Interaction of POB1, a Downstream Molecule of Small G Protein Ral, with PAG2, a Paxillin-binding Protein, Is Involved in Cell Migration*
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Akira Kikuchi | Shinya Koyama | Hisataka Sabe | Y. Onodera | T. Asahara | H. Sabe | A. Kikuchi | Toshimasa Asahara | Takafumi Oshiro | Shinichiro Sugiyama | Akiko Kondo | Yasuhito Onodera | S. Koyama | S. Sugiyama | T. Oshiro | A. Kondo | Yasuhito Onodera | Akiko Kondo
[1] M. A. Downs,et al. Epsin Binds to Clathrin by Associating Directly with the Clathrin-terminal Domain , 2000, The Journal of Biological Chemistry.
[2] S. Demo,et al. ralGDS family members interact with the effector loop of ras p21 , 1994, Molecular and cellular biology.
[3] H. Radhakrishna,et al. Localization of endogenous ARF6 to sites of cortical actin rearrangement and involvement of ARF6 in cell spreading. , 1998, Journal of cell science.
[4] P. Pelicci,et al. eps15 and eps15R are essential components of the endocytic pathway. , 1997, Cancer research.
[5] T. Kigawa,et al. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. , 2001, Science.
[6] A. Iwamatsu,et al. The exocyst complex binds the small GTPase RalA to mediate filopodia formation , 2002, Nature Cell Biology.
[7] M. Bretscher,et al. EGF induces recycling membrane to form ruffles , 1998, Current Biology.
[8] D. Görlich,et al. Nuclear import of RPA in Xenopus egg extracts requires a novel protein XRIPα but not importin α , 1999 .
[9] R. Wolthuis,et al. Ras-dependent activation of the small GTPase Ral , 1998, Current Biology.
[10] K. Vuori,et al. CAS/Crk Coupling Serves as a “Molecular Switch” for Induction of Cell Migration , 1998, The Journal of cell biology.
[11] P. Pelicci,et al. Mapping of the molecular determinants involved in the interaction between eps15 and AP-2. , 1997, Cancer research.
[12] Pier Paolo Di Fiore,et al. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis , 1998, Nature.
[13] L. Castagnoli,et al. Intersectin, a Novel Adaptor Protein with Two Eps15 Homology and Five Src Homology 3 Domains* , 1998, The Journal of Biological Chemistry.
[14] D. Strickland,et al. In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella , 1994, The Journal of cell biology.
[15] M. Bretscher. Getting Membrane Flow and the Cytoskeleton to Cooperate in Moving Cells , 1996, Cell.
[16] S. Cantor,et al. Evidence for a Ras/Ral signaling cascade. , 1996, Trends in biochemical sciences.
[17] R. Klausner,et al. Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments , 1995, The Journal of cell biology.
[18] M. Brown,et al. Paxillin-ARF GAP signaling and the cytoskeleton. , 2001, Current opinion in cell biology.
[19] M R Holt,et al. Cell motility: proline-rich proteins promote protrusions. , 2001, Trends in cell biology.
[20] R. Schekman,et al. A Primer on Vesicle Budding , 1999, Cell.
[21] A. Munn,et al. EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae , 1997, Molecular and cellular biology.
[22] R. Kahn,et al. Two distinct members of the ADP-ribosylation factor family of GTP-binding proteins regulate cell-free intra-golgi transport , 1992, Cell.
[23] S. Schmid,et al. AP-2/Eps15 Interaction Is Required for Receptor-mediated Endocytosis , 1998, The Journal of cell biology.
[24] A. Kikuchi,et al. Ras-interacting domain of Ral GDP dissociation stimulator like (RGL) reverses v-Ras-induced transformation and Raf-1 activation in NIH3T3 cells. , 1996, Cancer research.
[25] Li Guang,et al. Involvement of Ras and Ral in Chemotactic Migration of Skeletal Myoblasts , 2000, Molecular and Cellular Biology.
[26] B. Kay,et al. The EH network. , 1999, Experimental cell research.
[27] A. Iwamatsu,et al. Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis , 1999, Oncogene.
[28] K. Nagayama,et al. A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration. , 2000, Molecular biology of the cell.
[29] R. Kahn,et al. Arf proteins: the membrane traffic police? , 1995, Trends in biochemical sciences.
[30] L. Minichiello,et al. eps15, a novel tyrosine kinase substrate, exhibits transforming activity , 1993, Molecular and cellular biology.
[31] A. Tsubouchi,et al. An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization. , 2001, Molecular biology of the cell.
[32] C. Rossé,et al. The exocyst is a Ral effector complex , 2002, Nature Cell Biology.
[33] M. Roth,et al. Snapshots of ARF1 Implications for Mechanisms of Activation and Inactivation , 1999, Cell.
[34] S. Barry,et al. ARF1 Mediates Paxillin Recruitment to Focal Adhesions and Potentiates Rho-stimulated Stress Fiber Formation in Intact and Permeabilized Swiss 3T3 Fibroblasts , 1998, The Journal of cell biology.
[35] T. Urano,et al. An Eps Homology (EH) Domain Protein That Binds to the Ral-GTPase Target, RalBP1* , 1997, The Journal of Biological Chemistry.
[36] C. Turner. Paxillin and focal adhesion signalling , 2000, Nature Cell Biology.
[37] A. Kikuchi,et al. The post‐translational modifications of Ral and Rac1 are important for the action of Ral‐binding protein 1, a putative effector protein of Ral , 1997, FEBS letters.
[38] T. Hinoi,et al. Identification and Characterization of a Novel Protein Interacting with Ral-binding Protein 1, a Putative Effector Protein of Ral* , 1998, The Journal of Biological Chemistry.
[39] Jonathan A. Cooper,et al. ASAP1, a Phospholipid-Dependent Arf GTPase-Activating Protein That Associates with and Is Phosphorylated by Src , 1998, Molecular and Cellular Biology.
[40] S. Egan,et al. The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15 , 1999, The EMBO journal.
[41] H. Riezman,et al. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast , 1994, Molecular biology of the cell.
[42] K. Morinaka,et al. Regulation of Complex Formation of POB1/Epsin/Adaptor Protein Complex 2 by Mitotic Phosphorylation* , 2000, The Journal of Biological Chemistry.
[43] P. Pelicci,et al. Eps15R Is a Tyrosine Kinase Substrate with Characteristics of a Docking Protein Possibly Involved in Coated Pits-mediated Internalization* , 1998, The Journal of Biological Chemistry.
[44] E. V. van Donselaar,et al. EFA6, a sec7 domain‐containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization , 1999, The EMBO journal.
[45] T. Kataoka,et al. Synergistic activation of c-fos promoter activity by Raf and Ral GDP dissociation stimulator , 1997, Oncogene.
[46] P. Pelicci,et al. A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[47] H. Radhakrishna,et al. ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. , 1999, Journal of cell science.
[48] Y. Matsuura,et al. Colocalization of Ras and Ral on the membrane is required for Ras-dependent Ral activation through Ral GDP dissociation stimulator , 1997, Oncogene.
[49] C. D’Souza-Schorey,et al. A regulatory role for ARF6 in receptor-mediated endocytosis , 1995, Science.
[50] A. Iwamatsu,et al. Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors , 1999, The EMBO journal.
[51] J. Schlessinger,et al. Identification of a New Pyk2 Target Protein with Arf-GAP Activity , 1999, Molecular and Cellular Biology.
[52] J. Moss,et al. Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. , 1991, The Journal of biological chemistry.