Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
- PMID: 8072546
- DOI: 10.1038/371168a0
Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
Abstract
The pleckstrin homology (PH) domain is a new protein module of around 100 amino acids found in several proteins involved in signal transduction. Although its specific function has yet to be elucidated, the carboxy-terminal regions of many PH domains bind to the beta gamma subunits of G proteins. On the basis of structural similarities between PH domains and lipid-binding proteins, we have proposed that PH domains may be binding to lipophilic molecules. Indeed, many of the proteins that contain this domain associate with phospholipid membranes, and disruption of this domain can interfere with membrane association. Here we report that PH domains bind to phosphatidylinositol-4,5-bisphosphate and show that the lipid-binding site is located at the lip of the beta-barrel. This suggests that PH domains may be important for membrane localization of proteins through interactions with phosphatidylinositol-4,5-bisphosphate.
Similar articles
-
Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin.Structure. 2005 Feb;13(2):277-86. doi: 10.1016/j.str.2004.11.012. Structure. 2005. PMID: 15698571
-
Enigmatic relationship of Pleckstrin homology domain with phospholipid breakdown mediated signal transduction.Indian J Exp Biol. 1999 Jan;37(1):1-5. Indian J Exp Biol. 1999. PMID: 10355358 Review.
-
The solution structure of the pleckstrin homology domain of mouse Son-of-sevenless 1 (mSos1).J Mol Biol. 1997 Jun 20;269(4):579-91. doi: 10.1006/jmbi.1997.1041. J Mol Biol. 1997. PMID: 9217262
-
Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity.J Mol Biol. 1996 Jan 12;255(1):14-21. doi: 10.1006/jmbi.1996.0002. J Mol Biol. 1996. PMID: 8568861
-
Pleckstrin homology (PH) domains in signal transduction.J Cell Biochem. 1994 Dec;56(4):436-43. doi: 10.1002/jcb.240560403. J Cell Biochem. 1994. PMID: 7890802 Review.
Cited by
-
Defects in integrin complex formation promote CHKB-mediated muscular dystrophy.Life Sci Alliance. 2024 May 15;7(8):e202301956. doi: 10.26508/lsa.202301956. Print 2024 Aug. Life Sci Alliance. 2024. PMID: 38749543 Free PMC article.
-
Spontaneous signal generation by an excitable system for cell migration.Front Cell Dev Biol. 2024 Feb 28;12:1373609. doi: 10.3389/fcell.2024.1373609. eCollection 2024. Front Cell Dev Biol. 2024. PMID: 38481533 Free PMC article. Review.
-
GRAF1 Acts as a Downstream Mediator of Parkin to Regulate Mitophagy in Cardiomyocytes.Cells. 2024 Mar 4;13(5):448. doi: 10.3390/cells13050448. Cells. 2024. PMID: 38474413 Free PMC article.
-
Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA.Viruses. 2023 Dec 12;15(12):2413. doi: 10.3390/v15122413. Viruses. 2023. PMID: 38140654 Free PMC article. Review.
-
Targeting phosphoinositide signaling in cancer: relevant techniques to study lipids and novel avenues for therapeutic intervention.Front Cell Dev Biol. 2023 Oct 25;11:1297355. doi: 10.3389/fcell.2023.1297355. eCollection 2023. Front Cell Dev Biol. 2023. PMID: 37954209 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources