scholarly journals A GAL4-inducible transgenic tool kit for the in vivo modulation of Rho GTPase activity in zebrafish

2016 ◽  
Vol 245 (8) ◽  
pp. 844-853 ◽  
Author(s):  
Nicholas J. Hanovice ◽  
Emily McMains ◽  
Jeffrey M. Gross
Keyword(s):  
Rho Gtpase ◽  
Gtpase Activity

scholarly journals Corrigendum: A GAL4-inducible transgenic tool kit for the in vivo modulation of Rho GTPase activity in zebrafish

2017 ◽  
Vol 246 (6) ◽  
pp. 485-485
Author(s):  
Nicholas J. Hanovice ◽  
Emily McMains ◽  
Jeffrey M. Gross
Keyword(s):  
Rho Gtpase ◽  
Gtpase Activity

scholarly journals Cell Cycle-Dependent Rho GTPase Activity Dynamically Regulates Cancer Cell Motility and Invasion In Vivo

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e83629 ◽  
Author(s):  
Yoshinori Kagawa ◽  
Shinji Matsumoto ◽  
Yuji Kamioka ◽  
Koshi Mimori ◽  
Yoko Naito ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Motility ◽  
Cancer Cell ◽  
Rho Gtpase ◽  
Gtpase Activity ◽  
Cancer Cell Motility ◽  
Cycle Dependent

scholarly journals Secretory Pathway-Dependent Localization of the Saccharomyces cerevisiae Rho GTPase-Activating Protein Rgd1p at Growth Sites

2012 ◽  
Vol 11 (5) ◽  
pp. 590-600 ◽  
Author(s):  
Fabien Lefèbvre ◽  
Valérie Prouzet-Mauléon ◽  
Michel Hugues ◽  
Marc Crouzet ◽  
Aurélie Vieillemard ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Cell Cycle Progression ◽  
Secretory Pathway ◽  
Rho Gtpase ◽  
Secretory Vesicles ◽  
Gtpase Activating Protein ◽  
Content Type

ABSTRACT Establishment and maintenance of cell polarity in eukaryotes depends upon the regulation of Rho GTPases. In Saccharomyces cerevisiae , the Rho GTPase activating protein (RhoGAP) Rgd1p stimulates the GTPase activities of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. Consistent with the distribution of Rho3p and Rho4p, Rgd1p is found mostly in areas of polarized growth during cell cycle progression. Rgd1p was mislocalized in mutants specifically altered for Golgi apparatus-based phosphatidylinositol 4-P [PtdIns(4)P] synthesis and for PtdIns(4,5)P 2 production at the plasma membrane. Analysis of Rgd1p distribution in different membrane-trafficking mutants suggested that Rgd1p was delivered to growth sites via the secretory pathway. Rgd1p may associate with post-Golgi vesicles by binding to PtdIns(4)P and then be transported by secretory vesicles to the plasma membrane. In agreement, we show that Rgd1p coimmunoprecipitated and localized with markers specific to secretory vesicles and cofractionated with a plasma membrane marker. Moreover, in vivo imaging revealed that Rgd1p was transported in an anterograde manner from the mother cell to the daughter cell in a vectoral manner. Our data indicate that secretory vesicles are involved in the delivery of RhoGAP Rgd1p to the bud tip and bud neck.

scholarly journals Inactivation of Rho GTPases by Statins Attenuates Anthrax Lethal Toxin Activity

2008 ◽  
Vol 77 (1) ◽  
pp. 348-359 ◽  
Author(s):  
Aimee M. deCathelineau ◽  
Gary M. Bokoch
Keyword(s):  
Rho Gtpases ◽  
Rho Gtpase ◽  
Protective Antigen ◽  
Biological Effects ◽  
Lethal Factor ◽  
Lethal Toxin ◽  
Mitogen Activated Protein Kinase ◽  
Gtpase Activity ◽  
Anthrax Lethal Toxin ◽  
Reductase Inhibitors

ABSTRACT Anthrax lethal factor (LF), secreted by Bacillus anthracis, interacts with protective antigen to form a bipartite toxin (lethal toxin [LT]) that exerts pleiotropic biological effects resulting in subversion of the innate immune response. Although the mitogen-activated protein kinase kinases (MKKs) are the major intracellular protein targets of LF, the pathology induced by LT is not well understood. The statin family of HMG-coenzyme A reductase inhibitors have potent anti-inflammatory effects independent of their cholesterol-lowering properties, which have been attributed to modulation of Rho family GTPase activity. The Rho GTPases regulate vesicular trafficking, cytoskeletal dynamics, and cell survival and proliferation. We hypothesized that disruption of Rho GTPase function by statins might alter LT action. We show here that statins delay LT-induced death and MKK cleavage in RAW macrophages and that statin-mediated effects on LT action are attributable to disruption of Rho GTPases. The Rho GTPase-inactivating toxin, toxin B, did not significantly affect LT binding or internalization, suggesting that the Rho GTPases regulate trafficking and/or localization of LT once internalized. The use of drugs capable of inhibiting Rho GTPase activity, such as statins, may provide a means to attenuate intoxication during B. anthracis infection.

scholarly journals Low-dose Chemotherapeutic Agents Regulate Small Rho GTPase Activity in Dendritic Cells

2008 ◽  
Vol 31 (5) ◽  
pp. 491-499 ◽  
Author(s):  
Galina V. Shurin ◽  
Irina L. Tourkova ◽  
Michael R. Shurin
Keyword(s):  
Dendritic Cells ◽  
Low Dose ◽  
Rho Gtpase ◽  
Chemotherapeutic Agents ◽  
Gtpase Activity

scholarly journals The Formin mDia Regulates GSK3β through Novel PKCs to Promote Microtubule Stabilization but Not MTOC Reorientation in Migrating Fibroblasts

2006 ◽  
Vol 17 (12) ◽  
pp. 5004-5016 ◽  
Author(s):  
Christina H. Eng ◽  
Thomas M. Huckaba ◽  
Gregg G. Gundersen
Keyword(s):  
Rho Gtpase ◽  
Glycogen Synthase ◽  
Dominant Negative ◽  
Microtubule Stabilization ◽  
3T3 Fibroblasts ◽  
Organizing Center ◽  
Inhibitory Site ◽  
External Signals

In migrating cells, external signals polarize the microtubule (MT) cytoskeleton by stimulating the formation of oriented, stabilized MTs and inducing the reorientation of the MT organizing center (MTOC). Glycogen synthase kinase 3β (GSK3β) has been implicated in each of these processes, although whether it regulates both processes in a single system and how its activity is regulated are unclear. We examined these issues in wound-edge, serum-starved NIH 3T3 fibroblasts where MT stabilization and MTOC reorientation are triggered by lysophosphatidic acid (LPA), but are regulated independently by distinct Rho GTPase-signaling pathways. In the absence of other treatments, the GSK3β inhibitors, LiCl or SB216763, induced the formation of stable MTs, but not MTOC reorientation, in starved fibroblasts. Overexpression of GSK3β in starved fibroblasts inhibited LPA-induced stable MTs without inhibiting MTOC reorientation. Analysis of factors involved in stable MT formation (Rho, mDia, and EB1) showed that GSK3β functioned upstream of EB1, but downstream of Rho-mDia. mDia was both necessary and sufficient for inducing stable MTs and for up-regulating GSK3β phosphorylation on Ser9, an inhibitory site. mDia appears to regulate GSK3β through novel class PKCs because PKC inhibitors and dominant negative constructs of novel PKC isoforms prevented phosphorylation of GSK3β Ser9 and stable MT formation. Novel PKCs also interacted with mDia in vivo and in vitro. These results identify a new activity for the formin mDia in regulating GSK3β through novel PKCs and implicate novel PKCs as new factors in the MT stabilization pathway.

scholarly journals The Myosin IXb Motor Activity Targets the Myosin IXb RhoGAP Domain as Cargo to Sites of Actin Polymerization

2007 ◽  
Vol 18 (4) ◽  
pp. 1507-1518 ◽  
Author(s):  
Frank van den Boom ◽  
Heiko Düssmann ◽  
Katharina Uhlenbrock ◽  
Marouan Abouhamed ◽  
Martin Bähler
Keyword(s):  
Motor Activity ◽  
Actin Polymerization ◽  
Fluorescence Recovery After Photobleaching ◽  
Rho Gtpase ◽  
Tail Region ◽  
Lysine Residues ◽  
Motor Region ◽  
Necessary And Sufficient ◽  
Loop 2

Myosin IXb (Myo9b) is a single-headed processive myosin that exhibits Rho GTPase-activating protein (RhoGAP) activity in its tail region. Using live cell imaging, we determined that Myo9b is recruited to extending lamellipodia, ruffles, and filopodia, the regions of active actin polymerization. A functional motor domain was both necessary and sufficient for targeting Myo9b to these regions. The head domains of class IX myosins comprise a large insertion in loop2. Deletion of the large Myo9b head loop 2 insertion abrogated the enrichment in extending lamellipodia and ruffles, but enhanced significantly the enrichment at the tips of filopodia and retraction fibers. The enrichment in the tips of filopodia and retraction fibers depended on four lysine residues C-terminal to the loop 2 insertion and the tail region. Fluorescence recovery after photobleaching and photoactivation experiments in lamellipodia revealed that the dynamics of Myo9b was comparable to that of actin. The exchange rates depended on the Myo9b motor region and motor activity, and they were also dependent on the turnover of F-actin. These results demonstrate that Myo9b functions as a motorized RhoGAP molecule in regions of actin polymerization and identify Myo9b head sequences important for in vivo motor properties.

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