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1-14 of 14
Keywords: RhoA
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Articles
Lorna O'Donoghue, Shane P. Comer, Dishon W. Hiebner, Ingmar Schoen, Alex von Kriegsheim, Albert Smolenski
Journal:
Biochemical Journal
Biochem J (2023) 480 (14): 1109–1127.
Published: 19 July 2023
...Lorna O'Donoghue; Shane P. Comer; Dishon W. Hiebner; Ingmar Schoen; Alex von Kriegsheim; Albert Smolenski RhoGAP6 is the most highly expressed GTPase-activating protein (GAP) in platelets specific for RhoA. Structurally RhoGAP6 contains a central catalytic GAP domain surrounded by large, disordered...
Articles
Koichi Miura, Takashi Nojiri, Yoshiharu Akitake, Koji Ando, Shigetomo Fukuhara, Masahiro Zenitani, Toru Kimura, Jun Hino, Mikiya Miyazato, Hiroshi Hosoda, Kenji Kangawa
Journal:
Biochemical Journal
Biochem J (2017) 474 (11): 1897–1918.
Published: 19 May 2017
..., guanylyl cyclase-A (GC-A), ANP maintains cardiovascular homeostasis by exerting diuretic, natriuretic, and hypotensive effects mediated, in part, by endothelial cells. Both in vivo and in vitro , ANP enhances endothelial barrier function by reducing RhoA activity and reorganizing the actin cytoskeleton. We...
Includes: Multimedia, Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2013) 452 (1): 45–55.
Published: 25 April 2013
... in controlling cell spreading and migration. cell division cycle 42 (Cdc42) focal adhesion mRNA Rac1 RhoA translation Fibroblasts are highly migratory mesenchymal cells that mediate formation and remodelling of epithelial tissues and wound healing. As such, fibroblasts are key determinants...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2012) 443 (2): 439–450.
Published: 27 March 2012
... or attenuated the neurite outgrowth associated with dynamic remodelling of the actin-based cytoskeleton. We show that γ-enolase-mediated PI3K activation regulates RhoA kinase, a key regulator of actin cytoskeleton organization. Moreover, the inhibition of RhoA downstream effector ROCK (Rho-associated kinase...
Includes: Supplementary data
Articles
Hsiang-Hao Chuang, Chih-Hsuan Yang, Yeou-Guang Tsay, Chih-Yi Hsu, Ling-Ming Tseng, Zee-Fen Chang, Hsiao-Hui Lee
Journal:
Biochemical Journal
Biochem J (2012) 443 (1): 145–151.
Published: 14 March 2012
...Hsiang-Hao Chuang; Chih-Hsuan Yang; Yeou-Guang Tsay; Chih-Yi Hsu; Ling-Ming Tseng; Zee-Fen Chang; Hsiao-Hui Lee ROCK (Rho-associated protein kinase), a downstream effector of RhoA, plays an important role in many cellular processes. Accumulating evidence has shown the involvement of ROCK activation...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2011) 439 (1): 57–65.
Published: 14 September 2011
...Dean P. Staus; Joan M. Taylor; Christopher P. Mack It is clear that RhoA activates the DRF (diaphanous-related formin) mDia2 by disrupting the molecular interaction between the DAD (diaphanous autoregulatory domain) and the DID (diaphanous inhibitory domain). Previous studies indicate that a basic...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2011) 436 (3): 699–708.
Published: 27 May 2011
.... This interaction was involved in a laminin 511/521-to-actin signalling pathway leading to stress fibre formation. This skeletal rearrangement was associated with an activation of the small GTP-binding protein RhoA, which depended on the integrity of the Lu/BCAM laminin 511/521-binding site. It also required a Lu...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2004) 381 (2): 397–403.
Published: 06 July 2004
..., a Clostridium botulinum toxin and a selective inhibitor of the Rho family GTPase RhoA, and by co-transfection with a dominant negative form of RhoA. Co-transfection with a constitutively active form of RhoA stimulated expression 11.6±1.7-fold over basal. Mutations through the 104 bp construct identified a C...
Articles
Journal:
Biochemical Journal
Biochem J (2003) 371 (2): 565–571.
Published: 15 April 2003
... for the progression of the cytoskeletal response and that these include activation of RhoA. 1 To whom correspondence should be addressed (e-mail [email protected] ). 28 8 2002 12 12 2002 8 1 2003 8 1 2003 The Biochemical Society, London ©2003 2003 cell-surface...
Articles
A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases
Journal:
Biochemical Journal
Biochem J (2002) 367 (1): 57–65.
Published: 01 October 2002
... in vitro the GTPase activity of RhoA, but is inactive towards other Rho family proteins such as Rac1 and Cdc42; it is also specific for RhoA in vivo . The same is true for the full-length protein, which is furthermore able to down-regulate RhoA-dependent stress fibres in Ref-52 rat fibroblasts...
Articles
Journal:
Biochemical Journal
Biochem J (2002) 365 (1): 157–163.
Published: 01 July 2002
.... Accordingly, we used the Rhotekin binding assay to assess RhoA activation in intestinal epithelial cells and observed that RhoA was activated by leukotriene D 4 (LTD 4 ). We also found that, within 15s, activation of RhoA by LTD 4 led to an increased association of RhoA with G-protein βγ (Gβγ...
Articles
Andrea BLOMQUIST, Guntram SCHWÖRER, Helge SCHABLOWSKI, Amalia PSOMA, Michaela LEHNEN, Karl H. JAKOBS, Ulrich RÜMENAPP
Journal:
Biochemical Journal
Biochem J (2000) 352 (2): 319–325.
Published: 24 November 2000
... homology domain. p114-Rho-GEF interacted specifically with RhoA, in its nucleotide-free and guanosine 5′-[γ-thio]triphosphate-bound states, but not with Rac1 and Cdc42, and efficiently catalysed guanine nucleotide exchange of RhoA. Consistent with these results in vitro was our finding...
Articles
Journal:
Biochemical Journal
Biochem J (2000) 351 (3): 613–619.
Published: 24 October 2000
..., are expressed at sufficient levels. 1 To whom correspondence should be addressed (e-mail [email protected] ). 27 3 2000 26 6 2000 15 8 2000 The Biochemical Society, London © 2000 2000 regulation interaction ADP-ribosylation factor RhoA Biochem. J. (2000) 351, 613 619...
Articles
Journal:
Biochemical Journal
Biochem J (1999) 337 (2): 185–192.
Published: 08 January 1999
...)-mediated PLD activation, their role in monosodium urate (MSU)-stimulated PLD1 activity in human neutrophils is not clear. The translocation of PKCα, RhoA and Arf from the cytosol to the membranes was monitored. fMLP induced a cytochalasin B (CB)-dependent recruitment of Arf, RhoA and PKCα to neutrophil...