The DOI matches its Crossref record; 144 of the 144 references it cites were found in a registry or an index.
Phospholipid-binding protein domains
Abstract
Research into cellular mechanisms for signal transduction is currently one of the most exciting and rapidly advancing fields of biological study. It has been known for some time that numerous intracellular signals are transmitted by specific protein-protein interactions, as exemplified by those involving the Src homology domains. However, after some controversy, it has recently been widely accepted that specific protein-phospholipid interactions also play key roles in many signal transduction pathways. In this review, landmark discoveries and recent advances describing protein domains known to associate with phospholipids are discussed. Particular emphasis is placed on the interactions of proteins with phospholipids acting as second messengers in signalling pathways. For this purpose, the pleckstrin homology (PH) domain is highlighted, since studies of this domain provided some of the earliest, detailed data about protein-phospholipid interactions occurring downstream of growth factor-mediated receptor stimulation. Moreover, studies of PH domains have given insight into the mechanisms of certain diseases, revealed a number of intriguing functional variations on a common structural theme and recently culminated in providing the missing links in erstwhile mysteries of phosphoinositide-dependent signal transduction pathways. Finally, a short discussion is devoted to the developing field of protein-phospholipid interactions that influence cytoskeletal organisation.
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“This phospholipid is thought to govern the distribution and function of a variety of cytoskeletal and signaling proteins that bear pleckstrin homology (PH) domains or lysine/arginine-rich hydrophobic motifs, which interact directly and specifically with the headgroup of 4,5-PIP2 (Bottomley et al. 1998; Hinchliffe et al. 1998; Martin 1998; Czech 2000).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Bottomley et al. 1998
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Metadata
- Authors
- Bottomley, M. J., Salim, K., & Panayotou, G.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Ludwig Cancer Research (GB)
- Corresponding author
- Panayotou, G.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
- Publisher
- Elsevier BV
- Published
- 1998-12
- Volume
- 1436
- Issue
- 1-2
- Pages
- 165-183
- ISSN
- 1388-1981 (ISSN-L)
- OpenAlex
- W1964359053
- Cited by
- 118
- References
- 144
- Citations by year
- 2025: 2 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 2 · 2013: 3 · 2012: 1
- FWCI
- 1.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- pleckstrin homology domain, signal transduction, second messengers, cytoskeletal organization, Src homology domains
- MeSH terms
- Carrier Proteins, Cell Membrane, Inositol Phosphates, Phosphatidylinositols, Phospholipids, Signal Transduction, src Homology Domains
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