메뉴 건너뛰기




Volumn 24, Issue 6, 2013, Pages 848-857

CAMP-stimulated phosphorylation of diaphanous 1 regulates protein stability and interaction with binding partners in adrenocortical cells

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BETA ACTIN; BETA TUBULIN; CYCLIC AMP; DIAPHANOUS HOMOLOGUE 1 PROTEIN; DYNAMIN I; KINESIN; MITOGEN ACTIVATED PROTEIN KINASE; RHO FACTOR; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84875167919     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-08-0597     Document Type: Article
Times cited : (14)

References (61)
  • 1
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts AS (2001). Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J Biol Chem 276, 2824-2830.
    • (2001) J Biol Chem , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 2
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7
    • DOI 10.1074/jbc.273.15.8616
    • Alberts AS, Bouquin N, Johnston LH, Treisman R (1998). Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J Biol Chem 273, 8616-8622. (Pubitemid 28176136)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 7
    • 0032489802 scopus 로고    scopus 로고
    • Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid
    • DOI 10.1083/jcb.141.1.175
    • Cook TA, Nagasaki T, Gundersen GG (1998). Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid. J Cell Biol 141, 175-185. (Pubitemid 28182650)
    • (1998) Journal of Cell Biology , vol.141 , Issue.1 , pp. 175-185
    • Cook, T.A.1    Nagasaki, T.2    Gundersen, G.G.3
  • 8
    • 0036854328 scopus 로고    scopus 로고
    • The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization
    • DOI 10.1091/mbc.02-06-0092
    • Copeland JW, Treisman R (2002). The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol Biol Cell 13, 4088-4099. (Pubitemid 35398572)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.11 , pp. 4088-4099
    • Copeland, J.W.1    Treisman, R.2
  • 9
    • 67749120701 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division
    • De Ward AD, Alberts AS (2009). Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division. J Biol Chem 284, 20061-20069.
    • (2009) J Biol Chem , vol.284 , pp. 20061-20069
    • De Ward, A.D.1    Alberts, A.S.2
  • 11
    • 3543020962 scopus 로고    scopus 로고
    • Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex
    • DOI 10.1038/sj.emboj.7600287
    • Diviani D, Abuin L, Cotecchia S, Pansier L (2004). Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex. EMBO J 23, 2811-2820. (Pubitemid 39013553)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2811-2820
    • Diviani, D.1    Abuin, L.2    Cotecchia, S.3    Pansier, L.4
  • 12
    • 0035941212 scopus 로고    scopus 로고
    • AKAP-Lbc anchors protein kinase A and nucleates Galpha12-selective Rho-mediated stress fiber formation
    • Diviani D, Soderling J, Scott JD (2001). AKAP-Lbc anchors protein kinase A and nucleates Galpha12-selective Rho-mediated stress fiber formation. J Biol Chem 276, 44247-44257.
    • (2001) J Biol Chem , vol.276 , pp. 44247-44257
    • Diviani, D.1    Soderling, J.2    Scott, J.D.3
  • 14
    • 33845459805 scopus 로고    scopus 로고
    • The formin mDia regulates GSK3β through novel PKCs to promote microtubule stabilization but not MTOC reorientation in migrating fibroblasts
    • DOI 10.1091/mbc.E05-10-0914
    • Eng CH, Huckaba TM, Gundersen GG (2006). The formin mDia regulates GSK3beta through novel PKCs to promote microtubule stabilization but not MTOC reorientation in migrating fibroblasts. Mol Biol Cell 17, 5004-5016. (Pubitemid 44907346)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.12 , pp. 5004-5016
    • Eng, C.H.1    Huckaba, T.M.2    Gundersen, G.G.3
  • 15
    • 38549169589 scopus 로고    scopus 로고
    • Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling
    • DOI 10.1007/s00018-007-7325-2
    • Fairn GD, McMaster CR (2008). Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling. Cell Mol Sci 65, 228-236. (Pubitemid 351161484)
    • (2008) Cellular and Molecular Life Sciences , vol.65 , Issue.2 , pp. 228-236
    • Fairn, G.D.1    McMaster, C.R.2
  • 16
    • 35948978460 scopus 로고    scopus 로고
    • Moving mitochondria: Establishing distribution of an essential organelle
    • DOI 10.1111/j.1600-0854.2007.00644.x
    • Frederick RL, Shaw JM (2007). Moving mitochondria: establishing distribution of an essential organelle. Traffic 8, 1668-1675. (Pubitemid 350066679)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1668-1675
    • Frederick, R.L.1    Shaw, J.M.2
  • 17
    • 0037182585 scopus 로고    scopus 로고
    • LIM kinase and diaphanous cooperate to regulate serum response factor and actin dynamics
    • DOI 10.1083/jcb.200203126
    • Geneste O, Copeland JW, Treisman R (2002). LIM kinase and diaphanous cooperate to regulate serum response factor and actin dynamics. J Cell Biol 157, 831-838. (Pubitemid 34847820)
    • (2002) Journal of Cell Biology , vol.157 , Issue.5 , pp. 831-838
    • Geneste, O.1    Copeland, J.W.2    Treisman, R.3
  • 18
    • 34948891576 scopus 로고    scopus 로고
    • The RhoA effector mDiaphanous regulates MyoD expression and cell cycle progression via SRF-dependent and SRF-independent pathways
    • DOI 10.1242/jcs.006619
    • Gopinath SD, Narumiya S, Dhawan J (2007). The RhoA effector mDiaphanous regulates MyoD expression and cell cycle progression via SRF-dependent and SRF-independent pathways. J Cell Sci 120, 3086-3098. (Pubitemid 47517091)
    • (2007) Journal of Cell Science , vol.120 , Issue.17 , pp. 3086-3098
    • Gopinath, S.D.1    Narumiya, S.2    Dhawan, J.3
  • 19
    • 9244243320 scopus 로고    scopus 로고
    • Hither and yon: A review of bi-directional microtubule-based transport
    • DOI 10.1088/1478-3967/1/2/R01, PII S1478396704812373, R01
    • Gross SP (2004). Hither and yon: a review of bi-directional microtubulebased transport. Phys Biol 1, R1-R11. (Pubitemid 44362300)
    • (2004) Physical Biology , vol.1 , Issue.2
    • Gross, S.P.1
  • 20
    • 0031013732 scopus 로고    scopus 로고
    • The roles of calmodulin, actin, and vimentin in steroid synthesis by adrenal cells
    • DOI 10.1016/S0039-128X(96)00179-1, PII S0039128X96001798
    • Hall PF (1997). The roles of calmodulin, actin, and vimentin in steroid synthesis by adrenal cells. Steroids 62, 185-189. (Pubitemid 27067003)
    • (1997) Steroids , vol.62 , Issue.1 , pp. 185-189
    • Hall, P.F.1
  • 21
    • 43749120730 scopus 로고    scopus 로고
    • Biochemical characterization of the Rho GTPaseregulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in platelets
    • Higashi T et al. (2008). Biochemical characterization of the Rho GTPaseregulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in platelets. J Biol Chem 283, 8746-8755.
    • (2008) J Biol Chem , vol.283 , pp. 8746-8755
    • Higashi, T.1
  • 22
    • 0035141074 scopus 로고    scopus 로고
    • Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1
    • DOI 10.1038/35050598
    • Ishizaki T, Morishima Y, Okamoto M, Furuyashiki T, Kato T, Narumiya S (2001). Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nat Cell Biol 3, 8-14. (Pubitemid 32114826)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 8-14
    • Ishizaki, T.1    Morishima, Y.2    Okamoto, M.3    Furuyashiki, T.4    Kato, T.5    Narumiya, S.6
  • 24
    • 41549145379 scopus 로고    scopus 로고
    • Mechanisms of adrenocorticotropin-induced activation of extracellularly regulated kinase 1/2 mitogen-activated protein kinase in the human H295R adrenal cell line
    • DOI 10.1210/en.2007-0949
    • Janes ME, Chu KM, Clark AJ, King PJ (2008). Mechanisms of adrenocorticotropin-induced activation of extracellularly regulated kinase 1/2 mitogen-activated protein kinase in the human H295R adrenal cell line. Endocrinology 149, 1898-1905. (Pubitemid 351468309)
    • (2008) Endocrinology , vol.149 , Issue.4 , pp. 1898-1905
    • Janes, M.E.1    Chu, K.M.E.2    Clark, A.J.L.3    King, P.J.4
  • 25
    • 42549142892 scopus 로고    scopus 로고
    • Mdia function is critical for the cell suicide program triggered by farnesyl transferase inhibition
    • Kamasani U, Duhadaway JB, Alberts AS, Prendergast GC (2007). mDia function is critical for the cell suicide program triggered by farnesyl transferase inhibition. Cancer Biol Ther 6, 1422-1427. (Pubitemid 351590352)
    • (2007) Cancer Biology and Therapy , vol.6 , Issue.9 , pp. 1422-1427
    • Kamasani, U.1    DuHadaway, J.B.2    Alberts, A.S.3    Prendergast, G.C.4
  • 26
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • Kim W et al. (2001). Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 44, 325-340.
    • (2001) Mol Cell , vol.44 , pp. 325-340
    • Kim, W.1
  • 28
    • 0035798219 scopus 로고    scopus 로고
    • Ht31: The first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling
    • DOI 10.1016/S0014-5793(01)02995-7, PII S0014579301029957
    • Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W (2001). Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett 507, 264-268. (Pubitemid 33030247)
    • (2001) FEBS Letters , vol.507 , Issue.3 , pp. 264-268
    • Klussmann, E.1    Edemir, B.2    Pepperle, B.3    Tamma, G.4    Henn, V.5    Klauschenz, E.6    Hundsrucker, C.7    Maric, K.8    Rosenthal, W.9
  • 29
    • 33645095368 scopus 로고    scopus 로고
    • Videomicroscopic studies of the movement of mitochondria
    • Kulik AV, Gioeva FK, Minin AA (2002). Videomicroscopic studies of the movement of mitochondria. Russ J Dev Biol 33, 299-305.
    • (2002) Russ J Dev Biol , vol.33 , pp. 299-305
    • Kulik, A.V.1    Gioeva, F.K.2    Minin, A.A.3
  • 31
    • 0034812357 scopus 로고    scopus 로고
    • The regulation of MAPKs in Y1 mouse adrenocortical tumor cells
    • DOI 10.1210/en.142.10.4282
    • Le T, Schimmer BP (2001). The regulation of MAPKs in Y1 mouse adrenocortical tumor cells. Endocrinology 142, 4282-4287. (Pubitemid 32907055)
    • (2001) Endocrinology , vol.142 , Issue.10 , pp. 4282-4287
    • Le, T.1    Schimmer, B.P.2
  • 33
    • 77956019869 scopus 로고    scopus 로고
    • RhoA and DIAPH1 mediate adrenocorticotropinstimulated cortisol biosynthesis by regulating mitochondrial trafficking
    • Li D, Sewer MB (2010). RhoA and DIAPH1 mediate adrenocorticotropinstimulated cortisol biosynthesis by regulating mitochondrial trafficking. Endocrinology 151, 4313-4323.
    • (2010) Endocrinology , vol.151 , pp. 4313-4323
    • Li, D.1    Sewer, M.B.2
  • 34
    • 0034524087 scopus 로고    scopus 로고
    • Role of ERK/MAP kinase in mitogenic interaction between ACTH and FGF2 in mouse Y1 adrenocortical tumor cells
    • Lotfi CF, Costa ET, Schwindt TT, Armelin HA (2000). Role of ERK/MAP kinase in mitogenic interaction between ACTH and FGF2 in mouse Y1 adrenocortical tumor cells. Endocr Res 26, 873-877. (Pubitemid 32053114)
    • (2000) Endocrine Research , vol.26 , Issue.4 , pp. 873-877
    • Lotfi, C.F.P.1    Costa, E.T.2    Schwindt, T.T.3    Armelin, H.A.4
  • 35
    • 0029960434 scopus 로고    scopus 로고
    • Depletion of lysophosphatidic acid triggers a loss of oriented detyrosinated microtubules in motile fibroblasts
    • Nagasaki T, Gundersen GG (1996). Depletion of lysophosphatidic acid triggers a loss of oriented detyrosinated microtubules in motile fibroblasts. J Cell Sci 109, 2461-2469. (Pubitemid 26377521)
    • (1996) Journal of Cell Science , vol.109 , Issue.10 , pp. 2461-2469
    • Nagasaki, T.1    Gundersen, G.G.2
  • 36
    • 68549122708 scopus 로고    scopus 로고
    • Rho signaling, ROCK and mDia1, in transformation, metastasis, and invasion
    • Narumiya S, Tanji M, Ishizaki T (2009). Rho signaling, ROCK and mDia1, in transformation, metastasis, and invasion. Cancer Metastasis Rev 28, 65-76.
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 65-76
    • Narumiya, S.1    Tanji, M.2    Ishizaki, T.3
  • 37
    • 2342637722 scopus 로고    scopus 로고
    • Oxysterol binding proteins: In more than one place at one time?
    • DOI 10.1139/o03-088
    • Olkkonen VM, Levine TP (2004). Oxysterol binding proteins: in more than one place at one time. Biochem Cell Biol 82, 87-98. (Pubitemid 38580876)
    • (2004) Biochemistry and Cell Biology , vol.82 , Issue.1 , pp. 87-98
    • Olkkonen, V.M.1    Levine, T.P.2
  • 38
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • DOI 10.1016/j.molcel.2005.04.002, PII S1097276505012268
    • Otomo T, Otomo C, Tomchick DR, Machius M, Rosen MK (2005). Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol Cell 18, 273-281. (Pubitemid 41350533)
    • (2005) Molecular Cell , vol.18 , Issue.3 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    Machius, M.4    Rosen, M.K.5
  • 39
    • 0034907213 scopus 로고    scopus 로고
    • Mdia mediates Rho-regulated formation and orientation of stable microtubules
    • DOI 10.1038/35087035
    • Palazzo AF, Cook TA, Alberts AS, Gundersen GG (2001a). mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat Cell Biol 3, 723-729. (Pubitemid 32734250)
    • (2001) Nature Cell Biology , vol.3 , Issue.8 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 41
    • 77952314344 scopus 로고    scopus 로고
    • Oxysterol-binding proteins
    • Ridgway N (2010). Oxysterol-binding proteins. Subcell Biochem 51, 159-182.
    • (2010) Subcell Biochem , vol.51 , pp. 159-182
    • Ridgway, N.1
  • 42
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: A molecular view on the regulation of human formins
    • Schonichen A, Geyer M (2010). Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim Biophys Acta 1803, 152-163.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 152-163
    • Schonichen, A.1    Geyer, M.2
  • 44
    • 77950632472 scopus 로고    scopus 로고
    • Vimentin is a functional partner of hormone sensitive lipase and facilitates lipolysis
    • Shen WJ, Patel S, Eriksson JE, Kraemer FB (2010). Vimentin is a functional partner of hormone sensitive lipase and facilitates lipolysis. J Proteome Res 9, 1786-1794.
    • (2010) J Proteome Res , vol.9 , pp. 1786-1794
    • Shen, W.J.1    Patel, S.2    Eriksson, J.E.3    Kraemer, F.B.4
  • 46
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • DOI 10.1016/S1097-2765(04)00059-0, PII S1097276504000590
    • Shimada A, Nyitrai M, Vetter IR, Kuhlmann D, Bugyi B, Narumiya S, Geeves MA, Wittinghofer A (2004). The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. Mol Cell 13, 511-522. (Pubitemid 38299379)
    • (2004) Molecular Cell , vol.13 , Issue.4 , pp. 511-522
    • Shimada, A.1    Nyitrai, M.2    Vetter, I.R.3    Kuhlmann, D.4    Bugyi, B.5    Narumiya, S.6    Geeves, M.A.7    Wittinghofer, A.8
  • 47
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • Stefan CJ, Manford AG, Baird D, Yamada-Hanff Mao Y, Emr SD (2011). Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites. Cell 144, 389-401.
    • (2011) Cell , vol.144 , pp. 389-401
    • Stefan, C.J.1    Manford, A.G.2    Baird, D.3    Yamada-Hanff Mao, Y.4    Emr, S.D.5
  • 48
    • 0037112565 scopus 로고    scopus 로고
    • Characterization of the interactions between the small GTPase RhoA and its guanine nucleotide exchange factors
    • DOI 10.1016/S0003-2697(02)00382-2, PII S0003269702003822
    • Tan YC, Wu H, Wang WN, Zheng Y, Wang ZX (2002). Characterization of the interactions between the small GTPase RhoA and its guanine nucleotide exchange factors. Anal Biochem 310, 156-162. (Pubitemid 35388256)
    • (2002) Analytical Biochemistry , vol.310 , Issue.2 , pp. 156-162
    • Tan, Y.-C.1    Wu, H.2    Wang, W.-N.3    Zheng, Y.4    Wang, Z.-X.5
  • 49
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
    • DOI 10.1016/S0092-8674(00)81459-2
    • Tanaka Y, Kanai Y, Okada Y, Nonaka S, Takeda S, Harada A, Hirokawa N (1998). Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93, 1147-1158. (Pubitemid 28307420)
    • (1998) Cell , vol.93 , Issue.7 , pp. 1147-1158
    • Tanaka, Y.1    Kanai, Y.2    Okada, Y.3    Nonaka, S.4    Takeda, S.5    Harada, A.6    Hirokawa, N.7
  • 50
    • 78650637171 scopus 로고    scopus 로고
    • Rho-mDia1 pathway is required for adhesion, migration, and T-cell stimulation in dendritic cells
    • Tanizaki H et al. (2010). Rho-mDia1 pathway is required for adhesion, migration, and T-cell stimulation in dendritic cells. Blood 116, 5875-5884.
    • (2010) Blood , vol.116 , pp. 5875-5884
    • Tanizaki, H.1
  • 51
    • 70350446761 scopus 로고    scopus 로고
    • Traffic control: Regulation of kinesin motors
    • Verhey KJ, Hammond JW (2009). Traffic control: regulation of kinesin motors. Nat Rev Mol Cell Biol 10, 765-777.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 765-777
    • Verhey, K.J.1    Hammond, J.W.2
  • 52
    • 0036472330 scopus 로고    scopus 로고
    • Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments
    • DOI 10.1042/0264-6021:3610461
    • Wang C, Je Bailey L, Ridgway N (2002). Oxytsterol-binding-protein (OSBP) - related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate flaments. Biochem J 361, 461-472. (Pubitemid 34177815)
    • (2002) Biochemical Journal , vol.361 , Issue.3 , pp. 461-472
    • Wang, C.1    JeBailey, L.2    Ridgway, N.D.3
  • 53
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1, 136-143. (Pubitemid 129656017)
    • (1999) Nature Cell Biology , vol.1 , Issue.3 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 54
    • 0030911424 scopus 로고    scopus 로고
    • P140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • DOI 10.1093/emboj/16.11.3044
    • Watanabe N M P, Reid T, Ishizaki T, Watanabe G, Kakizuka A, Saito Y, Nakao K, Jockusch BM, Narumiya S (1997). p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J 16, 3044-3056. (Pubitemid 27234944)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6    Saito, Y.7    Nakao, K.8    Jockusch, B.M.9    Narumiya, S.10
  • 56
    • 40949117966 scopus 로고    scopus 로고
    • Functional interactions between phosphatase POPX2 and mDia modulate RhoA pathways
    • DOI 10.1242/jcs.013557
    • Xie Y, Tan EJ, Wee S, Manser E, Lim L, Koh CG (2008). Functional interactions between phosphatase POPX2 and mDia modulate RhoA pathways. J Cell Sci 121, 514-521. (Pubitemid 351405060)
    • (2008) Journal of Cell Science , vol.121 , Issue.4 , pp. 514-521
    • Xie, Y.1    Tan, E.-J.2    Wee, S.3    Manser, E.4    Lim, L.5    Koh, C.-G.6
  • 57
    • 0035947559 scopus 로고    scopus 로고
    • Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicular transport
    • Xu Y, Liu Y, Ridgway ND, McMaster CR (2001). Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicular transport. J Biol Chem 276, 18407-18414.
    • (2001) J Biol Chem , vol.276 , pp. 18407-18414
    • Xu, Y.1    Liu, Y.2    Ridgway, N.D.3    McMaster, C.R.4
  • 60
    • 33645966803 scopus 로고    scopus 로고
    • Interaction of Moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection
    • Yueh A, Leung J, Bhattacharyya S, Perrone LA, De Los Santos K, Pu SY, Goff SP (2006). Interaction of Moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection. J Virol 80, 342-352.
    • (2006) J Virol , vol.80 , pp. 342-352
    • Yueh, A.1    Leung, J.2    Bhattacharyya, S.3    Perrone, L.A.4    De Los Santos, K.5    Pu, S.Y.6    Goff, S.P.7
  • 61
    • 56149118852 scopus 로고    scopus 로고
    • Memo-RhoA-mDia1 signaling controls microtubules, the actin network, and adhesion site formation in migrating cells
    • Zaoui K, Honore S, Isnardon D, Braguer D, Badache A (2008). Memo-RhoA-mDia1 signaling controls microtubules, the actin network, and adhesion site formation in migrating cells. J Cell Biol 183, 401-408.
    • (2008) J Cell Biol , vol.183 , pp. 401-408
    • Zaoui, K.1    Honore, S.2    Isnardon, D.3    Braguer, D.4    Badache, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.