<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>22(20)</volume><submitter>Maeda M</submitter><pubmed_abstract>Rho GTPases are molecular switches that transmit biochemical signals in response to extracellular stimuli to elicit changes in the actin cytoskeleton. Rho GTPases cycle between an active, GTP-bound state and an inactive, GDP-bound state. These states are regulated by two distinct families of proteins-guanine nucleotide exchange factors and GTPase-activating proteins (GAPs). We studied the role of a previously uncharacterized GAP, ARHGAP18 (MacGAP). Overexpression of ARHGAP18 suppressed the activity of RhoA and disrupted stress fiber formation. Conversely, silencing of ARHGAP18 by small interfering RNA transfection-enhanced stress fiber formation and induced rounding of cells. We examined the role of ARHGAP18 in cell spreading and migration. Immunofluorescence analysis revealed that ARHGAP1</pubmed_abstract><journal>Molecular biology of the cell</journal><pagination>3840-52</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3192863</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>ARHGAP18, a GTPase-activating protein for RhoA, controls cell shape, spreading, and motility.</pubmed_title><pmcid>PMC3192863</pmcid><pubmed_authors>Shimokata K</pubmed_authors><pubmed_authors>Hasegawa H</pubmed_authors><pubmed_authors>Senga T</pubmed_authors><pubmed_authors>Asano E</pubmed_authors><pubmed_authors>Yuang H</pubmed_authors><pubmed_authors>Hyodo T</pubmed_authors><pubmed_authors>Ito S</pubmed_authors><pubmed_authors>Hasegawa Y</pubmed_authors><pubmed_authors>Funasaka K</pubmed_authors><pubmed_authors>Hamaguchi M</pubmed_authors><pubmed_authors>Maeda M</pubmed_authors></additional><is_claimable>false</is_claimable><name>ARHGAP18, a GTPase-activating protein for RhoA, controls cell shape, spreading, and motility.</name><description>Rho GTPases are molecular switches that transmit biochemical signals in response to extracellular stimuli to elicit changes in the actin cytoskeleton. Rho GTPases cycle between an active, GTP-bound state and an inactive, GDP-bound state. These states are regulated by two distinct families of proteins-guanine nucleotide exchange factors and GTPase-activating proteins (GAPs). We studied the role of a previously uncharacterized GAP, ARHGAP18 (MacGAP). Overexpression of ARHGAP18 suppressed the activity of RhoA and disrupted stress fiber formation. Conversely, silencing of ARHGAP18 by small interfering RNA transfection-enhanced stress fiber formation and induced rounding of cells. We examined the role of ARHGAP18 in cell spreading and migration. Immunofluorescence analysis revealed that ARHGAP1</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Oct</publication><modification>2025-04-04T07:24:43.534Z</modification><creation>2019-03-27T00:44:56Z</creation></dates><accession>S-EPMC3192863</accession><cross_references><pubmed>21865595</pubmed><doi>10.1091/mbc.E11-04-0364</doi></cross_references></HashMap>