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Статті в журналах з теми "Rac1 protein"

Автор: Grafiati

Опубліковано: 11 березня 2023

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1

Dumontier, M., P. Hocht, U. Mintert, and J. Faix. "Rac1 GTPases control filopodia formation, cell motility, endocytosis, cytokinesis and development in Dictyostelium." Journal of Cell Science 113, no. 12 (2000): 2253–65. http://dx.doi.org/10.1242/jcs.113.12.2253.

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The function of the highly homologous Rac1A, Rac1B, and Rac1C GTPases of the Dictyostelium Rac1 group was investigated. All three GTPases bound with an equal capacity to the IQGAP-related protein DGAP1, with a preference for the activated GTP-bound form. Strong overexpression of wild-type Rac1 GTPases N-terminally tagged with green fluorescent protein (GFP), predominantly induced the formation of numerous long filopodia. Remarkably, expression of the constitutively-activated GTPases resulted in dominant-negative phenotypes: these Rac1-V12 mutants completely lacked filopodia but formed numerous

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2

Seiz, Julia R., Johannes Klinke, Laura Scharlibbe, et al. "Different signaling and functionality of Rac1 and Rac1b in the progression of lung adenocarcinoma." Biological Chemistry 401, no. 4 (2020): 517–31. http://dx.doi.org/10.1515/hsz-2019-0329.

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AbstractRac1 is a ubiquitously expressed Rho GTPase and an important regulator of the actin cytoskeleton. Its splice variant Rac1b exhibits a 19-amino acid (aa) in-frame insertion and is predominantly active. Both proteins were described in tumorigenesis or metastasis. We investigated the contribution of Rac1 and Rac1b to tumor progression of human non-small-cell lung adenocarcinoma (NSCLA). Rac1 protein was present in 8/8 NSCLA cell lines analyzed, whereas Rac1b was expressed in only 6/8. In wound-healing assays, enhanced green fluorescence protein (EGFP)-Rac1 slightly decreased cell migratio

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3

Nagata, Koh-ichi, Yukio Okano, and Yoshinori Nozawa. "Differential Expression of Low Mr GTP-binding Proteins in Human Megakaryoblastic Leukemia Cell Line, MEG-01, and their Possible Involvement in the Differentiation Process." Thrombosis and Haemostasis 77, no. 02 (1997): 368–75. http://dx.doi.org/10.1055/s-0038-1655970.

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SummaryThe expression of various low Mr GTP-binding proteins at various states of differentiation of a human megakaryoblastic leukemia cell line, MEG-01, was analyzed using thermocycle amplification of mRNA and immunoblotting. MEG-01 cells were found to express mRNAs of rap1A, rap1B, rap2B, ralA, rhoA, rac1, rac2, CDC42Hs, rab1, rab3B, rab6, ram and ran, but not rab4, and the proteins of Rap 1, Rap2, RhoA, Rac1, Rac2, Rab3B, Rab4, Rab6 and Rab8 were expressed. Differentiation of MEG-01 cells induced by 100 nM 12-O-tetradecanoylphorbol-13-acetate revealed the considerable increases in mRNA expr

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4

Hoppe, Adam D., and Joel A. Swanson. "Cdc42, Rac1, and Rac2 Display Distinct Patterns of Activation during Phagocytosis." Molecular Biology of the Cell 15, no. 8 (2004): 3509–19. http://dx.doi.org/10.1091/mbc.e03-11-0847.

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The small G proteins Cdc42, Rac1, and Rac2 regulate the rearrangements of actin and membrane necessary for Fcγ receptor-mediated phagocytosis by macrophages. Activated, GTP-bound Cdc42, Rac1, and Rac2 bind to the p21-binding domain (PBD) of PAK1, and this interaction provided a basis for microscopic methods to localize activation of these G proteins inside cells. Fluorescence resonance energy transfer-based stoichiometry of fluorescent chimeras of actin, PBD, Cdc42, Rac1, and Rac2 was used to quantify G protein activation relative to actin movements during phagocytosis of IgG-opsonized erythro

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5

Kalfa, Theodosia A., Suvarnamala Pushkaran, Narla Mohandas, et al. "Rac GTPases regulate the morphology and deformability of the erythrocyte cytoskeleton." Blood 108, no. 12 (2006): 3637–45. http://dx.doi.org/10.1182/blood-2006-03-005942.

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Abstract Actin oligomers are a significant structural component of the erythrocyte cytoskeleton. Rac1 and Rac2 GTPases regulate actin structures and have multiple overlapping as well as distinct roles in hematopoietic cells; therefore, we studied their role in red blood cells (RBCs). Conditional gene targeting with a loxP-flanked Rac1 gene allowed Crerecombinase–induced deletion of Rac1 on a Rac2 null genetic background. The Rac1–/–;Rac2–/– mice developed microcytic anemia with a hemoglobin drop of about 20% and significant anisocytosis and poikilocytosis. Reticulocytes increased more than 2-f

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6

Thomas, Emily K., Jose A. Cancelas, Heedon Chae, et al. "Rac GTPases Are Potential Therapeutic Targets in p210-BCR-ABL-Induced Myeloproliferative Disease (MPD)." Blood 110, no. 11 (2007): 465. http://dx.doi.org/10.1182/blood.v110.11.465.465.

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Abstract The p210-BCR-ABL fusion protein is a constitutively active tyrosine kinase that is necessary and sufficient for the development of chronic myelogenous leukemia (CML). ABL-kinase inhibitors such as imatinib mesylate (Gleevec, STI571) potently block BCR-ABL activation, but the continued presence of leukemic stem cells and the emergence of imatinib-resistant BCR-ABL mutants suggest that ABL kinase inhibitors alone cannot completely eradicate disease. Rac GTPases have been implicated in BCR-ABL-mediated proliferation in cell lines and regulate many of the same signaling pathways as BCR-AB

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7

Chuang, T. H., X. Xu, L. A. Quilliam, and G. M. Bokoch. "SmgGDS stabilizes nucleotide-bound and -free forms of the Rac1 GTP-binding protein and stimulates GTP/GDP exchange through a substituted enzyme mechanism." Biochemical Journal 303, no. 3 (1994): 761–67. http://dx.doi.org/10.1042/bj3030761.

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The Rac proteins, Rac1 and Rac2, are essential components of the NADPH oxidase system of phagocytes and regulate the actin assembly associated with membrane ruffling. These functions are controlled by the GTP-bound form of Rac. The biochemical interaction between Rac and its only known GDP-dissociation stimulator (termed smgGDS) was characterized. SmgGDS was able to stimulate the incorporation of guanosine 5′-[gamma-thio]-triphosphate GTP[gamma S] into the RhoA, Rac2, Rac1, Rap1A and CDC42Hs GTP-binding proteins, but the activity was greatest toward RhoA and Rac2. Isoprenoid modification of th

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8

Engers, R., S. Ziegler, M. Mueller, A. Walter, R. Willers, and H. E. Gabbert. "Prognostic relevance of increased Rac GTPase expression in prostate carcinomas." Endocrine-Related Cancer 14, no. 2 (2007): 245–56. http://dx.doi.org/10.1677/erc-06-0036.

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Rac proteins of the Rho-like GTPase family, including the ubiquitous Rac1, the hematopoiesis-specific Rac2, and the least-characterized Rac3 play a major role in oncogenic transformation, tumor invasion and metastasis. However, the prognostic relevance of Rac expression in human tumors has not been investigated yet. In the present study, Rac protein expression was analyzed in benign secretory epithelium, high-grade prostatic intraepithelium neoplasia (HG-PIN), and prostate carcinomas of 60 R0-resected radical prostatectomy specimens by semiquantitative immunohistochemistry. Thus, Rac proteins

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9

Kuncewicz, Teresa, Priya Balakrishnan, Mark B. Snuggs, and Bruce C. Kone. "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages." American Journal of Physiology-Renal Physiology 281, no. 2 (2001): F326—F336. http://dx.doi.org/10.1152/ajprenal.2001.281.2.f326.

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Nitric oxide synthase-2 (NOS2) is responsible for high-output nitric oxide production important in renal inflammation and injury. Using a yeast two-hybrid assay, we identified Rac2, a Rho GTPase member, as a NOS2-interacting protein. NOS2 and Rac2 proteins coimmunoprecipitated from activated RAW 264.7 macrophages. The two proteins colocalized in an intracellular compartment of these cells. Glutathione- S-transferase (GST) pull-down assays revealed that both Rac1 and Rac2 associated with GST-NOS2 and that the NOS2 oxygenase domain was necessary and sufficient for the interaction. [35S]methionin

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10

Michaelson, David, Joseph Silletti, Gretchen Murphy, Peter D'Eustachio, Mark Rush, and Mark R. Philips. "Differential Localization of Rho Gtpases in Live Cells." Journal of Cell Biology 152, no. 1 (2001): 111–26. http://dx.doi.org/10.1083/jcb.152.1.111.

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Determinants of membrane targeting of Rho proteins were investigated in live cells with green fluorescent fusion proteins expressed with or without Rho-guanine nucleotide dissociation inhibitor (GDI)α. The hypervariable region determined to which membrane compartment each protein was targeted. Targeting was regulated by binding to RhoGDIα in the case of RhoA, Rac1, Rac2, and Cdc42hs but not RhoB or TC10. Although RhoB localized to the plasma membrane (PM), Golgi, and motile peri-Golgi vesicles, TC10 localized to PMs and endosomes. Inhibition of palmitoylation mislocalized H-Ras, RhoB, and TC10

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11

RAMASWAMY, MADHU, CELINE DUMONT, JAGAN R. MUPPIDI, VICTOR L. TYBULEWICZ, and RICHARD M. SIEGEL. "Rac GTPases are required for restimulation-induced CD4+ T Cell Death (RICD) (87.20)." Journal of Immunology 178, no. 1_Supplement (2007): S131. http://dx.doi.org/10.4049/jimmunol.178.supp.87.20.

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Abstract In activated CD4 T cells, TCR restimulation or antigen leads to FasL mRNA synthesis, expression and eventually apoptosis through cis or trans FasL-Fas interactions, in the process known as restimulation-induced cell death (RICD). Apoptosis requires both FasL synthesis and secretion and a protein-synthesis independent ‘competency to die’ signal that sensitizes TCR-stimulated cells to apoptosis induced by FasL. Recent work in our lab correlated competency signals with translocation of Fas into specialized membrane micro-domains (lipid rafts) in TCR restimulated T cells. However, what si

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12

Ma, Zhong, Keena S. Thomas, Donna J. Webb, et al. "Regulation of Rac1 activation by the low density lipoprotein receptor–related protein." Journal of Cell Biology 159, no. 6 (2002): 1061–70. http://dx.doi.org/10.1083/jcb.200207070.

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The low density lipoprotein receptor–related protein (LRP-1) binds and mediates the endocytosis of multiple ligands, transports the urokinase-type plasminogen activator receptor (uPAR) and other membrane proteins into endosomes, and binds intracellular adaptor proteins involved in cell signaling. In this paper, we show that in murine embryonic fibroblasts (MEFs) and L929 cells, LRP-1 functions as a major regulator of Rac1 activation, and that this activity depends on uPAR. LRP-1–deficient MEFs demonstrated increased Rac1 activation compared with LRP-1–expressing MEFs, and this property was rev

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13

Shutes, Adam, Cercina Onesto, Virginie Picard, Bertrand Leblond, Fabien Schweighoffer, and Channing J. Der. "Specificity and Mechanism of Action of EHT 1864, a Novel Small Molecule Inhibitor of Rac Family Small GTPases." Journal of Biological Chemistry 282, no. 49 (2007): 35666–78. http://dx.doi.org/10.1074/jbc.m703571200.

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There is now considerable experimental evidence that aberrant activation of Rho family small GTPases promotes the uncontrolled proliferation, invasion, and metastatic properties of human cancer cells. Therefore, there is considerable interest in the development of small molecule inhibitors of Rho GTPase function. However, to date, most efforts have focused on inhibitors that indirectly block Rho GTPase function, by targeting either enzymes involved in post-translational processing or downstream protein kinase effectors. We recently determined that the EHT 1864 small molecule can inhibit Rac fu

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14

Zohn, Irene E., Marc Symons, Magdalena Chrzanowska-Wodnicka, John K. Westwick, and Channing J. Der. "Mas Oncogene Signaling and Transformation Require the Small GTP-Binding Protein Rac." Molecular and Cellular Biology 18, no. 3 (1998): 1225–35. http://dx.doi.org/10.1128/mcb.18.3.1225.

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ABSTRACT The Mas oncogene encodes a novel G-protein-coupled receptor that was identified originally as a transforming protein when overexpressed in NIH 3T3 cells. The mechanism and signaling pathways that mediate Mas transformation have not been determined. We observed that the foci of transformed NIH 3T3 cells caused by Mas were similar to those caused by activated Rho and Rac proteins. Therefore, we determined if Mas signaling and transformation are mediated through activation of a specific Rho family protein. First, we observed that, like activated Rac1, Mas cooperated with activated Raf an

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15

Yang, Shigao, Alfred T. Harding, Catherine Sweeney, et al. "Control of antiviral innate immune response by protein geranylgeranylation." Science Advances 5, no. 5 (2019): eaav7999. http://dx.doi.org/10.1126/sciadv.aav7999.

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The mitochondrial antiviral signaling protein (MAVS) orchestrates host antiviral innate immune response to RNA virus infection. However, how MAVS signaling is controlled to eradicate virus while preventing self-destructive inflammation remains obscure. Here, we show that protein geranylgeranylation, a posttranslational lipid modification of proteins, limits MAVS-mediated immune signaling by targeting Rho family small guanosine triphosphatase Rac1 into the mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) at the mitochondria-ER junction. Protein geranylgeranylation and subsequ

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16

KITAMURA, Yukari, Tadahiro KITAMURA, Hiroshi SAKAUE, et al. "Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac." Biochemical Journal 322, no. 3 (1997): 873–78. http://dx.doi.org/10.1042/bj3220873.

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Bacterially expressed glutathione S-transferase fusion proteins containing Rac1 were used to identify binding proteins of this Rho family GTPase present in a bovine brain extract. Five proteins of 85, 110, 125, 140 and 170 kDa were detected, all of which were associated exclusively with guanosine 5´-[γ-thio]triphosphate-bound Rac1, not with GDP-bound Rac1. The 85 and 110 kDa proteins were identified as the regulatory and catalytic subunits respectively of phosphatidylinositol 3-kinase. Several lines of evidence suggested that the 125 kDa protein is identical with Nck-associated protein 1 (Nap1

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17

Gauthier-Rouvière, Cécile, Emmanuel Vignal, Mayya Mériane, Pierre Roux, Philippe Montcourier, and Philippe Fort. "RhoG GTPase Controls a Pathway That Independently Activates Rac1 and Cdc42Hs." Molecular Biology of the Cell 9, no. 6 (1998): 1379–94. http://dx.doi.org/10.1091/mbc.9.6.1379.

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RhoG is a member of the Rho family of GTPases that shares 72% and 62% sequence identity with Rac1 and Cdc42Hs, respectively. We have expressed mutant RhoG proteins fused to the green fluorescent protein and analyzed subsequent changes in cell surface morphology and modifications of cytoskeletal structures. In rat and mouse fibroblasts, green fluorescent protein chimera and endogenous RhoG proteins colocalize according to a tubular cytoplasmic pattern, with perinuclear accumulation and local concentration at the plasma membrane. Constitutively active RhoG proteins produce morphological and cyto

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18

Choi, Ki Young, Min Sup Lee, Young Jun Cho, Myong Ho Jeong, Seung Jin Han, and Seung Hwan Hong. "p104 Binds to Rac1 and Reduces Its Activity during Myotube Differentiation of C2C12 Cell." Scientific World Journal 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/592450.

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The p104 protein inhibits cellular proliferation when overexpressed in NIH3T3 cells and has been shown to associate with p85α, Grb2, and PLCγ1. In order to isolate other proteins that interact with p104, yeast two-hybrid screening was performed. Rac1 was identified as a binding partner of p104 and the interaction between p104 and Rac1 was confirmed by immunoprecipitation. Using a glutathione S-transferase (GST) pull-down assay with various p104 fragments, the 814–848 amino acid residue at the carboxyl-terminal region of p104 was identified as the key component to interact with Rac1. The CrkII

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19

Heyworth, P. G., U. G. Knaus, J. Settleman, J. T. Curnutte, and G. M. Bokoch. "Regulation of NADPH oxidase activity by Rac GTPase activating protein(s)." Molecular Biology of the Cell 4, no. 11 (1993): 1217–23. http://dx.doi.org/10.1091/mbc.4.11.1217.

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Activation of the NADPH oxidase of phagocytic cells requires the action of Rac2 or Rac1, members of the Ras superfamily of GTP-binding proteins. Rac proteins are active when in the GTP-bound form and can be regulated by a variety of proteins that modulate the exchange of GDP for GTP and/or GTP hydrolysis. The p190 Rac GTPase Activating Protein (GAP) inhibits human neutrophil NADPH oxidase activity in a cell-free assay system with a K1 of approximately 100 nM. Inhibition by p190 was prevented by GTP gamma S, a nonhydrolyzable analogue of GTP. Similar inhibition was seen with a second protein ex

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20

Buscemi, Nina, Chris Murray, Amanda Doherty-Kirby, Gilles Lajoie, Mark A. Sussman, and Jennifer E. Van Eyk. "Myocardial subproteomic analysis of a constitutively active Rac1-expressing transgenic mouse with lethal myocardial hypertrophy." American Journal of Physiology-Heart and Circulatory Physiology 289, no. 6 (2005): H2325—H2333. http://dx.doi.org/10.1152/ajpheart.01041.2004.

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A two-dimensional gel electrophoresis (2-DE)-based proteomic approach was used to study a transgenic mouse model of acerbated dilated cardiomyopathy in which the small monomeric GTPase, Rac1, was constitutively expressed exclusively in the myocardium. A subfractionation procedure allowed for the focused analysis of both cytoplasmic and myofilament protein-enriched extracts of ventricular tissue from Rac1 transgenic and age-matched nontransgenic (NTG) mice. The majority of these mice displayed severe hypertrophy (heart-to-body weight ratios >2-fold greater in the Rac1 mice) and died from ove

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21

Hamill, Kevin J., Susan B. Hopkinson, Philip DeBiase та Jonathan C. R. Jones. "BPAG1e Maintains Keratinocyte Polarity through β4 Integrin–mediated Modulation of Rac 1 and Cofilin Activities". Molecular Biology of the Cell 20, № 12 (2009): 2954–62. http://dx.doi.org/10.1091/mbc.e09-01-0051.

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α6β4 integrin, a component of hemidesmosomes, also plays a role in keratinocyte migration via signaling through Rac1 to the actin-severing protein cofilin. Here, we tested the hypothesis that the β4 integrin-associated plakin protein, bullous pemphigoid antigen 1e (BPAG1e) functions as a scaffold for Rac1/cofilin signal transduction. We generated keratinocyte lines exhibiting a stable knockdown in BPAG1e expression. Knockdown of BPAG1e does not affect expression levels of other hemidesmosomal proteins, nor the amount of β4 integrin expressed at the cell surface. However, the amount of Rac1 ass

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22

Aranda, Juan F., Natalia Reglero-Real, Leonor Kremer, et al. "MYADM regulates Rac1 targeting to ordered membranes required for cell spreading and migration." Molecular Biology of the Cell 22, no. 8 (2011): 1252–62. http://dx.doi.org/10.1091/mbc.e10-11-0910.

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Membrane organization into condensed domains or rafts provides molecular platforms for selective recruitment of proteins. Cell migration is a general process that requires spatiotemporal targeting of Rac1 to membrane rafts. The protein machinery responsible for making rafts competent to recruit Rac1 remains elusive. Some members of the MAL family of proteins are involved in specialized processes dependent on this type of membrane. Because condensed membrane domains are a general feature of the plasma membrane of all mammalian cells, we hypothesized that MAL family members with ubiquitous expre

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23

Wang, Xiaohui, Dongbin Liu, Fangzhen Wei, et al. "Stress-Sensitive Protein Rac1 and Its Involvement in Neurodevelopmental Disorders." Neural Plasticity 2020 (November 24, 2020): 1–11. http://dx.doi.org/10.1155/2020/8894372.

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Ras-related C3 botulinum toxin substrate 1 (Rac1) is a small GTPase that is well known for its sensitivity to the environmental stress of a cell or an organism. It senses the external signals which are transmitted from membrane-bound receptors and induces downstream signaling cascades to exert its physiological functions. Rac1 is an important regulator of a variety of cellular processes, such as cytoskeletal organization, generation of oxidative products, and gene expression. In particular, Rac1 has a significant influence on certain brain functions like neuronal migration, synaptic plasticity

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24

Faix, J., C. Clougherty, A. Konzok, et al. "The IQGAP-related protein DGAP1 interacts with Rac and is involved in the modulation of the F-actin cytoskeleton and control of cell motility." Journal of Cell Science 111, no. 20 (1998): 3059–71. http://dx.doi.org/10.1242/jcs.111.20.3059.

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DGAP1 of Dictyostelium discoideum is a cell cortex associated 95 kDa protein that shows homology to both RasGTPase-activating proteins (RasGAPs) and RasGAP-related proteins. When tested for RasGAP activity, recombinant DGAP1 protein did not promote the GTPase activity of human H-Ras or of Dictyostelium RasG in vitro. Instead, DGAP1 bound to Dictyostelium Rac1A and human Rac1, but not to human Cdc42. DGAP1 preferentially interacted with the activated GTP-bound forms of Rac1 and Rac1A, but did not affect the GTPase activities. Since Rho-type GTPases are implicated in the formation of specific F-

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25

Kalfa, Theodosia A., Suvarnamala Pushkaran, James F. Johnson, Qian Wei, David A. Williams, and Yi Zheng. "Erythrocyte Cytoskeletal Defects Induced in Mice by Deletion of Rac GTPases." Blood 104, no. 11 (2004): 1573. http://dx.doi.org/10.1182/blood.v104.11.1573.1573.

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Abstract The small Rho GTPases Rac1 and Rac2 have been implicated in regulating actin structures in a variety of cells, including hematopoietic stem cells and leucocytes. Actin oligomers are a significant structural component of the erythrocyte cytoskeleton. We explored the possible role of Rac1 and Rac2 signaling molecules in the dynamic assembly of actin in the red blood cells (RBC), and thus in the regulation of morphology and function of the erythrocyte cytoskeleton. Rac1 and Rac2 GTPases have been shown to have overlapping as well as distinct roles in actin organization, cell survival, an

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26

Zang, Li, Quan Hong, Guoqing Yang, et al. "MACROD1/LRP16 Enhances LPS-Stimulated Inflammatory Responses by Up-Regulating a Rac1-Dependent Pathway in Adipocytes." Cellular Physiology and Biochemistry 51, no. 6 (2018): 2591–603. http://dx.doi.org/10.1159/000495931.

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Background/Aims: Chronic inflammation contributes to the development of type 2 diabetes mellitus by targeting the insulin receptor substrate protein-1 (IRS-1) signaling pathway. Previous studies showed that Leukemia related protein 16 (LRP16) reduced insulin stimulated glucose uptake in adipocytes by impairing the IRS-1 signaling pathway. We explored the mechanism by which LRP16 promotes the inflammatory response. Methods: We screened LRP16 induced proteins in the lipopolysaccharide (LPS)-stimulated inflammatory response using liquid chromatography-mass spectrometry (LC-MS) and analyzed the po

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27

Weiß, Lukas, Lana Gaelings, Tina Reiner, et al. "Posttranslational modification of the RHO of plants protein RACB by phosphorylation and cross-kingdom conserved ubiquitination." PLOS ONE 17, no. 3 (2022): e0258924. http://dx.doi.org/10.1371/journal.pone.0258924.

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Small RHO-type G-proteins act as signaling hubs and master regulators of polarity in eukaryotic cells. Their activity is tightly controlled, as defective RHO signaling leads to aberrant growth and developmental defects. Two major processes regulate G-protein activity: canonical shuttling between different nucleotide bound states and posttranslational modification (PTM), of which the latter can support or suppress RHO signaling, depending on the individual PTM. In plants, regulation of Rho of plants (ROPs) signaling activity has been shown to act through nucleotide exchange and GTP hydrolysis,

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28

Eiden, Caroline, and Hendrik Ungefroren. "The Ratio of RAC1B to RAC1 Expression in Breast Cancer Cell Lines as a Determinant of Epithelial/Mesenchymal Differentiation and Migratory Potential." Cells 10, no. 2 (2021): 351. http://dx.doi.org/10.3390/cells10020351.

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Breast cancer (BC) is a heterogenous disease encompassing tumors with different histomorphological phenotypes and transcriptionally defined subtypes. However, the non-mutational/epigenetic alterations that are associated with or causally involved in phenotype diversity or conversion remain to be elucidated. Data from the pancreatic cancer model have shown that the small GTPase RAC1 and its alternatively spliced isoform, RAC1B, antagonistically control epithelial–mesenchymal transition and cell motility induced by transforming growth factor β. Using a battery of established BC cell lines with e

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29

Yang, Xiaoxu, Yongjin Sun, Xu Li та Wenzhi Zhang. "Rac1 regulates nucleus pulposus cell degeneration by activating the Wnt/β-catenin signaling pathway and promotes the progression of intervertebral disc degeneration". American Journal of Physiology-Cell Physiology 322, № 3 (2022): C496—C507. http://dx.doi.org/10.1152/ajpcell.00355.2021.

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Nucleus pulposus cell (NPC) dysfunction is considered as an important event related to intervertebral disc degeneration (IVDD). In the present study, tandem mass spectrometry (TMT) was used to detect total protein expression of nucleus pulposus (NP) in patients with IVDD and healthy controls. Bioinformatic analysis was performed to identify differentially expressed proteins that may be involved in the degeneration of NP. The results show that Rac1 may be a key protein involved in the degeneration of NP via Wnt/β-catenin pathway activation. We investigated the influence of Rac1 on IVDD degenera

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Chan, Diane, Allison Citro, Joanna M. Cordy, Grace C. Shen, and Benjamin Wolozin. "Rac1 Protein Rescues Neurite Retraction Caused by G2019S Leucine-rich Repeat Kinase 2 (LRRK2)." Journal of Biological Chemistry 286, no. 18 (2011): 16140–49. http://dx.doi.org/10.1074/jbc.m111.234005.

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Mutations in leucine-rich repeat kinase 2 (LRRK2) are currently the most common genetic cause of familial late-onset Parkinson disease, which is clinically indistinguishable from idiopathic disease. The most common pathological mutation in LRRK2, G2019S LRRK2, is known to cause neurite retraction. However, molecular mechanisms underlying regulation of neurite length by LRRK2 are unknown. Here, we demonstrate a novel interaction between LRRK2 and the Rho GTPase, Rac1, which plays a critical role in actin cytoskeleton remodeling necessary for the maintenance of neurite morphology. LRRK2 binds st

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Azim, Anser C., Hongmei Cao, Xiaopei Gao, et al. "Regulation of cyclooxygenase-2 expression by small GTPase Rac2 in bone marrow macrophages." American Journal of Physiology-Lung Cellular and Molecular Physiology 293, no. 3 (2007): L668—L673. http://dx.doi.org/10.1152/ajplung.00043.2007.

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Cyclooxygenase 2 (COX-2) is induced by microbial products, proinflammatory cytokines, growth factors, and oncogenes. The Rho family includes RhoA, Rac1, Rac2, Rac3, and Cdc42 and is involved in regulation of the actin cytoskeleton organization, cell growth, vesicular cell trafficking, and transcriptional regulation. Rac2 binds to NADPH oxidase protein complex, and Rac2 null neutrophils are known to have poor phagocytic activity. We examined whether Rac2, the predominant small GTPase in hematopoietic cells, influences COX-2 expression in bone marrow-derived macrophages (BMDM). We showed that BM

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Clerk, Angela, Fong H. Pham, Stephen J. Fuller, et al. "Regulation of Mitogen-Activated Protein Kinases in Cardiac Myocytes through the Small G Protein Rac1." Molecular and Cellular Biology 21, no. 4 (2001): 1173–84. http://dx.doi.org/10.1128/mcb.21.4.1173-1184.2001.

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ABSTRACT Small guanine nucleotide-binding proteins of the Ras and Rho (Rac, Cdc42, and Rho) families have been implicated in cardiac myocyte hypertrophy, and this may involve the extracellular signal-related kinase (ERK), c-Jun N-terminal kinase (JNK), and/or p38 mitogen-activated protein kinase (MAPK) cascades. In other systems, Rac and Cdc42 have been particularly implicated in the activation of JNKs and p38-MAPKs. We examined the activation of Rho family small G proteins and the regulation of MAPKs through Rac1 in cardiac myocytes. Endothelin 1 and phenylephrine (both hypertrophic agonists)

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Brill, S., S. Li, C. W. Lyman, et al. "The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases." Molecular and Cellular Biology 16, no. 9 (1996): 4869–78. http://dx.doi.org/10.1128/mcb.16.9.4869.

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We previously described IQGAP1 as a human protein related to a putative Ras GTPase-activating protein (RasGAP) from the fission yeast Schizosaccharomyces pombe. Here we report the identification of a liver-specific human protein that is 62% identical to IQGAP1. Like IQGAP1, the novel IQGAP2 protein harbors an N-terminal calponin homology motif which functions as an F-actin binding domain in members of the spectrin, filamin, and fimbrin families. Both IQGAPs also harbor several copies of a novel 50- to 55-amino-acid repeat, a single WW domain, and four IQ motifs and have 25% sequence identity w

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Hope, Hannah, Stéphanie Bogliolo, Robert A. Arkowitz, and Martine Bassilana. "Activation of Rac1 by the Guanine Nucleotide Exchange Factor Dck1 Is Required for Invasive Filamentous Growth in the Pathogen Candida albicans." Molecular Biology of the Cell 19, no. 9 (2008): 3638–51. http://dx.doi.org/10.1091/mbc.e07-12-1272.

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Rho G proteins and their regulators are critical for cytoskeleton organization and cell morphology in all eukaryotes. In the opportunistic pathogen Candida albicans, the Rho G proteins Cdc42 and Rac1 are required for the switch from budding to filamentous growth in response to different stimuli. We show that Dck1, a protein with homology to the Ced-5, Dock180, myoblast city family of guanine nucleotide exchange factors, is necessary for filamentous growth in solid media, similar to Rac1. Our results indicate that Dck1 and Rac1 do not function in the same pathway as the transcription factor Czf

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Vartiainen, Maria, Pauli J. Ojala, Petri Auvinen, Johan Peränen, and Pekka Lappalainen. "Mouse A6/Twinfilin Is an Actin Monomer-Binding Protein That Localizes to the Regions of Rapid Actin Dynamics." Molecular and Cellular Biology 20, no. 5 (2000): 1772–83. http://dx.doi.org/10.1128/mcb.20.5.1772-1783.2000.

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ABSTRACT In our database searches, we have identified mammalian homologues of yeast actin-binding protein, twinfilin. Previous studies suggested that these mammalian proteins were tyrosine kinases, and therefore they were named A6 protein tyrosine kinase. In contrast to these earlier studies, we did not find any tyrosine kinase activity in our recombinant protein. However, biochemical analysis showed that mouse A6/twinfilin forms a complex with actin monomer and prevents actin filament assembly in vitro. A6/twinfilin mRNA is expressed in most adult tissues but not in skeletal muscle and spleen

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Khosravi-Far, R., P. A. Solski, G. J. Clark, M. S. Kinch, and C. J. Der. "Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation." Molecular and Cellular Biology 15, no. 11 (1995): 6443–53. http://dx.doi.org/10.1128/mcb.15.11.6443.

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Although substantial evidence supports a critical role for the activation of Raf-1 and mitogen-activated protein kinases (MAPKs) in oncogenic Ras-mediated transformation, recent evidence suggests that Ras may activate a second signaling pathway which involves the Ras-related proteins Rac1 and RhoA. Consequently, we used three complementary approaches to determine the contribution of Rac1 and RhoA function to oncogenic Ras-mediated transformation. First, whereas constitutively activated mutants of Rac1 and RhoA showed very weak transforming activity when transfected alone, their coexpression wi

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Liu, Kathleen D., Anirban Datta, Wei Yu, et al. "Rac1 is required for reorientation of polarity and lumen formation through a PI 3-kinase-dependent pathway." American Journal of Physiology-Renal Physiology 293, no. 5 (2007): F1633—F1640. http://dx.doi.org/10.1152/ajprenal.00053.2007.

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Epithelial cells are characterized by the ability to form sheets of cells that surround fluid-filled lumens. Cells in these sheets exhibit a characteristic subcellular polarity, with an apical pole that faces the lumen and a basolateral pole that is in contact with other cells and the extracellular matrix (ECM). To investigate the signaling events required for polarization and lumen formation, we have taken advantage of the ability of Madin-Darby canine kidney (MDCK) cells to dynamically remodel their polarity in response to changes in ECM cues. When MDCK cells are grown in suspension culture,

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Abdrabou, Abdalla, Daniel Brandwein, Changyu Liu, and Zhixiang Wang. "Rac1 S71 Mediates the Interaction between Rac1 and 14-3-3 Proteins." Cells 8, no. 9 (2019): 1006. http://dx.doi.org/10.3390/cells8091006.

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Both 14-3-3 proteins (14-3-3s) and Rho proteins regulate cytoskeleton remodeling and cell migration, which suggests a possible interaction between the signaling pathways regulated by these two groups of proteins. Indeed, more and more emerging evidence indicates the mutual regulation of these two signaling pathways. However, all of the data regarding the interaction between Rac1 signaling pathways and 14-3-3 signaling pathways are through either the upstream regulators or downstream substrates. It is not clear if Rac1 could interact with 14-3-3s directly. It is interesting to notice that the R

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Tyasi, Thobela Louis, Xue Sun, Xuesong Shan, et al. "Effects of RAC1 on Proliferation of Hen Ovarian Prehierarchical Follicle Granulosa Cells." Animals 10, no. 9 (2020): 1589. http://dx.doi.org/10.3390/ani10091589.

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RAC1 belongs to the small G protein Rho subfamily and is implicated in regulating gene expression, cell proliferation and differentiation in mammals and humans; nevertheless, the function of RAC1 in growth and development of hen ovarian follicles is still unclear. This study sought to understand the biological effects of RAC1 on granulosa cell (GC) proliferation and differentiation of hen ovarian prehierarchical follicles. Firstly, our results showed expression levels of RAC1 mRNA in the follicles with diameters of 7.0–8.0 mm, 6.0–6.9 mm and 1.0–3.9 mm were greater than other follicles (p <

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Zavarella, Salvatore, Mitsutoshi Nakada, Shawn Belverud, et al. "Role of Rac1-regulated signaling in medulloblastoma invasion." Journal of Neurosurgery: Pediatrics 4, no. 2 (2009): 97–104. http://dx.doi.org/10.3171/2009.4.peds08322.

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Object Medulloblastomas are the most common malignant brain tumors in children. These tumors are highly invasive, and patients harboring these lesions are frequently diagnosed with distant spread. In this study, the authors investigated the role of Rac1, a member of the Rho family of small guanosine triphosphatases, in medulloblastoma invasion. Methods Three established medulloblastoma cell lines were used: DAOY, UW-228, and ONS-76. Specific depletion of Rac1 protein was accomplished by transient transfection of small interfering RNA. Cell invasion through extracellular matrix (Matrigel) was q

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Vallim, Marcelo A., Connie B. Nichols, Larissa Fernandes, Kari L. Cramer, and J. Andrew Alspaugh. "A Rac Homolog Functions Downstream of Ras1 To Control Hyphal Differentiation and High-Temperature Growth in the Pathogenic Fungus Cryptococcus neoformans." Eukaryotic Cell 4, no. 6 (2005): 1066–78. http://dx.doi.org/10.1128/ec.4.6.1066-1078.2005.

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ABSTRACT The Cryptococcus neoformans Ras1 protein serves as a central regulator for several signaling pathways. Ras1 controls the induction of the mating pheromone response cascade as well as a distinct signaling pathway that allows this pathogenic fungus to grow at human physiological temperature. To characterize elements of the Ras1-dependent high-temperature growth pathway, we performed a multicopy suppressor screen, identifying genes whose overexpression allows the ras1 mutant to grow at 37°C. Using this genetic technique, we identified a C. neoformans gene encoding a Rac homolog that supp

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Chatterjee, Moumita, Linda Sequeira, Mashariki Jenkins-Kabaila, Cara W. Dubyk, Surabhi Pathak, and Kenneth L. van Golen. "Individual Rac GTPases Mediate Aspects of Prostate Cancer Cell and Bone Marrow Endothelial Cell Interactions." Journal of Signal Transduction 2011 (June 27, 2011): 1–13. http://dx.doi.org/10.1155/2011/541851.

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The Rho GTPases organize the actin cytoskeleton and are involved in cancer metastasis. Previously, we demonstrated that RhoC GTPase was required for PC-3 prostate cancer cell invasion. Targeted down-regulation of RhoC led to sustained activation of Rac1 GTPase and morphological, molecular and phenotypic changes reminiscent of epithelial to mesenchymal transition. We also reported that Rac1 is required for PC-3 cell diapedesis across a bone marrow endothelial cell layer. In the current study, we queried whether Rac3 and RhoG GTPases also have a role in prostate tumor cell diapedesis. Using spec

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Khanday, Firdous A., Lakshmi Santhanam, Kenji Kasuno, et al. "Sos-mediated activation of rac1 by p66shc." Journal of Cell Biology 172, no. 6 (2006): 817–22. http://dx.doi.org/10.1083/jcb.200506001.

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The Son of Sevenless 1 protein (sos1) is a guanine nucleotide exchange factor (GEF) for either the ras or rac1 GTPase. We show that p66shc, an adaptor protein that promotes oxidative stress, increases the rac1-specific GEF activity of sos1, resulting in rac1 activation. P66shc decreases sos1 bound to the growth factor receptor bound protein (grb2) and increases the formation of the sos1–eps8–e3b1 tricomplex. The NH2-terminal proline-rich collagen homology 2 (CH2) domain of p66shc associates with full-length grb2 in vitro via the COOH-terminal src homology 3 (C-SH3) domain of grb2. A proline-ri

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Wang, Bo, Fiona G. Wylie, Rohan D. Teasdale, and Jennifer L. Stow. "Polarized trafficking of E-cadherin is regulated by Rac1 and Cdc42 in Madin-Darby canine kidney cells." American Journal of Physiology-Cell Physiology 288, no. 6 (2005): C1411—C1419. http://dx.doi.org/10.1152/ajpcell.00533.2004.

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E-cadherin is a major cell-cell adhesion protein of epithelia that is trafficked to the basolateral cell surface in a polarized fashion. The exact post-Golgi route and regulation of E-cadherin transport have not been fully described. The Rho GTPases Cdc42 and Rac1 have been implicated in many cell functions, including the exocytic trafficking of other proteins in polarized epithelial cells. These Rho family proteins are also associated with the cadherin-catenin complexes at the cell surface. We have used functional mutants of Rac1 and Cdc42 and inactivating toxins to demonstrate specific roles

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DiPaolo, Brian C., Nurit Davidovich, Marcelo G. Kazanietz, and Susan S. Margulies. "Rac1 pathway mediates stretch response in pulmonary alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 305, no. 2 (2013): L141—L153. http://dx.doi.org/10.1152/ajplung.00298.2012.

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Alveolar epithelial cells (AECs) maintain the pulmonary blood-gas barrier integrity with gasketlike intercellular tight junctions (TJ) that are anchored internally to the actin cytoskeleton. We have previously shown that AEC monolayers stretched cyclically and equibiaxially undergo rapid magnitude- and frequency-dependent actin cytoskeletal remodeling to form perijunctional actin rings (PJARs). In this work, we show that even 10 min of stretch induced increases in the phosphorylation of Akt and LIM kinase (LIMK) and decreases in cofilin phosphorylation, suggesting that the Rac1/Akt pathway is

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Kwon, Taegun, Do Yoon Kwon, Jaesun Chun, Jae Hong Kim, and Sang Sun Kang. "Akt Protein Kinase Inhibits Rac1-GTP Binding through Phosphorylation at Serine 71 of Rac1." Journal of Biological Chemistry 275, no. 1 (2000): 423–28. http://dx.doi.org/10.1074/jbc.275.1.423.

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Yakubchyk, Yury, Hanan Abramovici, Jean-Christian Maillet та ін. "Regulation of Neurite Outgrowth in N1E-115 Cells through PDZ-Mediated Recruitment of Diacylglycerol Kinase ζ". Molecular and Cellular Biology 25, № 16 (2005): 7289–302. http://dx.doi.org/10.1128/mcb.25.16.7289-7302.2005.

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ABSTRACT Syntrophins are scaffold proteins that regulate the subcellular localization of diacylglycerol kinase ζ (DGK-ζ), an enzyme that phosphorylates the lipid second-messenger diacylglycerol to yield phosphatidic acid. DGK-ζ and syntrophins are abundantly expressed in neurons of the developing and adult brain, but their function is unclear. Here, we show that they are present in cell bodies, neurites, and growth cones of cultured cortical neurons and differentiated N1E-115 neuroblastoma cells. Overexpression of DGK-ζ in N1E-115 cells induced neurite formation in the presence of serum, which

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Silva, Guillermo B., and Jeffrey L. Garvin. "Rac1 mediates NaCl-induced superoxide generation in the thick ascending limb." American Journal of Physiology-Renal Physiology 298, no. 2 (2010): F421—F425. http://dx.doi.org/10.1152/ajprenal.00472.2009.

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Superoxide (O2−) produced by NADPH oxidase regulates Na absorption and renal hemodynamics. Increased NaCl in the thick ascending limb (TAL) stimulates O2− generation. However, we do not know whether physiological changes in NaCl concentration augment O2− generation, nor do we know the mediator(s) involved. In other cells, Rac1, a regulatory subunit of NADPH oxidase, is activated by elevated NaCl. We hypothesized that increasing luminal NaCl within the physiological range activates Rac1 and NADPH oxidase and, thereby, increases O2− production. We increased NaCl from 10 to 57 mM in medullary TAL

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Arrizabalaga, Onetsine, Hadriano M. Lacerda, Ana M. Zubiaga, and José L. Zugaza. "Rac1 Protein Regulates Glycogen Phosphorylase Activation and Controls Interleukin (IL)-2-dependent T Cell Proliferation." Journal of Biological Chemistry 287, no. 15 (2012): 11878–90. http://dx.doi.org/10.1074/jbc.m111.297804.

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Small GTPases of the Rho family have been implicated in important cellular processes such as cell migration and adhesion, protein secretion, and/or gene transcription. In the lymphoid system, these GTPases participate in the signaling cascades that are activated after engagement of antigen receptors. However, little is known about the role that Rho GTPases play in IL-2-mediated responses. Here, we show that IL-2 induces Rac1 activation in Kit 225 T cells. We identified by mass spectrometry the muscle isoform of glycogen phosphorylase (PYGM) as a novel Rac1 effector molecule in IL-2-stimulated

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Modha, Rakhee, Louise J. Campbell, Daniel Nietlispach, Heeran R. Buhecha, Darerca Owen, and Helen R. Mott. "The Rac1 Polybasic Region Is Required for Interaction with Its Effector PRK1." Journal of Biological Chemistry 283, no. 3 (2007): 1492–500. http://dx.doi.org/10.1074/jbc.m706760200.

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Protein kinase C-related kinase 1 (PRK1 or PKN) is involved in regulation of the intermediate filaments of the actin cytoskeleton, as well as having effects on processes as diverse as mitotic timing and apoptosis. It is activated by interacting with the Rho family small G proteins and arachidonic acid or by caspase cleavage. We have previously shown that the HR1b of PRK1 binds exclusively to Rac1, whereas the HR1a domain binds to both Rac1 and RhoA. Here, we have determined the solution structure of the HR1b-Rac complex. We show that HR1b binds to the C-terminal end of the effector loop and sw

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