scholarly journals Developmentally regulated GTP-binding protein 1 modulates ciliogenesis via an interaction with Dishevelled

2019 ◽  
Vol 218 (8) ◽  
pp. 2659-2676 ◽  
Author(s):  
Moonsup Lee ◽  
Yoo-Seok Hwang ◽  
Jaeho Yoon ◽  
Jian Sun ◽  
Adam Harned ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Binding Protein ◽  
Basal Bodies ◽  
Apical Surface ◽  
Gtp Binding Protein ◽  
Developmentally Regulated ◽  
Rhoa Activity ◽  
Gtp Binding ◽  
Xenopus Laevis Embryo ◽  
Multiciliated Cells

Cilia are critical for proper embryonic development and maintaining homeostasis. Although extensively studied, there are still significant gaps regarding the proteins involved in regulating ciliogenesis. Using the Xenopus laevis embryo, we show that Dishevelled (Dvl), a key Wnt signaling scaffold that is critical to proper ciliogenesis, interacts with Drg1 (developmentally regulated GTP-binding protein 1). The loss of Drg1 or disruption of the interaction with Dvl reduces the length and number of cilia and displays defects in basal body migration and docking to the apical surface of multiciliated cells (MCCs). Moreover, Drg1 morphants display abnormal rotational polarity of basal bodies and a decrease in apical actin and RhoA activity that can be attributed to disruption of the protein complex between Dvl and Daam1, as well as between Daam1 and RhoA. These results support the concept that the Drg1–Dvl interaction regulates apical actin polymerization and stability in MCCs. Thus, Drg1 is a newly identified partner of Dvl in regulating ciliogenesis.

scholarly journals Developmentally Regulated GTP binding protein 1 (DRG1) controls microtubule dynamics

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Anna Katharina Schellhaus ◽  
Daniel Moreno-Andrés ◽  
Mayank Chugh ◽  
Hideki Yokoyama ◽  
Athina Moschopoulou ◽  
...  
Keyword(s):  
Binding Protein ◽  
Microtubule Dynamics ◽  
Gtp Binding Protein ◽  
Developmentally Regulated ◽  
Gtp Binding

DRG: A novel developmentally regulated GTP-binding protein

1992 ◽  
Vol 189 (1) ◽  
pp. 363-370 ◽  
Author(s):  
Takashi Sazuka ◽  
Yasuhiro Tomooka ◽  
Yoji Ikawa ◽  
Makoto Noda ◽  
Sharad Kumar
Keyword(s):  
Binding Protein ◽  
Gtp Binding Protein ◽  
Developmentally Regulated ◽  
Gtp Binding

Cloning and characterization of Xenopus laevis drg2, a member of the developmentally regulated GTP-binding protein subfamily

Gene ◽  
2003 ◽  
Vol 322 ◽  
pp. 105-112 ◽  
Author(s):  
Kosuke Ishikawa ◽  
Sakura Azuma ◽  
Shuntaro Ikawa ◽  
Yasuyuki Morishita ◽  
Jin Gohda ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Developmentally Regulated ◽  
Gtp Binding

Developmentally regulated GTP-binding protein 2 ameliorates EAE by suppressing the development of TH17 cells

2014 ◽  
Vol 150 (2) ◽  
pp. 225-235 ◽  
Author(s):  
Myoung Seok Ko ◽  
Hyo Jeong Kim ◽  
Hong Kyung Kim ◽  
Nal Ae Yoon ◽  
Unn Hwa Lee ◽  
...  
Keyword(s):  
Th17 Cells ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Developmentally Regulated ◽  
Gtp Binding

scholarly journals ADP-ribosylation of the GTP-binding protein Rho by Clostridium limosum exoenzyme affects basal, but not N-formyl-peptide-stimulated, actin polymerization in human myeloid leukaemic (HL60) cells

1994 ◽  
Vol 299 (3) ◽  
pp. 775-779 ◽  
Author(s):  
G Koch ◽  
J Norgauer ◽  
K Aktories
Keyword(s):  
Actin Polymerization ◽  
Binding Protein ◽  
Dependent Manner ◽  
Gtp Binding Protein ◽  
Intact Cells ◽  
Hl60 Cells ◽  
Adp Ribosylation ◽  
Gtp Binding ◽  
Long Term Treatment ◽  
Formyl Peptide

Treatment of human myeloid leukaemic (HL60) cells with Clostridium limosum exoenzyme, which inactivates the small GTP-binding protein Rho by ADP-ribosylation, decreased the basal F-actin content. Inhibition of F-actin occurred after long-term treatment (24 h) of intact HL60 cells or after introduction of the toxin by electropermeabilization in a toxin-concentration-dependent manner. Concomitantly with the decrease in the basal F-actin content, the GTP-binding protein Rho was ADP-ribosylated in intact cells. However, Clostridium limosum toxin had no inhibitory effect on N-formyl-peptide-induced actin polymerization. Moreover, the relative N-formyl-peptide-stimulated polymerization was substantially enhanced in cells treated with Clostridium limosum transferase. In contrast with Clostridium limosum exoenzyme, component C21 of the Clostridium botulinum C2 toxin, which ADP-ribosylates G-actin, depolymerized basal F-actin and inhibited N-formyl-peptide-induced actin polymerization in electropermeabilized HL60 cells. These findings indicate that Rho proteins are involved in the basal, but not the ligand-evoked, actin polymerization in HL60 cells.

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