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This paper shows that elevated levels of FRNK, the autonomously expressed carboxy-terminal domain of focal adhesion kinase (FAK), prevent the activation of FAK by a dominant-negative mechanism, thereby inhibiting tyrosine phosphorylation of paxillin and tensin as well as formation of focal adhesions and spreading on fibronectin
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This paper shows that a β1 integrin subunit deletion mutant unable to activate focal adhesion kinase (FAK) can promote ERK activation, while FRNK can inhibit FAK without affecting ERK activation
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Un TH, Aplin AE, Shen Y, Chen Q, Schaller M, Romer L, Aukhil I, Juliano RL: Integrin-mediated activation of MAP kinase is independent of FAK: evidence for dual integrin signaling pathways in fibroblasts. J Cell Biol 1997, 136:1385-1395. This paper shows that a β1 integrin subunit deletion mutant unable to activate focal adhesion kinase (FAK) can promote ERK activation, while FRNK can inhibit FAK without affecting ERK activation.
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Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
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Ilic D, Furuta Y, Kanazawa S, Takeda N, Sobue K, Nakatsuji N, Nomura S, Fujimoto J, Okada M, Yamamoto T, Aizawa S: Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 1995, 377:539-544.
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Control of adhesion-dependent cell survival by focal adhesion kinase
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Ovexpression of CD2-focal adhesion kinase (FAK), a membrane-anchored form of FAK which is constitutively active and associated with Src, rescues epithelial cells from suspension-induced apoptosis and induces anchorage-independent growth in MDCK cells
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Frisch SM, Vuori K, Ruoslahti E, Chan-Hui PY: Control of adhesion-dependent cell survival by focal adhesion kinase. J Cell Biol 1996, 134:793-799. Ovexpression of CD2-focal adhesion kinase (FAK), a membrane-anchored form of FAK which is constitutively active and associated with Src, rescues epithelial cells from suspension-induced apoptosis and induces anchorage-independent growth in MDCK cells.
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Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics
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This paper reports the identification of Mena and Evl, two mammalian proteins that are closely related to the Drosophila AbI substrate Enabled. The amino-terminal EVH-1 domain of Mena binds to zyxin and vinculin and is necessary for the incorporation of Mena in focal adhesions, while the central proline-rich segment interacts with profilin and regulates microfilament assembly
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Gertler FB, Niebuhr K, Reinhard M, Wehland J, Soriano P: Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 1996, 87:227-239. This paper reports the identification of Mena and Evl, two mammalian proteins that are closely related to the Drosophila AbI substrate Enabled. The amino-terminal EVH-1 domain of Mena binds to zyxin and vinculin and is necessary for the incorporation of Mena in focal adhesions, while the central proline-rich segment interacts with profilin and regulates microfilament assembly.
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This paper describes the isolation of integrin-linked kinase cDNA and the initial characterization of the encoded kinase
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Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, Coppolino MG, Radeva G, Filmus J, Bell JC, Dedhar S: Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase. Nature 1996, 379:91-96. This paper describes the isolation of integrin-linked kinase cDNA and the initial characterization of the encoded kinase.
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Radeva G, Petrocelli T, Behrend E, Leung-Hagesteijn C, Filmus J, Slingerland J, Dedhar S: Overexpression of the integrin linked kinase (ILK) promotes anchorage-independent cell cycle progression. J Biol Chem 1997, 272:13937-13944.
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Molecular cloning of integrin-associated protein: An immunoglobulin family member with multiple membrane-spanning domains implicated in αvβ3-dependent ligand binding
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Ren XD, Bokoch GM, Traynor-Kaplan A, Jenkins GH, Anderson RA, Schwartz MA: Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol Biol Cell 1996, 7:435-442.
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0030980345
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The coupling of α6β4 integrin to Ras-MAP kinase pathways mediated by Shc controls keratinocyte proliferation
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1 phase of the cell cycle in primary keratinocytes exposed to epidermal growth factor. In contrast, adhesion mediated by α2β1 integrin, which is unable to activate Shc signaling, does not induce these events
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1 phase of the cell cycle in primary keratinocytes exposed to epidermal growth factor. In contrast, adhesion mediated by α2β1 integrin, which is unable to activate Shc signaling, does not induce these events.
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Maniero, F.1
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40
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Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
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This study shows that phosphatidylinositol 4,5-bisphosphate dissociates the intramolecular interaction between the head and the tail of vinculin, thereby promoting the binding of the head and tail to talin and actin, respectively
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Gilmore AP, Burridge K: Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 1996, 381:531-535. This study shows that phosphatidylinositol 4,5-bisphosphate dissociates the intramolecular interaction between the head and the tail of vinculin, thereby promoting the binding of the head and tail to talin and actin, respectively.
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Gilmore, A.P.1
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0031048791
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Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
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This study shows that wild-type Rho kinase stimulates the assembly of focal adhesions and stress fibers, while two dominant-negative forms of the kinase suppress the process
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Amano M, Chihara K, Kimura K, Fukata Y, Nakamura N, Matsuura Y, Kaibuchi K: Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 1997, 275:1308-1311. This study shows that wild-type Rho kinase stimulates the assembly of focal adhesions and stress fibers, while two dominant-negative forms of the kinase suppress the process.
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Science
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Amano, M.1
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Kaibuchi, K.7
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43
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9444242736
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Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rhokinase)
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This paper shows that Rho kinase phosphorylates and inactivates myosin phosphatase, thereby elevating the amounts of phosphorylated myosin in cells
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Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Nakafuku M, Yamamori B, Feng J, Nakano T, Okawa K et al.: Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rhokinase). Science 1996, 273:245-248. This paper shows that Rho kinase phosphorylates and inactivates myosin phosphatase, thereby elevating the amounts of phosphorylated myosin in cells.
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Science
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Kimura, K.1
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Chrzanowska-Wodnicka M, Burridge K: Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 1996, 133:1403-1415.
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Integrin function: Molecular hierarchies of cytoskeletal and signalling molecules
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Miyamoto S, Teramoto H, Coso OA, Gutkind JS, Burbelo PD, Akiyama SK, Yamada KM: Integrin function: molecular hierarchies of cytoskeletal and signalling molecules. J Cell Biol 1995, 131:791-805.
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0030911052
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Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras
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Various effector loop mutants of Ras and dominant-negative forms of phosphoinositide 3-kinase (PI-3K) are used to demonstrate that PI-3K is the target effector of Ras that activates Rac and thereby induces reorganization of the actin cytoskeleton. Evidence is provided that oncogenic Ras needs to interact with both PI-3K and Raf to transform fibroblasts
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Rodriguez-Viciana P, Warne PH, Khwaja A, Marte BM, Pappin D, Das P, Waterfield MD, Ridley A, Downward J: Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. Cell 1997, 89:457-467. Various effector loop mutants of Ras and dominant-negative forms of phosphoinositide 3-kinase (PI-3K) are used to demonstrate that PI-3K is the target effector of Ras that activates Rac and thereby induces reorganization of the actin cytoskeleton. Evidence is provided that oncogenic Ras needs to interact with both PI-3K and Raf to transform fibroblasts.
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Cell
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Rodriguez-Viciana, P.1
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Das, P.6
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47
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0029802561
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RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
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This study shows that activated forms of Rac and Cdc42 regulate the actin cytoskeleton and promote cell cycle progression by interacting with target effector(s) distinct from p21 (Cdc42/Rac)-activated kinase, which is involved in activation of JNK
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This study shows that cell adhesion activates phosphoinositide 3-kinase (PI-3K), thereby elevating the levels of phosphatidylinositol bisphosphate at the plasma membrane and causing the recruitment and activation of Akt. Inhibition of PI-3K suppresses Raf-ERK signaling without preventing Ras activation in response to cell adhesion
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67
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