S.H. and Kankel,D.R. (1983) Golgi and genetic mosaic analyses of visual system mutants in Drosophila melanogaster. Dev. Biol., 96, 445-466.
    • (1983) Dev. Biol. , vol.96 , pp. 445-466
    • Garen, S.H.1    Kankel, D.R.2
  • 46
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Corthésy-Theulaz,I., Pauloin,A. and Pfeffer,S.R. (1992) Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol., 118, 1333-1345.
    • (1992) J. Cell Biol. , vol.118 , pp. 1333-1345
    • Corthésy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 47
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath,K.R., Trimbur,G.M. and Burgess,D.R. (1994) Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol., 126, 661-675.
    • (1994) J. Cell Biol. , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 48
    • 10344242949 scopus 로고    scopus 로고
    • Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide processing enzyme
    • Alam,M.R., Caldwell,B.D., Johnson,R.C., Darlington,D.N., Mains,R.E. and Eipper,B.A. (1996) Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide processing enzyme. J. Biol. Chem., 271, 28636-28640.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28636-28640
    • Alam, M.R.1    Caldwell, B.D.2    Johnson, R.C.3    Darlington, D.N.4    Mains, R.E.5    Eipper, B.A.6
  • 49
    • 0030973545 scopus 로고    scopus 로고
    • Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine α-amidating monooxygenase, an integral membrane peptide-processing enzyme
    • Alam,M.R., Johnson,R.C., Darlington,D.N., Hand,T.A., Mains,R.E. and Eipper,B.A. (1997) Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine α-amidating monooxygenase, an integral membrane peptide-processing enzyme. J. Biol. Chem., 272, 12667-12675.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12667-12675
    • Alam, M.R.1    Johnson, R.C.2    Darlington, D.N.3    Hand, T.A.4    Mains, R.E.5    Eipper, B.A.6
  • 50
    • 0030035227 scopus 로고    scopus 로고
    • Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein
    • Milgram,S.L., Mains,R.E. and Eipper,B.A. (1996) Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein. J. Biol. Chem., 271, 17526-17535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17526-17535
    • Milgram, S.L.1    Mains, R.E.2    Eipper, B.A.3
  • 51
    • 0028077885 scopus 로고
    • Troponin T is capable of binding dystrophin via leucine zipper
    • Pearlman,J.A., Powaser,P.A., Elledge,S.J. and Caskey,C.T. (1994) Troponin T is capable of binding dystrophin via leucine zipper. FEBS Lett., 354, 183-186.
    • (1994) FEBS Lett. , vol.354 , pp. 183-186
    • Pearlman, J.A.1    Powaser, P.A.2    Elledge, S.J.3    Caskey, C.T.4
  • 52
    • 0028933382 scopus 로고
    • Kinectin, an essential anchor for kinesin-driven vesicle motility
    • Kumar,J., Yu,H. and Sheetz,M.P. (1995) Kinectin, an essential anchor for kinesin-driven vesicle motility. Science, 267, 1834-1837.
    • (1995) Science , vol.267 , pp. 1834-1837
    • Kumar, J.1    Yu, H.2    Sheetz, M.P.3
  • 53
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee,R.B. and Sheetz,M.P. (1996) Targeting of motor proteins. Science, 271, 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 54
    • 0025994787 scopus 로고
    • The identification of mammalian centrosomal antigens using human autoimmune anticentrosome antisera
    • Balczon,R. and West,K. (1991) The identification of mammalian centrosomal antigens using human autoimmune anticentrosome antisera. Cell Motil. Cytoskeleton, 20, 121-135.
    • (1991) Cell Motil. Cytoskeleton , vol.20 , pp. 121-135
    • Balczon, R.1    West, K.2
  • 55
    • 0021982117 scopus 로고
    • Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease
    • Graveland,G.A., Williams,R.S. and DiFiglia,M. (1985) Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease. Science, 227, 770-773.
    • (1985) Science , vol.227 , pp. 770-773
    • Graveland, G.A.1    Williams, R.S.2    DiFiglia, M.3
  • 56
    • 0027377217 scopus 로고
    • Evidence for neuronal degeneration and dendritic plasticity of pyramidal neurons of Huntington's disease: A quantitative Golgi study
    • Sotrel,A., Williams,R.S., Kaufmann,W.E. and Myers,R.H. (1993) Evidence for neuronal degeneration and dendritic plasticity of pyramidal neurons of Huntington's disease: a quantitative Golgi study. Neurology, 43, 2088-2096.
    • (1993) Neurology , vol.43 , pp. 2088-2096
    • Sotrel, A.1    Williams, R.S.2    Kaufmann, W.E.3    Myers, R.H.4
  • 58
  • 59
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast: Identification of mammalian proteins that react with the leucine zipper of Jun
    • Chevray,P.M. and Nathans,D. (1992) Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc. Natl. Acad. Sci. USA, 89, 5789-5793.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2
  • 60
    • 0028124463 scopus 로고
    • The two-hybrid system: An assay for protein-protein interactions
    • Fields,S. and Sternglanz,R. (1994) The two-hybrid system: an assay for protein-protein interactions. Trends Genet., 10, 286-292.
    • (1994) Trends Genet. , vol.10 , pp. 286-292
    • Fields, S.1    Sternglanz, R.2
  • 62
    • 0023545249 scopus 로고
    • PC12 pheocromocytoma cells: Culture, nerve growth factor treatment, and experimental exploitation
    • Green,L.A., Aletta,J.M., Rukenstein,A. and Green,S.H. (1987) PC12 pheocromocytoma cells: culture, nerve growth factor treatment, and experimental exploitation. Methods Enzymol., 147B, 207-216.
    • (1987) Methods Enzymol. , vol.147 B , pp. 207-216
    • Green, L.A.1    Aletta, J.M.2    Rukenstein, A.3    Green, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.