UPDATE: PH Domains--A Universal Membrane Adapter
- 28 March 1997
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 275 (5308), 1899
- https://doi.org/10.1126/science.275.5308.1899
Abstract
The enzyme PI 3-kinase seems to mediate extraordinarily diverse cellular responses to growth factors. In his Update Perspective, Hemmings offers an explanation by outlining the evidence for a common target of the phospholipid signaling molecules generated by PI 3-kinase—the pleckstrin homology (PH) domains located on at least 100 cellular proteins, which could mediate the diverse responses of cells. On p. 1927 of this issue, Klarlund et al . report the isolation of one of these PH domain-containing proteins, GRP1.Keywords
This publication has 10 references indexed in Scilit:
- Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology DomainsScience, 1997
- Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factorProceedings of the National Academy of Sciences, 1997
- Direct Regulation of the Akt Proto-Oncogene Product by Phosphatidylinositol-3,4-bisphosphateScience, 1997
- A Specific Product of Phosphatidylinositol 3-Kinase Directly Activates the Protein Kinase Akt through Its Pleckstrin Homology DomainMolecular and Cellular Biology, 1997
- A human exchange factor for ARF contains Sec7- and pleckstrin-homology domainsNature, 1996
- αLβ2 Integrin/LFA-1 Binding to ICAM-1 Induced by Cytohesin-1, a Cytoplasmic Regulatory MoleculeCell, 1996
- Phosphoinositide kinasesCurrent Opinion in Cell Biology, 1996
- The pleckstrin homology domain: An intriguing multifunctional protein moduleBioEssays, 1996
- Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domainCell, 1995
- Solution structure of a pleckstrin-homology domainNature, 1994