Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway

@article{Brown1996HumanSH,
  title={Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway},
  author={Jeffrey Brown and Lisa Stowers and M. Baer and JoAnn Trejo and Shaun R Coughlin and John Chant},
  journal={Current Biology},
  year={1996},
  volume={6},
  pages={598-605}
}

Figures from this paper

Characterization of OSR1, a Member of the Mammalian Ste20p/Germinal Center Kinase Subfamily*

Analysis of the protein kinase components of mitogen-activated protein (MAP) kinase (MAPK) cascades in Drosophila S2 cells found that distinct upstream kinases were involved in responses to sorbitol and lipopolysaccharide, and extended that analysis to the possible MAPK kinase kinase Kinases (MAP4Ks) in the JNK pathway.

Regulation of Phosphorylation Pathways by p21 GTPases

Members of the Rho subfamily, and kinases that bind to these p21s are intimately involved in immediate morphological processes as well as long-term transcriptional events, with their associated kinases having a role in the integration of the reorganization of the actin cytoskeleton.

MST4, a new Ste20-related kinase that mediates cell growth and transformation via modulating ERK pathway

The cloning and characterization of a novel human Ste20-related kinase that is highly homologous to MST3 and SOK is reported, providing the first evidence that MST4 is biologically active in the activation of MEK/ERK pathway and in mediating cell growth and transformation.

Hsl7p, a negative regulator of Ste20p protein kinase in the Saccharomyces cerevisiae filamentous growth-signaling pathway.

A potent negative regulator of Ste20p in the yeast filamentous growth-signaling pathway is described and it is suggested that Cdc42p and Hsl7p compete for binding to Ste 20p for pseudohyphal development when starved for nitrogen.

Cdc42: An Essential Rho-Type GTPase Controlling Eukaryotic Cell Polarity

In the budding yeast Saccharomyces cerevisiae, Cdc42p plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth.

A Novel Regulator of p21-activated Kinases*

The identification of two closely related Pak3-binding proteins, possibly arising from alternative splicing, designated p50 and p85Cool-1 (cloned out of library) are reported, indicating a novel mechanism of regulation of Pak signaling.

A Conserved Gβ Binding (GBB) Sequence Motif in Ste20p/PAK Family Protein Kinases

The GBB motif is a novel type of signaling domain that serves to link protein kinases of the Ste20p/PAK family to G protein coupled receptors.

Isolation of TAO1, a Protein Kinase That Activates MEKs in Stress-activated Protein Kinase Cascades*

The activation of and binding to MEK3 by TAO1 implicates TAO2 in the regulation of the p38-containing stress-responsive MAP kinase pathway, and showsTAO1 is highly expressed in brain, as is a homolog TAO 2.

Human JIK, a Novel Member of the STE20 Kinase Family That Inhibits JNK and Is Negatively Regulated by Epidermal Growth Factor*

JIK might represent the first member of the STE20 kinase family whose activity can be negatively regulated by tyrosine kinase receptors, and whose downstream targets inhibit, rather than enhance, JNK/SAPK activation.
...

References

SHOWING 1-10 OF 44 REFERENCES

Identification of a Mouse p21Cdc42/Rac Activated Kinase (*)

It is found that mPAK-3, expressed in vitro and in vivo, shows highly specific binding to the SH3 domain of phospholipase C- and at least one SH3domain in the adapter protein Nck, raising the possibility of an additional level of regulation of the PAK family in vivo.

Rho Family GTPases Regulate p38 Mitogen-activated Protein Kinase through the Downstream Mediator Pak1 (*)

Rac and Cdc42 appear to regulate a protein kinase cascade initiated at the level of Pak and leading to activation of p38 and JNK, and a dominant negative Pak1 suppresses both interleukin-1- and Rac/Cdc42-induced p38 activity.

Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85.

It is suggested that PI 3-kinase, through the Rho-GAP homology domain of p85, can couple to the effector domain of Cdc42Hs and that p85 may be a target for the GTP-bound forms of CDC42HS and Rac1.

An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1

When microinjected into quiescent fibroblasts, Rho, Rac, and Cdc42 stimulated cell cycle progression through G1 and subsequent DNA synthesis, and microinjection of dominant negative forms of Rac and CDC42 or of the Rho inhibitor C3 transferase blocked serum-induced DNA synthesis.

Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24

It is proposed that Cdc42p plays a pivotal role both in polarization of the cytoskeleton and in pheromone signalling in Saccharomyces cerevisiae.

Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase

Activation of the SAPK pathway by GCK illustrates further the striking conservation of eukaryotic signalling mechanisms and defines the first physiological function of a mammalian Ste20.

A novel serine kinase activated by rac1/CDC42Hs‐dependent autophosphorylation is related to PAK65 and STE20.

HPAK65 had only a marginal effect on the intrinsic GTPase activity of CDC42Hs, but significantly affected the binding and GAP activity of p190, consistent with a model in which hPAK 65 functions as an effector molecule for rac1 and CDC42 Hs.

A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42

The findings indicate that there may be a regulatory mechanism that sustains the GTP-bound active form of Cdc42Hs and which is directly linked to a tyrosine phosphorylation pathway.

Cdc42 and PAK-mediated Signaling Leads to Jun Kinase and p38 Mitogen-activated Protein Kinase Activation (*)

The PAK family of protein kinases has been suggested as a potential target of the Cdc42 and Rac GTPases based on studies in vitro but it is shown that PAK-3 is activated by CDC42 in vivo and may mediate the effects of cytokines on transcriptional regulation.