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Добірка наукової літератури з теми "Rac1 protein"

Автор: Grafiati

Опубліковано: 11 березня 2023

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Статті в журналах з теми "Rac1 protein"

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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