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Volumn 15, Issue 6, 2004, Pages 2771-2781

AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus

Author keywords

[No Author keywords available]

Indexed keywords

A KINASE ANCHORING PROTEIN 350; BINDING PROTEIN; CDC42 INTERACTING PROTEIN 4; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; FORMIN BINDING PROTEIN 17; FORMIN BINDING PROTEIN 17A; FORSKOLIN; GUANOSINE TRIPHOSPHATE; PROTEIN; PROTEIN CDC42; SMALL INTERFERING RNA; TYPE 2 PROTEIN KINASE A ANCHORING PROTEIN; UNCLASSIFIED DRUG; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 2542431138     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-10-0757     Document Type: Article
Times cited : (57)

References (57)
  • 2
    • 0031194076 scopus 로고    scopus 로고
    • A Cdc42 target protein with homology to the nonkinase domain of FER has a potential role in regulating the actin cytoskeleton
    • Aspenstrom, P. (1997). A Cdc42 target protein with homology to the nonkinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr. Biol. 7, 479-487.
    • (1997) Curr. Biol. , vol.7 , pp. 479-487
    • Aspenstrom, P.1
  • 3
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • Barr, F.A., and Short, B. (2003). Golgins in the structure and dynamics of the Golgi apparatus. Curr. Opin. Cell Biol. 15, 405-413.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 405-413
    • Barr, F.A.1    Short, B.2
  • 5
    • 0242322691 scopus 로고    scopus 로고
    • CLIC4 is enriched at cell-cell junctions and colocalizes with AKAP350 at the centrosome and midbody of cultured mammalian cells
    • Berryman, M.A., and Goldenring, J.R. (2003). CLIC4 is enriched at cell-cell junctions and colocalizes with AKAP350 at the centrosome and midbody of cultured mammalian cells. Cell Motil. Cytoskeleton 56, 159-172.
    • (2003) Cell Motil. Cytoskeleton , vol.56 , pp. 159-172
    • Berryman, M.A.1    Goldenring, J.R.2
  • 6
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp, T.R., Bernards, R., and Agami, R. (2002). A system for stable expression of short interfering RNAs in mammalian cells. Science 296, 550-553.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 7
    • 0141429975 scopus 로고    scopus 로고
    • The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus
    • Cabrera, M., Muniz, M., Hidalgo, J., Vega, L., Martin, M.E., and Velasco, A. (2003). The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus. Mol. Biol. Cell 14, 4114-4125.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4114-4125
    • Cabrera, M.1    Muniz, M.2    Hidalgo, J.3    Vega, L.4    Martin, M.E.5    Velasco, A.6
  • 8
    • 0029981652 scopus 로고    scopus 로고
    • Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan, D.C., Bedford, M.T., and Leder, P. (1996). Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15, 1045-1054.
    • (1996) EMBO J. , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 9
    • 0036790976 scopus 로고    scopus 로고
    • The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes
    • Chang, L., Adams, R.D., and Saltiel, A.R. (2002). The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes. Proc. Natl. Acad. Sci. USA 99, 12835-12840.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12835-12840
    • Chang, L.1    Adams, R.D.2    Saltiel, A.R.3
  • 10
    • 0036847903 scopus 로고    scopus 로고
    • Novel membrane traffic steps regulate the exocytosis of the Menkes disease ATPase
    • Cobbold, C., Ponnambalam, S., Francis, M.J., and Monaco, A.P. (2002). Novel membrane traffic steps regulate the exocytosis of the Menkes disease ATPase. Hum. Mol. Gen. 11, 2855-2866.
    • (2002) Hum. Mol. Gen. , vol.11 , pp. 2855-2866
    • Cobbold, C.1    Ponnambalam, S.2    Francis, M.J.3    Monaco, A.P.4
  • 11
    • 0030905468 scopus 로고    scopus 로고
    • Identification and characterization of a novel A-kinase-anchoring protein (AKAP120) from rabbit gastric parietal cells
    • Dransfield, D.T., Yeh, J.L., Bradford, A.J., and Goldenring, J.R. (1997). Identification and characterization of a novel A-kinase-anchoring protein (AKAP120) from rabbit gastric parietal cells. Biochem. J. 322, 801-808.
    • (1997) Biochem. J. , vol.322 , pp. 801-808
    • Dransfield, D.T.1    Yeh, J.L.2    Bradford, A.J.3    Goldenring, J.R.4
  • 12
  • 13
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S.M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 14
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian cdc42 is a Brefeldin A-sensitive component of the Golgi apparatus
    • Erickson, J.W., Zhan, Ch., Kahn, R.A., Evans, T., and Cerione, R.A. (1996). Mammalian cdc42 is a Brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem. 271, 26850-26854.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26850-26854
    • Erickson, J.W.1    Zhan, Ch.2    Kahn, R.A.3    Evans, T.4    Cerione, R.A.5
  • 15
    • 0035902604 scopus 로고    scopus 로고
    • The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia
    • Fuchs, U., et al. (2001). The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Proc. Natl. Acad. Sci. USA 98, 8756-8761.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8756-8761
    • Fuchs, U.1
  • 17
    • 0037416130 scopus 로고    scopus 로고
    • AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation
    • Ghosh, P., and Kornfeld, S. (2003). AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation. J. Cell Biol. 160, 699-708.
    • (2003) J. Cell Biol. , vol.160 , pp. 699-708
    • Ghosh, P.1    Kornfeld, S.2
  • 18
    • 0034574615 scopus 로고    scopus 로고
    • The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin
    • Gillingham, A.K., and Munro, S. (2000). The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin. EMBO Rep. 1, 524-529.
    • (2000) EMBO Rep. , vol.1 , pp. 524-529
    • Gillingham, A.K.1    Munro, S.2
  • 19
    • 0032422123 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42
    • Guinamard, R., Aspenstrom, P., Fougereau, M., Chavrier, P., and Guillemot, J.C. (1998). Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42. FEBS Lett. 434, 431-436.
    • (1998) FEBS Lett. , vol.434 , pp. 431-436
    • Guinamard, R.1    Aspenstrom, P.2    Fougereau, M.3    Chavrier, P.4    Guillemot, J.C.5
  • 20
    • 0344838402 scopus 로고    scopus 로고
    • Cdc-42-interacting protein 4 binds to huntingtin: Neuropathololgic and biological evidence for a role in Huntignton's disease
    • Holbert, S., Dedeoglu, A., Humbert, S., Saudou, F., Ferrante, R.J., and Neri, C. (2002). Cdc-42-interacting protein 4 binds to huntingtin: Neuropathololgic and biological evidence for a role in Huntignton's disease. Proc. Natl. Acad. Sci. USA 100, 2712-2717.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2712-2717
    • Holbert, S.1    Dedeoglu, A.2    Humbert, S.3    Saudou, F.4    Ferrante, R.J.5    Neri, C.6
  • 21
    • 0026091737 scopus 로고
    • Selective inhibition of transcytosis by brefeldin A in MDCK cells
    • Hunziker, W., Whitney, J.A., and Mellman, I. (1991). Selective inhibition of transcytosis by brefeldin A in MDCK cells. Cell 67, 617-627.
    • (1991) Cell , vol.67 , pp. 617-627
    • Hunziker, W.1    Whitney, J.A.2    Mellman, I.3
  • 22
    • 0033526005 scopus 로고    scopus 로고
    • GMAP-210, A cis-Golgi network-associated protein, is a minus end microtubule-binding protein
    • Infante, C., Ramos-Morales, F., Fedriani, C., Bornens, M., and Rios, R.M. (1999). GMAP-210, A cis-Golgi network-associated protein, is a minus end microtubule-binding protein. J. Cell Biol. 145, 83-98.
    • (1999) J. Cell Biol. , vol.145 , pp. 83-98
    • Infante, C.1    Ramos-Morales, F.2    Fedriani, C.3    Bornens, M.4    Rios, R.M.5
  • 24
    • 0027256671 scopus 로고
    • A high-affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II in the centrosome of human cells
    • Keryer, G., Rios, R.M., Landmark, B.F., Skalhegg, B., Lohmann, S.M., and Bornens, M. (1993). A high-affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II in the centrosome of human cells. Exp. Cell Res. 204, 230-40.
    • (1993) Exp. Cell Res. , vol.204 , pp. 230-240
    • Keryer, G.1    Rios, R.M.2    Landmark, B.F.3    Skalhegg, B.4    Lohmann, S.M.5    Bornens, M.6
  • 25
    • 0032719971 scopus 로고    scopus 로고
    • VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction
    • Lapierre, L.A., Tuma, P.L., Navarre, J., Goldenring, J.R., and Anderson, J.M. (1999). VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction, J. Cell Sci. 112, 3723-3732.
    • (1999) J. Cell Sci. , vol.112 , pp. 3723-3732
    • Lapierre, L.A.1    Tuma, P.L.2    Navarre, J.3    Goldenring, J.R.4    Anderson, J.M.5
  • 26
    • 0037452694 scopus 로고    scopus 로고
    • Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)
    • Li, H., Adamik, R., Pacheco-Rodriguez, G., Moss, J., and Vaughan, M. (2003), Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2). Proc. Natl. Acad. Sci. USA 100, 1627-1632.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1627-1632
    • Li, H.1    Adamik, R.2    Pacheco-Rodriguez, G.3    Moss, J.4    Vaughan, M.5
  • 27
    • 0032520827 scopus 로고    scopus 로고
    • Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1
    • Lin, W.J., Wyszynski, M., Madhaven, R., Sealock, R., Kim, J.U., and Sheng, M. (1998). Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. J. Neurosci. 18, 2017-2027.
    • (1998) J. Neurosci. , vol.18 , pp. 2017-2027
    • Lin, W.J.1    Wyszynski, M.2    Madhaven, R.3    Sealock, R.4    Kim, J.U.5    Sheng, M.6
  • 28
    • 0029038898 scopus 로고
    • A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus
    • Lindstedt, A.D., Foquet, M., Renz, M., Seelig, H.P., Glick, B.S., and Hauri, H.P. (1995). A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus. Proc. Natl. Acad. Sci. USA 92, 5102-5105.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5102-5105
    • Lindstedt, A.D.1    Foquet, M.2    Renz, M.3    Seelig, H.P.4    Glick, B.S.5    Hauri, H.P.6
  • 29
    • 0034678436 scopus 로고    scopus 로고
    • The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130
    • Lowe, M., Gonatas, N.K., and Warren, G. (2000). The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130. J. Cell Biol. 149, 341-356.
    • (2000) J. Cell Biol. , vol.149 , pp. 341-356
    • Lowe, M.1    Gonatas, N.K.2    Warren, G.3
  • 30
    • 0037423287 scopus 로고    scopus 로고
    • GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network
    • Luke, M.R., Kjer-Nielsen, L., Brown, D.L., Stow, J.L., and Gleeson, P.A. (2003). GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. J. Biol. Chem. 278, 4216-4226.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4216-4226
    • Luke, M.R.1    Kjer-Nielsen, L.2    Brown, D.L.3    Stow, J.L.4    Gleeson, P.A.5
  • 31
    • 0034705490 scopus 로고    scopus 로고
    • Effect of protein kinase A activity on the association of ADP-ribosylation factor 1 to Golgi membranes
    • Martin, M.E., Hidalgo, J., Rosa, J.L., Crottet, P., and Velasco, A. (2000). Effect of protein kinase A activity on the association of ADP-ribosylation factor 1 to Golgi membranes. J. Biol. Chem. 275, 19050-19059.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19050-19059
    • Martin, M.E.1    Hidalgo, J.2    Rosa, J.L.3    Crottet, P.4    Velasco, A.5
  • 32
    • 0029843580 scopus 로고    scopus 로고
    • A regulatory role for cAMP-dependent protein kinase in protein traffic along the exocytic route
    • Muniz, M., Martin, M.E., Hidalgo, J., and Velasco, A. (1996). A regulatory role for cAMP-dependent protein kinase in protein traffic along the exocytic route. J. Biol. Chem. 271, 30935-30941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30935-30941
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 33
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muniz, M., Martin, M.E., Hidalgo, J., and Velasco, A. (1997). Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl. Acad. Sci. USA 94, 14461-14466.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14461-14466
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 34
    • 0035860812 scopus 로고    scopus 로고
    • Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1
    • Richnau, N., and Aspenstrom, P. (2001). Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. J. Biol. Chem. 276, 35060-35070.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35060-35070
    • Richnau, N.1    Aspenstrom, P.2
  • 35
    • 0037223631 scopus 로고    scopus 로고
    • The Golgi apparatus at the cell centre
    • Rios, R.M., and Bornens, M. (2003). The Golgi apparatus at the cell centre. Curr. Opin. Cell Biol. 15, 60-66.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 60-66
    • Rios, R.M.1    Bornens, M.2
  • 36
    • 0023581760 scopus 로고
    • Antibodies to rat pancreas Golgi subfractions: Identification of a 58-kD cis-Golgi protein
    • Saraste, J., Palade, G.E., and Farquhar, M.G. (1987). Antibodies to rat pancreas Golgi subfractions: identification of a 58-kD cis-Golgi protein. J. Cell Biol. 105, 2021-2029.
    • (1987) J. Cell Biol. , vol.105 , pp. 2021-2029
    • Saraste, J.1    Palade, G.E.2    Farquhar, M.G.3
  • 38
    • 0037174956 scopus 로고    scopus 로고
    • AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member
    • Shanks, R.A., Larocca, M.C., Berryman, M., Edwards, J.C., Urushidani, T., Navarre, J., and Goldenring, J.R. (2002b). AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member. J. Biol. Chem. 277, 40973-40980.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40973-40980
    • Shanks, R.A.1    Larocca, M.C.2    Berryman, M.3    Edwards, J.C.4    Urushidani, T.5    Navarre, J.6    Goldenring, J.R.7
  • 39
    • 0037174869 scopus 로고    scopus 로고
    • AKAP350 at the Golgi apparatus. I. Identification of a distinct Golgi apparatus targeting motif in AKAP350
    • Shanks, R.A., Steadman, B.T., Schmidt, P.H., and Goldenring, J.R. (2002a). AKAP350 at the Golgi apparatus. I. Identification of a distinct Golgi apparatus targeting motif in AKAP350. J. Biol. Chem. 277, 40967-40972.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40967-40972
    • Shanks, R.A.1    Steadman, B.T.2    Schmidt, P.H.3    Goldenring, J.R.4
  • 40
    • 0035842903 scopus 로고    scopus 로고
    • A GRASP55-Rab2 effector complex linking Golgi structure to membrane traffic
    • Short, B., Preisinger, C., Korner, R., Kopajtich, R., Byron, O., and Barr, F.A. (2001). A GRASP55-Rab2 effector complex linking Golgi structure to membrane traffic. J. Cell Biol. 155, 877-883.
    • (2001) J. Cell Biol. , vol.155 , pp. 877-883
    • Short, B.1    Preisinger, C.2    Korner, R.3    Kopajtich, R.4    Byron, O.5    Barr, F.A.6
  • 41
  • 42
    • 0036387280 scopus 로고    scopus 로고
    • Centrosomal anchoring of the protein kinase CK1delta mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450
    • Sillibourne, J.E., Milne, D.M., Takahashi, M., Ono, Y., and Meek, D.W. (2002). Centrosomal anchoring of the protein kinase CK1delta mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450. J Mol Biol. 322, 785-797.
    • (2002) J Mol Biol. , vol.322 , pp. 785-797
    • Sillibourne, J.E.1    Milne, D.M.2    Takahashi, M.3    Ono, Y.4    Meek, D.W.5
  • 43
    • 0036702196 scopus 로고    scopus 로고
    • Regulating the actin cytoskeleton during vesicular transport
    • Stammer, M. (2002). Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14, 428-433.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 428-433
    • Stammer, M.1
  • 44
    • 0037119467 scopus 로고    scopus 로고
    • Transforming acidic coiled-coil-containing protein 4 interacts with centrosomal AKAP350 and the mitotic spindle apparatus
    • Steadman, B.T., Schmidt, P.H., Shanks, R.A., Lapierre, L.A., and Goldenring, J.R. (2002). Transforming acidic coiled-coil-containing protein 4 interacts with centrosomal AKAP350 and the mitotic spindle apparatus. J. Biol. Chem. 277, 30165-30176.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30165-30176
    • Steadman, B.T.1    Schmidt, P.H.2    Shanks, R.A.3    Lapierre, L.A.4    Goldenring, J.R.5
  • 45
    • 0034602398 scopus 로고    scopus 로고
    • Association of immature hypophosphorylated protein kinase C epsilon with an anchoring protein CG-NAP
    • Takahashi, M., Mukai, H., Oishi, K., Isagawa, T., and Ono, Y. (2000). Association of immature hypophosphorylated protein kinase C epsilon with an anchoring protein CG-NAP. J. Biol. Chem. 275, 34592-34596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34592-34596
    • Takahashi, M.1    Mukai, H.2    Oishi, K.3    Isagawa, T.4    Ono, Y.5
  • 46
    • 0033546152 scopus 로고    scopus 로고
    • Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus
    • Takahashi, M., Shibata, H., Shimakawa, M., Miyamoto, M., Mukai, H., and Ono, Y. (1999). Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus. J. Biol. Chem. 274, 17267-17274.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17267-17274
    • Takahashi, M.1    Shibata, H.2    Shimakawa, M.3    Miyamoto, M.4    Mukai, H.5    Ono, Y.6
  • 47
    • 0036736094 scopus 로고    scopus 로고
    • Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex
    • Takahashi, M., Yamagiwa, A., Nishimura, T., Mukai, H., and Ono, Y. (2002). Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex. Mol. Biol. Cell 13, 3235-3245.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3235-3245
    • Takahashi, M.1    Yamagiwa, A.2    Nishimura, T.3    Mukai, H.4    Ono, Y.5
  • 48
    • 0035933817 scopus 로고    scopus 로고
    • Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area
    • Tasken, K.A., Collas, P., Kemmner, W.A., Witczak, O., Conti, M., and Tasken, K. (2001). Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area. J. Biol. Chem. 276, 21999-22002.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21999-22002
    • Tasken, K.A.1    Collas, P.2    Kemmner, W.A.3    Witczak, O.4    Conti, M.5    Tasken, K.6
  • 49
    • 0034677932 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules
    • Tian, L., Nelson, D.L., and Stewart, D.M. (2000). Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J. Biol. Chem. 275, 7854-7861.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7854-7861
    • Tian, L.1    Nelson, D.L.2    Stewart, D.M.3
  • 50
    • 0034467145 scopus 로고    scopus 로고
    • Molecular cloning and chromosomal localization of human salt-tolerant protein
    • Tsuji, E., and Tsuji, Y. (2000). Molecular cloning and chromosomal localization of human salt-tolerant protein. Genetica 108, 259-262.
    • (2000) Genetica , vol.108 , pp. 259-262
    • Tsuji, E.1    Tsuji, Y.2
  • 51
    • 0034800091 scopus 로고    scopus 로고
    • Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells
    • Valderrama, F., Duran, J.M., Babia, T., Barth, H., Renau-Piqueras, J., and Egea, G. (2001). Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells. Traffic 2, 717-726.
    • (2001) Traffic , vol.2 , pp. 717-726
    • Valderrama, F.1    Duran, J.M.2    Babia, T.3    Barth, H.4    Renau-Piqueras, J.5    Egea, G.6
  • 52
    • 0028301797 scopus 로고
    • Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells
    • Wagner, M., Rajasekaran, A.K., Hanzel, D.K., Mayor, S., and Rodriguez-Boulan, E. (1994). Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells. J. Cell Sci. 107, 933-943.
    • (1994) J. Cell Sci. , vol.107 , pp. 933-943
    • Wagner, M.1    Rajasekaran, A.K.2    Hanzel, D.K.3    Mayor, S.4    Rodriguez-Boulan, E.5
  • 53
    • 0035809910 scopus 로고    scopus 로고
    • The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins
    • Walenta, J.H., Didier, A.J., Liu, X., and Kramer, H. (2001). The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins. J. Cell Biol. 152, 923-934.
    • (2001) J. Cell Biol. , vol.152 , pp. 923-934
    • Walenta, J.H.1    Didier, A.J.2    Liu, X.3    Kramer, H.4
  • 56
    • 0345435932 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450
    • Witczak, O., Skalhegg, B.S., Keryer, G., Bornens, M., Tasken, K., Jahnsen, T., and Orstavik, S. (1999). Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. EMBO J. 18, 1858-1868.
    • (1999) EMBO J. , vol.18 , pp. 1858-1868
    • Witczak, O.1    Skalhegg, B.S.2    Keryer, G.3    Bornens, M.4    Tasken, K.5    Jahnsen, T.6    Orstavik, S.7
  • 57
    • 0036677592 scopus 로고    scopus 로고
    • Casein Kinase I regulates membrane binding by ARF GAP1
    • Yu, S., and Roth, M.G. (2002). Casein Kinase I regulates membrane binding by ARF GAP1. Mol. Biol. Cell 13, 2559-2570.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2559-2570
    • Yu, S.1    Roth, M.G.2


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