斑马鱼Striatin基因的分子克隆及发育表达分析
摘要
在许多种不同的细胞进程中,如细胞分裂分化、生长繁殖、信号转导、DNA复制、基因调控和细胞衰老凋亡等生命进程中蛋白质Ser/Thr磷酸酶2A(PP2A)起着重要的调节作用。结构亚基A,调节亚基B和催化亚基C组装构成一个PP2A的异源三聚体。其中各有两种异构体存在在结构亚基A和催化亚基C中,而调节亚基B则有十多种异构体按其特异性分为至少四个不同的家族,分别为B,B′,B″和B′″。多种不同的基因分别编码这些不同的调节亚基,而调节亚基B的功能除了能介导催化特异性的底物外还能介导PP2A全酶的在细胞内的亚定位。
调节亚基B中的striatin的在低等脊椎动物中的功能和作用及其独特的表达定位引起了我们的研究兴趣,为此在本实验中我们采用RACE克隆方法克隆了斑马鱼PP2A调节亚基B'''-striatin基因的全长序列。所得序列结果为斑马鱼striatin基因包含2349bp的CDS其编码的氨基酸序列长782个aa。较高的同源性存在于斑马鱼striatin氨基酸序列与其他物种的striatin氨基酸序列之间。关于斑马鱼striatin基因的表达模式分析,RT-PCR分析显示在9个组织中striatin mRNA有不同程度的表达,而在斑马鱼胚胎发育各时期中在两细胞期、多细胞期、囊胚期和原肠期中表达量很高,而在其他发育时期表达量较低。
Western Blot结果分析,在脑组织中检测到striatin有最高的表达。然而在心脏、鳃和鳍中striatin蛋白没有被检测到。在发育过程中,striatin蛋白在原肠、神经胚和视原基期有非常强烈的表达,随后表达量在多细胞和心跳期下调。这些结果揭示出striatin在成体组织中和斑马鱼发育过程中有很重要的作用。
It is well established that the protein serine/threonine phosphatase 2A (PP2A) plays very important roles in many different cellular processes, including cell proliferation and differentiation, gene expression, neurotransmission, apoptosis, aging, and so on. PP2A consists of three heterogenic subunits:the scaffold subunit A, the catalytic subunit C, and the regulatory subunit B. While both the scaffold and the catalytic subunits contain only two isoforms, at least four subfamilies of the regulatory subunits, B, B', B'', and B''' have been identified. These regulatory subunits from different families are encoded by different genes and bear other functions besides directing the specificity of PP2A.
To explore the possible functions of the regulatory subunits of PP2A in lower vertebrates, we have cloned the full-length cDNA sequence of the gene encoding the regulatory subunit striatin of PP2A from zebrafish, Danio rerio using RACE cloning method. The result of sequence showed that the stiatin cDNA of zebrafish contains an ORF of 2349 bp encoding a protein of 782 amino acids. The striatin protein displays a very high level of sequence identity with the striatin regulatory subunit from other species of vertebrates. Regarding its expression pattern, RT-PCR analysis reveals that the striatin gene is differentially expressed in 9 tissues examined. During twelve different developmental stages of the zebrafish, the highest level of mRNA expression was detected at the stages of two-cell, multiple-cell, blastula and gastrula, and a decreased level of the striatin mRNA was detected in other developmental stages.
At the protein level, the highest expression level of the striatin protein was found in brain. In contrast, the striatin protein was hardly detectable in kidney, heart, gill and fin. Developmentally, the striatin protein was initially expressed at low level in two-cell, multiple-cell and blastula stage, then significantly upregulated at the stages of gastrula, neurula, and optic vesicle, and then decreased at heart beating and later stages. These results suggest that striatin appears to play a very important role during zebrafish development and also in adult tissue homeostasis.
调节亚基B中的striatin的在低等脊椎动物中的功能和作用及其独特的表达定位引起了我们的研究兴趣,为此在本实验中我们采用RACE克隆方法克隆了斑马鱼PP2A调节亚基B'''-striatin基因的全长序列。所得序列结果为斑马鱼striatin基因包含2349bp的CDS其编码的氨基酸序列长782个aa。较高的同源性存在于斑马鱼striatin氨基酸序列与其他物种的striatin氨基酸序列之间。关于斑马鱼striatin基因的表达模式分析,RT-PCR分析显示在9个组织中striatin mRNA有不同程度的表达,而在斑马鱼胚胎发育各时期中在两细胞期、多细胞期、囊胚期和原肠期中表达量很高,而在其他发育时期表达量较低。
Western Blot结果分析,在脑组织中检测到striatin有最高的表达。然而在心脏、鳃和鳍中striatin蛋白没有被检测到。在发育过程中,striatin蛋白在原肠、神经胚和视原基期有非常强烈的表达,随后表达量在多细胞和心跳期下调。这些结果揭示出striatin在成体组织中和斑马鱼发育过程中有很重要的作用。
It is well established that the protein serine/threonine phosphatase 2A (PP2A) plays very important roles in many different cellular processes, including cell proliferation and differentiation, gene expression, neurotransmission, apoptosis, aging, and so on. PP2A consists of three heterogenic subunits:the scaffold subunit A, the catalytic subunit C, and the regulatory subunit B. While both the scaffold and the catalytic subunits contain only two isoforms, at least four subfamilies of the regulatory subunits, B, B', B'', and B''' have been identified. These regulatory subunits from different families are encoded by different genes and bear other functions besides directing the specificity of PP2A.
To explore the possible functions of the regulatory subunits of PP2A in lower vertebrates, we have cloned the full-length cDNA sequence of the gene encoding the regulatory subunit striatin of PP2A from zebrafish, Danio rerio using RACE cloning method. The result of sequence showed that the stiatin cDNA of zebrafish contains an ORF of 2349 bp encoding a protein of 782 amino acids. The striatin protein displays a very high level of sequence identity with the striatin regulatory subunit from other species of vertebrates. Regarding its expression pattern, RT-PCR analysis reveals that the striatin gene is differentially expressed in 9 tissues examined. During twelve different developmental stages of the zebrafish, the highest level of mRNA expression was detected at the stages of two-cell, multiple-cell, blastula and gastrula, and a decreased level of the striatin mRNA was detected in other developmental stages.
At the protein level, the highest expression level of the striatin protein was found in brain. In contrast, the striatin protein was hardly detectable in kidney, heart, gill and fin. Developmentally, the striatin protein was initially expressed at low level in two-cell, multiple-cell and blastula stage, then significantly upregulated at the stages of gastrula, neurula, and optic vesicle, and then decreased at heart beating and later stages. These results suggest that striatin appears to play a very important role during zebrafish development and also in adult tissue homeostasis.
引文
[1]Makio Takahashi, Hirotaka Kanuka, et al. Phosphorylation of a-synuclein characteristic of synucleinopathy lesions is recapitulated in a-synuclein transgenic Drosophila[J]. Neuroscience Letters., 2003(336):155-158.
[2]Zha J, Harada H, et al. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)[J]. Cell.,1996(87):619-628.
[3]Michael H. Cardone, Natalie Roy, et al. Regulation of Cell Death Protease Caspase-9 by Phosphorylation[J]. Science.,1998(282): 1318-1321.
[4]Christine E. Canman, Dae-Sik Lim, et al.Activation of the ATM Kinase by Ionizing Radiation and Phosphorylation of p53[J]. Science.,1998(281):1677-1679.
[5]Sandeep Robert Datta, Henryk Dudek, et al. Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery[J]. Cell.,1997(91):231-241.
[6]Brent McCright, Ann M. Rivers, et al. The B56 Family of Protein Phosphatase 2A (PP2A) Regulatory Subunits Encodes Differentiation-induced Phosphoproteins That Target PP2A to Both Nucleus and Cytoplasm[J]. The Journal of Biological Chemistry., 1996(271):22081-22089.
[7]Joel Raingeaud, Shashi Gupta, et al. Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine[J]. The Journal of Biological Chemistry.,1995(270):7420-7426.
[8]Karl Deisseroth, Haruhiko Bito, et al. Signaling from Synapse to Nucleus:Postsynaptic CREB Phosphorylation during Multiple Forms of Hippocampal Synaptic Plasticity[J]. Neuron.,1996(16): 89-101.
[9]Mutsuki Amano, Masaaki Ito, Kazushi Kimura, et al. Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)[J]. The Journal of Biological Chemistry., 1996(271):20246-20249.
[10]Grundke-Iqbal, K Iqbal, et al. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology [J]. PNAS.,1986(83):4913-4917.
[11]Stefanie Dimmeler, Ingrid Fleming, et al. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation [J]. Nature.,1999(399):601-605.
[12]Michael Karin and Yinon Ben-Neriah. Phosphorylation Meets Ubiquitination:The Control of NF-κB Activity[J]. Annual Review of Immunology.,2000(18):621-663.
[13]Shigeaki Kato, Hideki Endoh, et al. Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein Kinase [J]. Science.,1995(270):1491-1494.
[14]JOHN C. CHRIVIA, ROLAND P. S. KWOK, et al. Phosphorylated CREB binds specifically to the nuclear protein CBP[J]. Nature., 1993 (365):855-859.
[15]BERND J.PULVERER, JOHN M. KYRIAKIS, et al. Phosphorylation of c-jun mediated by MAP kinases[J]. Nature., 1991(353):670-674.
[16]WALTER KOLCH, GISELAHEIDECKER, et al. Protein kinase Cα activates RAF-1 by direct phosphorylation[J]. Nature.,1993(364): 249-252.
[17]Joni M. Seeling, Jeffrey R. Miller, et al. Regulation of P-Catenin Signaling by the B56 Subunit of Protein Phosphatase 2A[J]. Science., 1999(283):2089-2091.
[18]M P Egloff, D F Johnson, et al. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1[J]. The EMBO Journal.,1997,16(8):1876-1887.
[19]Andreas Wissmann, Julia Ingles and Paul E. Mains. TheCaenorhabditis elegans mel-11Myosin Phosphatase Regulatory Subunit Affects Tissue Contraction in the Somatic Gonad and the Embryonic Epidermis and Genetically Interacts with the Rac Signaling Pathway[J]. Developmental Biology.,1999(209):111-127.
[20]Brent McCright and David M. Virshup. Identification of a New Family of Protein Phosphatase 2A Regulatory Subunits[J]. The Journal of Biological Chemistry.,1995(271):26123-26128.
[21]Kazue Ueki, Taro Muramatsu and Randall L. Kincaid. Structure and expression of two isoforms of the murine calmodulin-dependent protein phosphatase regulatory subunit (calcineurin B) [J]. Biochemical and Biophysical Research Communications.,1992(187): 537-543.
[22]J B Stock, A J Ninfa and A M Stock. Protein phosphorylation and regulation of adaptive responses in bacteria[J]. Microbiol Mol Biol Rev.,1989,53(4):450-490.
[23]Moreno CS& Park S., Nelson K, et al. WD40 repeat proteins striatin and S/G2 nuclear autoan tigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A[J].JBiofChem.,2000,275(8):5257-5263.
[24]Florence Margottin, Stephan P Bour, et al. A Novel Human WD Protein, h-βTrCP, that Interacts with HIV-1 Vpu Connects CD4 to the ER Degradation Pathway through an F-Box Motif[J]. Molecular Cell.,1998(1):565-574.
[25]Bernd Hoffmann, Hans-Ulrich Mosch, et al. The WD protein Cpc2p is required for repression of Gcn4 protein activity in yeast in the absence of amino-acid starvation[J]. Molecular Microbiology., 2002(37):807-822.
[26]A. Yarrow Madrona and David K. Wilson. The structure of Ski8p, a protein regulating mRNA degradation:Implications for WD protein structure[J]. Protein Sci.,2004,13(6):1557-1565.
[27]CS Buensuceso, D Woodside, et al. The WD protein Rackl mediates protein kinase C and integrin-dependent cell migration[J]. The Journal of Cell Science.,2001(114):1691-1698.
[28]Kinga Nemeth, Klaus Salchert, et al. Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD protein, in Arabidopsis[J]. Genes&Dev.,1998(12):3059-3073.
[29]Carlos S. Moreno, Susan Park, et al. WD40 Repeat Proteins Striatin and S/G2 Nuclear Autoantigen Are Members of a Novel Family of Calmodulin-binding Proteins That Associate with Protein Phosphatase 2A[J]. The Journal of Biological Chemistry.,2000(275): 5257-5263.
[30]Sabine Adam-Klages, Dieter Adam, Katja Wiegmann, et al. FAN, a Novel WD-Repeat Protein, Couples the p55 TNF-Receptor to Neutral Sphingomyelinase[J]. Cell.,1996(86):937-947.
[31]Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. The ancient regulatory-protein family of WD-repeat proteins[J]. Nature.,1997, 371(6495):297-300.
[32]Xing Xian Yu, Xianxing Du, et al. Methylation of the Protein Phosphatase 2A Catalytic Subunit Is Essential for Association of Ba Regulatory Subunit But Not SG2NA, Striatin, or Polyomavirus Middle Tumor Antigen [J]. Mol. Biol. Cell.,2001(12):19970-19977.
[33]Carlos S. Moreno, William S. Lane, et al. A Mammalian Homolog of Yeast MOB1 Is Both a Member and a Putative Substrate of Striatin Family-Protein Phosphatase 2A Complexes[J]. The Journal of Biological Chemistry.,2001(276):24253-24260.
[34]Dos D. Sarbassov, David A. Guertin, et al. Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex [J]. Science., 2005(307):1098-1101.
[35]Marc Bartoli, Jean-Pierre Ternaux, et al. Down-regulation of striatin, a neuronal calmodulin-binding protein, impairs rat locomotor activity[J]. The Journal of Neurobiology.,1999(40):234-243.
[36]F Castets, M Bartoli, J V Barnier, et al. A novel calmodulin-binding protein, belonging to the WD-repeat family, is localized in dendrites of a subset of CNS neurons[J]. The Journal of Cell Biology., 1996(134):1051-1062.
[37]Marc Bartoli, Ariane Monneron and Daniel Ladant. Interaction of Calmodulin with Striatin, a WD-repeat Protein Present in Neuronal Dendritic Spines[J]. The Journal of Biological Chemistry., 1998(273):22248-22253.
[38]Stefanie Poggeler and Ulrich Kuck. A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin[J]. Eukaryotic Cell.,2004(3):232-240.
[39]Pascal Salin, Philippe Kachidian, et al. Distribution of Striatin, a newly identified calmodulin-binding protein in the rat brain:An in situ hybridization and immunocytochemical study[J]. The Journal of Comparative Neurology.,1998(397):41-59.
[40]Stephane Gaillard, Marc Bartoli, et al. Striatin, a calmodulin-dependent scaffolding protein, directly binds caveolin-1[J]. FEBS Letters.,2002(508):49.
[41]Qing Lu, David C. Pallas, et al. Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor a[J]. PNAS., 2004(101):17126-17131.
[42]Stefan Strack, J. Thomas Cribbs and Lisa Gomez. Critical Role for Protein Phosphatase 2A Heterotrimers in Mammalian Cell Survival [J]. The Journal of Biological Chemistry.,2004(279): 47732-47739.
[43]Francis Castets, Tatiana Rakitina, et al. Zinedin, SG2NA, and Striatin Are Calmodulin-binding, WD Repeat Proteins Principally Expressed in the Brain[J]. The Journal of Biological Chemistry., 2000(275):19970-19977.
[44]Peter Mundel, Hans W. Heid, et al. Synaptopodin:An Actin-associated Protein in Telencephalic Dendrites and Renal Podocytes[J]. The Journal of Cell Biology.,1997(139):193-204.
[45]Gilbert Baillat, Abdelaziz Moqrich, et al. Molecular Cloning and Characterization of Phocein, a Protein Found from the Golgi Complex to Dendritic Spines[J]. Molecular Biology of the Cell., 2001(12):663-673.
[46]Marilyn Goudreault, Lisa M. D'Ambrosio, et al. A PP2A Phosphatase High Density Interaction Network Identifies a Novel Striatin-interacting Phosphatase and Kinase Complex Linked to the Cerebral Cavernous Malformation 3 (CCM3) Protein[J]. Molecular & Cellular Proteomics.,2009(8):157-171.
[47]Marion Benoist, Stephane Gaillard and Francis Castets. The striatin family:Anew signaling platform in dendritic spines[J]. The Journal of Physiology-Paris.,2006(99):146-153.
[48]Maya Breitman, Alona Zilberberg, et al. The armadillo repeat domain of the APC tumor suppressor protein interacts with Striatin family members[J]. Biochimica et Biophysica Acta (BBA) Molecular Cell Research.,2008 (1783):1792-1802.
[49]C Blondeau, S Gaillard, et al. Expression and distribution of phocein and members of the striatin family in neurones of rat peripheral ganglia[J]. Histochemistry and Cell Biology.,2004(119):131-138.
[50]Moqrich A, Mattei M.G., et al. Cloning of Human Striatin cDNA (STRN), Gene Mapping to 2p22-p21, and Preferential Expression in Brain[J]. Genomics.,1998(51):136-139.
[51]Katrina Sleeman and Michael D. Baron. The polymerase (L) protein of rinderpest virus interacts with the host cell protein striatin[J]. Virology.,2004(332):225-234.
[52]P. Kachidian, J. Vuillet, et al. Relationships between striatin-containing neurons and cortical or thalamic afferent fibres in the rat striatum. An ultrastructural study by dual labelling[J]. Neuroscience.,1998 (85):111-122.
[53]Yannick J. R. Bailly and Francis Castets. Phocein:A potential actor in vesicular trafficking at Purkinje cell dendritic spines [J]. The Cerebellum.,2007(6):344-352.
[54]P. Kremarik, M. J. Freund-Mercier and Q. J. Pittman. Fundus striati vasopressin receptors in blood pressure control[J]. Am J Physiol RegulIntegr Comp Physiol.,1995(269):497-503.
[2]Zha J, Harada H, et al. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)[J]. Cell.,1996(87):619-628.
[3]Michael H. Cardone, Natalie Roy, et al. Regulation of Cell Death Protease Caspase-9 by Phosphorylation[J]. Science.,1998(282): 1318-1321.
[4]Christine E. Canman, Dae-Sik Lim, et al.Activation of the ATM Kinase by Ionizing Radiation and Phosphorylation of p53[J]. Science.,1998(281):1677-1679.
[5]Sandeep Robert Datta, Henryk Dudek, et al. Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery[J]. Cell.,1997(91):231-241.
[6]Brent McCright, Ann M. Rivers, et al. The B56 Family of Protein Phosphatase 2A (PP2A) Regulatory Subunits Encodes Differentiation-induced Phosphoproteins That Target PP2A to Both Nucleus and Cytoplasm[J]. The Journal of Biological Chemistry., 1996(271):22081-22089.
[7]Joel Raingeaud, Shashi Gupta, et al. Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine[J]. The Journal of Biological Chemistry.,1995(270):7420-7426.
[8]Karl Deisseroth, Haruhiko Bito, et al. Signaling from Synapse to Nucleus:Postsynaptic CREB Phosphorylation during Multiple Forms of Hippocampal Synaptic Plasticity[J]. Neuron.,1996(16): 89-101.
[9]Mutsuki Amano, Masaaki Ito, Kazushi Kimura, et al. Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)[J]. The Journal of Biological Chemistry., 1996(271):20246-20249.
[10]Grundke-Iqbal, K Iqbal, et al. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology [J]. PNAS.,1986(83):4913-4917.
[11]Stefanie Dimmeler, Ingrid Fleming, et al. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation [J]. Nature.,1999(399):601-605.
[12]Michael Karin and Yinon Ben-Neriah. Phosphorylation Meets Ubiquitination:The Control of NF-κB Activity[J]. Annual Review of Immunology.,2000(18):621-663.
[13]Shigeaki Kato, Hideki Endoh, et al. Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein Kinase [J]. Science.,1995(270):1491-1494.
[14]JOHN C. CHRIVIA, ROLAND P. S. KWOK, et al. Phosphorylated CREB binds specifically to the nuclear protein CBP[J]. Nature., 1993 (365):855-859.
[15]BERND J.PULVERER, JOHN M. KYRIAKIS, et al. Phosphorylation of c-jun mediated by MAP kinases[J]. Nature., 1991(353):670-674.
[16]WALTER KOLCH, GISELAHEIDECKER, et al. Protein kinase Cα activates RAF-1 by direct phosphorylation[J]. Nature.,1993(364): 249-252.
[17]Joni M. Seeling, Jeffrey R. Miller, et al. Regulation of P-Catenin Signaling by the B56 Subunit of Protein Phosphatase 2A[J]. Science., 1999(283):2089-2091.
[18]M P Egloff, D F Johnson, et al. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1[J]. The EMBO Journal.,1997,16(8):1876-1887.
[19]Andreas Wissmann, Julia Ingles and Paul E. Mains. TheCaenorhabditis elegans mel-11Myosin Phosphatase Regulatory Subunit Affects Tissue Contraction in the Somatic Gonad and the Embryonic Epidermis and Genetically Interacts with the Rac Signaling Pathway[J]. Developmental Biology.,1999(209):111-127.
[20]Brent McCright and David M. Virshup. Identification of a New Family of Protein Phosphatase 2A Regulatory Subunits[J]. The Journal of Biological Chemistry.,1995(271):26123-26128.
[21]Kazue Ueki, Taro Muramatsu and Randall L. Kincaid. Structure and expression of two isoforms of the murine calmodulin-dependent protein phosphatase regulatory subunit (calcineurin B) [J]. Biochemical and Biophysical Research Communications.,1992(187): 537-543.
[22]J B Stock, A J Ninfa and A M Stock. Protein phosphorylation and regulation of adaptive responses in bacteria[J]. Microbiol Mol Biol Rev.,1989,53(4):450-490.
[23]Moreno CS& Park S., Nelson K, et al. WD40 repeat proteins striatin and S/G2 nuclear autoan tigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A[J].JBiofChem.,2000,275(8):5257-5263.
[24]Florence Margottin, Stephan P Bour, et al. A Novel Human WD Protein, h-βTrCP, that Interacts with HIV-1 Vpu Connects CD4 to the ER Degradation Pathway through an F-Box Motif[J]. Molecular Cell.,1998(1):565-574.
[25]Bernd Hoffmann, Hans-Ulrich Mosch, et al. The WD protein Cpc2p is required for repression of Gcn4 protein activity in yeast in the absence of amino-acid starvation[J]. Molecular Microbiology., 2002(37):807-822.
[26]A. Yarrow Madrona and David K. Wilson. The structure of Ski8p, a protein regulating mRNA degradation:Implications for WD protein structure[J]. Protein Sci.,2004,13(6):1557-1565.
[27]CS Buensuceso, D Woodside, et al. The WD protein Rackl mediates protein kinase C and integrin-dependent cell migration[J]. The Journal of Cell Science.,2001(114):1691-1698.
[28]Kinga Nemeth, Klaus Salchert, et al. Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD protein, in Arabidopsis[J]. Genes&Dev.,1998(12):3059-3073.
[29]Carlos S. Moreno, Susan Park, et al. WD40 Repeat Proteins Striatin and S/G2 Nuclear Autoantigen Are Members of a Novel Family of Calmodulin-binding Proteins That Associate with Protein Phosphatase 2A[J]. The Journal of Biological Chemistry.,2000(275): 5257-5263.
[30]Sabine Adam-Klages, Dieter Adam, Katja Wiegmann, et al. FAN, a Novel WD-Repeat Protein, Couples the p55 TNF-Receptor to Neutral Sphingomyelinase[J]. Cell.,1996(86):937-947.
[31]Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. The ancient regulatory-protein family of WD-repeat proteins[J]. Nature.,1997, 371(6495):297-300.
[32]Xing Xian Yu, Xianxing Du, et al. Methylation of the Protein Phosphatase 2A Catalytic Subunit Is Essential for Association of Ba Regulatory Subunit But Not SG2NA, Striatin, or Polyomavirus Middle Tumor Antigen [J]. Mol. Biol. Cell.,2001(12):19970-19977.
[33]Carlos S. Moreno, William S. Lane, et al. A Mammalian Homolog of Yeast MOB1 Is Both a Member and a Putative Substrate of Striatin Family-Protein Phosphatase 2A Complexes[J]. The Journal of Biological Chemistry.,2001(276):24253-24260.
[34]Dos D. Sarbassov, David A. Guertin, et al. Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex [J]. Science., 2005(307):1098-1101.
[35]Marc Bartoli, Jean-Pierre Ternaux, et al. Down-regulation of striatin, a neuronal calmodulin-binding protein, impairs rat locomotor activity[J]. The Journal of Neurobiology.,1999(40):234-243.
[36]F Castets, M Bartoli, J V Barnier, et al. A novel calmodulin-binding protein, belonging to the WD-repeat family, is localized in dendrites of a subset of CNS neurons[J]. The Journal of Cell Biology., 1996(134):1051-1062.
[37]Marc Bartoli, Ariane Monneron and Daniel Ladant. Interaction of Calmodulin with Striatin, a WD-repeat Protein Present in Neuronal Dendritic Spines[J]. The Journal of Biological Chemistry., 1998(273):22248-22253.
[38]Stefanie Poggeler and Ulrich Kuck. A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin[J]. Eukaryotic Cell.,2004(3):232-240.
[39]Pascal Salin, Philippe Kachidian, et al. Distribution of Striatin, a newly identified calmodulin-binding protein in the rat brain:An in situ hybridization and immunocytochemical study[J]. The Journal of Comparative Neurology.,1998(397):41-59.
[40]Stephane Gaillard, Marc Bartoli, et al. Striatin, a calmodulin-dependent scaffolding protein, directly binds caveolin-1[J]. FEBS Letters.,2002(508):49.
[41]Qing Lu, David C. Pallas, et al. Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor a[J]. PNAS., 2004(101):17126-17131.
[42]Stefan Strack, J. Thomas Cribbs and Lisa Gomez. Critical Role for Protein Phosphatase 2A Heterotrimers in Mammalian Cell Survival [J]. The Journal of Biological Chemistry.,2004(279): 47732-47739.
[43]Francis Castets, Tatiana Rakitina, et al. Zinedin, SG2NA, and Striatin Are Calmodulin-binding, WD Repeat Proteins Principally Expressed in the Brain[J]. The Journal of Biological Chemistry., 2000(275):19970-19977.
[44]Peter Mundel, Hans W. Heid, et al. Synaptopodin:An Actin-associated Protein in Telencephalic Dendrites and Renal Podocytes[J]. The Journal of Cell Biology.,1997(139):193-204.
[45]Gilbert Baillat, Abdelaziz Moqrich, et al. Molecular Cloning and Characterization of Phocein, a Protein Found from the Golgi Complex to Dendritic Spines[J]. Molecular Biology of the Cell., 2001(12):663-673.
[46]Marilyn Goudreault, Lisa M. D'Ambrosio, et al. A PP2A Phosphatase High Density Interaction Network Identifies a Novel Striatin-interacting Phosphatase and Kinase Complex Linked to the Cerebral Cavernous Malformation 3 (CCM3) Protein[J]. Molecular & Cellular Proteomics.,2009(8):157-171.
[47]Marion Benoist, Stephane Gaillard and Francis Castets. The striatin family:Anew signaling platform in dendritic spines[J]. The Journal of Physiology-Paris.,2006(99):146-153.
[48]Maya Breitman, Alona Zilberberg, et al. The armadillo repeat domain of the APC tumor suppressor protein interacts with Striatin family members[J]. Biochimica et Biophysica Acta (BBA) Molecular Cell Research.,2008 (1783):1792-1802.
[49]C Blondeau, S Gaillard, et al. Expression and distribution of phocein and members of the striatin family in neurones of rat peripheral ganglia[J]. Histochemistry and Cell Biology.,2004(119):131-138.
[50]Moqrich A, Mattei M.G., et al. Cloning of Human Striatin cDNA (STRN), Gene Mapping to 2p22-p21, and Preferential Expression in Brain[J]. Genomics.,1998(51):136-139.
[51]Katrina Sleeman and Michael D. Baron. The polymerase (L) protein of rinderpest virus interacts with the host cell protein striatin[J]. Virology.,2004(332):225-234.
[52]P. Kachidian, J. Vuillet, et al. Relationships between striatin-containing neurons and cortical or thalamic afferent fibres in the rat striatum. An ultrastructural study by dual labelling[J]. Neuroscience.,1998 (85):111-122.
[53]Yannick J. R. Bailly and Francis Castets. Phocein:A potential actor in vesicular trafficking at Purkinje cell dendritic spines [J]. The Cerebellum.,2007(6):344-352.
[54]P. Kremarik, M. J. Freund-Mercier and Q. J. Pittman. Fundus striati vasopressin receptors in blood pressure control[J]. Am J Physiol RegulIntegr Comp Physiol.,1995(269):497-503.