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The PH domain: a common piece in the structural patchwork of signalling proteins
A Musacchio1, T Gibson, P Rice
1European Molecular Biology Laboratory, Heidelberg, Germany.
Trends in Biochemical Sciences
|September 1, 1993
Summary
The pleckstrin homology (PH) domain, a module in signaling proteins, is found in various kinases and GTP-binding proteins. This review identifies new PH domain proteins, suggesting their role in protein interactions.
Area of Science:
- Molecular Biology
- Cell Signaling
Background:
- The pleckstrin homology (PH) domain is a conserved protein module.
- PH domains are increasingly recognized as important in cellular signaling pathways.
Purpose of the Study:
- To identify novel proteins containing pleckstrin homology (PH) domains.
- To explore the potential role of PH domains in protein-protein interactions, particularly with GTP-binding proteins.
Main Methods:
- Extensive database searches using profile search methods.
- Bioinformatic analysis to identify conserved PH domain sequences.
Main Results:
- Identified numerous additional proteins containing PH domains.
- PH domains are prevalent in kinases, phospholipase C isoforms, GTPases, and related factors.
- A PH domain in beta-adrenergic receptor kinase was found in a G protein interaction region.
Conclusions:
- PH domains are widespread in signaling proteins.
- PH domains likely play a significant role in mediating interactions with GTP-binding proteins.