Rho‐specific binding and guanine nucleotide exchange catalysis by KIAA0380, a Dbl family member

@article{Rmenapp1999RhospecificBA,
  title={Rho‐specific binding and guanine nucleotide exchange catalysis by KIAA0380, a Dbl family member},
  author={Ulrich R{\"u}menapp and Andrea Blomquist and G. Schw{\"o}rer and Helge Schablowski and Amalia Psoma and Karl Jakobs},
  journal={FEBS Letters},
  year={1999},
  volume={459}
}
XPLN, a Guanine Nucleotide Exchange Factor for RhoA and RhoB, But Not RhoC*
TLDR
A Rho family GEF that can discriminate between the closely related RhoA, RhoB, and RhoC is described, possibly giving insight to the divergent functions of these three proteins.
Identification and characterization of a novel Rho-specific guanine nucleotide exchange factor.
TLDR
Rho GTPases are implicated in a multitude of cellular processes regulated by membrane receptors, such as cytoskeletal rearrangements, gene transcription and cell growth and motility, and the activity of this novel Rho-GEF, which is widely expressed in human tissues, can be controlled by G-protein-coupled receptors.
A mammalian Rho-specific guanine-nucleotide exchange factor (p164-RhoGEF) without a pleckstrin homology domain.
Rho GTPases, which are activated by specific guanine-nucleotide exchange factors (GEFs), play pivotal roles in several cellular functions. We identified a recently cloned human cDNA, namely KIAA0337,
Mechanistic Insights into Specificity, Activity, and Regulatory Elements of the Regulator of G-protein Signaling (RGS)-containing Rho-specific Guanine Nucleotide Exchange Factors (GEFs) p115, PDZ-RhoGEF (PRG), and Leukemia-associated RhoGEF (LARG)*
TLDR
This comparative study presents detailed kinetic data on specificity, activity, and regulation of the catalytic DH domains of four GEFs, namely p115, p190, PDZ-RhoGEF (PRG), and leukemia-associated Rho GEF (LARG), supporting the proposed models of an intramolecular autoinhibitory mechanism for p115-like RhoGEFs.
Interaction of plexin-B1 with PDZ domain-containing Rho guanine nucleotide exchange factors.
p63RhoGEF and GEFT are Rho-specific guanine nucleotide exchange factors encoded by the same gene
TLDR
It is concluded that p63RhoGEF and GEFT are apparently isoforms derived from the same gene and that GEFT, similar to p63Cdc42-specific GEF, activates RhoA in several cell types.
The Minimal Autoinhibited Unit of the Guanine Nucleotide Exchange Factor Intersectin
TLDR
It is proposed that the actual autoinhibited structure contains the related intramolecular SH3(E)-DH interaction, which may block or distort the GTPase binding region of the DH domain.
Identification of a novel sequence in PDZ-RhoGEF that mediates interaction with the actin cytoskeleton.
TLDR
It is demonstrated that PDZ-RhoGEF, a member of a subfamily of RhoGEFs that contain regulator of G protein signaling domains, is partially localized at or near the plasma membranes in 293T, COS-7, and Neuro2a cells, and this localization is coincident with cortical actin.
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A Novel PDZ Domain Containing Guanine Nucleotide Exchange Factor Links Heterotrimeric G Proteins to Rho*
TLDR
The findings suggest the existence of a novel mechanism whereby the large family of cell surface receptors that transmit signals through heterotrimeric G proteins activate Rho-dependent pathways: by stimulating the activity of members of the Gα12 family which, in turn, activate an exchange factor acting on Rho.
Cloning and Characterization of GEF-H1, a Microtubule-associated Guanine Nucleotide Exchange Factor for Rac and Rho GTPases*
TLDR
Results suggest that GEF-H1 may have a direct role in activation of Rac and/or Rho and in bringing the activated GTPase to specific target sites such as microtubules.
Lfc and Lsc Oncoproteins Represent Two New Guanine Nucleotide Exchange Factors for the Rho GTP-binding Protein*
TLDR
It is shown that Lfc and Lsc, like their closest relative Lbc, are highly specific guanine nucleotide exchange factors (GEFs) for Rho, causing a >10-fold stimulation of [3H]GDP dissociation from Rho and a marked stimulation of GDP-[35S]GTPγs (guanosine 5′-O-(3-thiotriphosphate) exchange.
Identification of a Novel Guanine Nucleotide Exchange Factor for the Rho GTPase*
TLDR
Results indicate that p115-RhoGEF may be a general regulator of Rho and its associated cellular phenotypes, as determined by its ability to induce the transformation of NIH 3T3 cells.
Analysis of RhoA-binding Proteins Reveals an Interaction Domain Conserved in Heterotrimeric G Protein β Subunits and the Yeast Response Regulator Protein Skn7*
TLDR
Functional assays in yeast suggest that the Skn7 ROCK-I/Kinectin homology region is required for its function in vivo, and it is shown that β2 and Skn 7 can interact with mammalian RhoA and Cdc42 and yeast Rho1, both in vivo and in vitro.
Activation of RhoA and SAPK/JNK signalling pathways by the RhoA‐specific exchange factor mNET1
TLDR
MNET1 can activate signalling pathways in addition to those directly controlled by activated RhoA, and requires a C3 transferase‐sensitive GTPase, although mNET1ΔN‐induced SAPK/JNK activation occurs independently of the generation of titratable GTP‐bound Rho a.
p115 RhoGEF, a GTPase activating protein for Gα12 and Gα13
Members of the regulators of G protein signaling (RGS) family stimulate the intrinsic guanosine triphosphatase (GTPase) activity of the α subunits of certain heterotrimeric guanine nucleotide–binding
Guanine Nucleotide Exchange Factors Regulate Specificity of Downstream Signaling from Rac and Cdc42*
TLDR
Investigating the action of several well characterized guanine nucleotide exchange factors (GEFRho) to activate Rac- and/or Cdc42-dependent kinase pathways concludes that GEFs can be important determinants of downstream signaling specificity for members of the Rho GTPase family.
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