Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-6-21
pubmed:abstractText
Phosphoinositides are important regulators of cellular homoeostasis and numerous signal-transduction pathways. One of their major features is their ability to recruit signalling proteins to membranes by direct interaction with phosphoinositide-binding modules. The distribution and dynamics of membrane phosphoinositides are therefore major determinants in the spatiotemporal control of cell signalling and membrane trafficking. However, standard biochemical approaches cannot reveal the dynamics of phosphoinositides at the single-cell level. A major technical advance has been the development of genetically encoded fluorescent phosphoinositide probes on the basis of the phosphoinositide-binding domains found in signalling proteins, such as the PH (pleckstrin homology) domain. This review describes the diverse fluorescent phosphoinositide probes available for imaging specific phosphoinositide species and how their use has improved the understanding of phosphoinositide signalling at the single-cell level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0248-4900
pubmed:author
pubmed:issnType
Print
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
501-18
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Imaging phosphoinositide dynamics using GFP-tagged protein domains.
pubmed:affiliation
Department of Physiology, University College London, Gower Street, London WC1E 6BT, UK. g.halet@ucl.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't