Pleckstrin homology (PH) domains in signal transducton

@article{Ingley1994PleckstrinH,
  title={Pleckstrin homology (PH) domains in signal transducton},
  author={Evan Ingley and Brian A. Hemmings},
  journal={Journal of Cellular Biochemistry},
  year={1994},
  volume={56}
}
A diverse array of molecules involved in signal transduction have recently been recognised as containing a new homology domain, the pleckstrin homology (PH) domain. These include kinases (both serine/threonine and tyrosine specific), all currently known mammalian phospholipase Cs, GTPases, GTPage‐activatng proteins, GTpace‐exchange factors, “adapter” proteins, cyotskeletal proteins, and kinase substrates. This has sparked a new surge of research into elucidating its sturcture and function. The… 
A Phosphatidylinositol 4-Kinase Pleckstrin Homology Domain That Binds Phosphatidylinositol 4-Monophosphate*
TLDR
The recombinant PI 4-kinase PH domain was explored for its ability to bind to different phospholipids and had the highest affinity for PI-4-P, the product of the reaction.
Structure of the binding site for inositol phosphates in a PH domain.
TLDR
A model in which PH domains are involved in reversible anchoring of proteins to membranes via their specific binding to phosphoinositides is proposed, which could also participate in a response to a second messenger such as inositol trisphosphate, organizing cross‐roads in cellular signalling.
The pleckstrin homology domain: An intriguing multifunctional protein module
  • G. Shaw
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1996
TLDR
PH domains are discussed in detail and it is concluded that they form a versatile family of membrane binding and protein localization modules.
Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins
  • H. Levine
  • Biology, Chemistry
    Molecular Neurobiology
  • 2007
TLDR
This review describes what is known about the physical structures of the 7-transmembrane helix receptors, the heterotrimeric GTP binding coupling proteins, the adenylate cyclase and phospholipase C effector proteins, and signaling modulatory proteins.
Pleckstrin homology domains: a fact file.
RACK1, a protein kinase C anchoring protein, coordinates the binding of activated protein kinase C and select pleckstrin homology domains in vitro.
TLDR
In vitro data suggest that Rack1 binds selective PH domains, and that PKC regulates this interaction, and it is proposed that, in vivo, RACK1 may colocalize the kinase with its PH domain-containing substrates.
Large-scale expression and purification of a soluble form of the pleckstrin homology domain of the human protooncogenic serine/threonine protein kinase PKB (c-akt) in Escherichia coli.
TLDR
Large-scale purification of the PKB PH domain was easily achieved by exploiting the (His)(6) tag and the high isoelectric point of the protein attributable to the additional 3 carboxyl-terminal lysines.
Novel inhibitors of AKT: assessment of a different approach targeting the pleckstrin homology domain.
TLDR
This review summarizes other approaches scientists have developed to inhibit the activity and function of protein kinase B/AKT by targeting the pleckstrin homology (PH) domain of AKT.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 31 REFERENCES
Structure of the pleckstrin homology domain from β-spectrin
TLDR
The three-dimensional structure of the PH domain of the cytoskeletal protein spectrin is reported using homonuclear nuclear magnetic resonance to report a distant relationship to the peptidyl-prolyl-cis-trans-isomerase FKBP in which this pocket is involved in the binding of the macrocyclic compound FK506.
Solution structure of a pleckstrin-homology domain
TLDR
The solution structure of the N-terminal pleckstrin-homology domain of pleckSTRin is determined using heteronuclear three-dimensional nuclear magnetic resonance spectroscopy and is similar to that of the retinol-binding protein family of structures.
Identification of novel pleckstrin homology (PH) domains provides a hypothesis for PH domain function.
  • G. Shaw
  • Biology
    Biochemical and biophysical research communications
  • 1993
TLDR
A simple program developed to overcome this difficulty identified three proteins containing previously unrecognized PH domains; the beta-adrenergic receptor kinase, the tecA protein kinase and the insulin receptor substrate protein IRS-1, suggesting a general hypothesis for PH domain function.
SH2 domain specificity and activity modified by a single residue
TLDR
The results identify a residue that can modify SH2 selectivity, and indicate that the biological activity of an SH2 domain correlates with its binding specificity.
Lipid modification at the N terminus of photoreceptor G-protein α-subunit
TLDR
It is suggested that a looser subunit interaction in transducin which is due to an abundance of N-linked fatty acids other than myristate would favour the rapid turnover and catalysis essential for the visual excitation in photoreceptor cells.
Diversity of G proteins in signal transduction
TLDR
The heterotrimeric guanine nucleotide-binding proteins acting as switches that regulate information processing circuits connecting cell surface receptors to a variety of effectors generate the pathways that modulate cellular responses to complex chemical signals.
...
1
2
3
4
...