Linked Life Data

18491048

Source:http://linkedlifedata.com/resource/pubmed/id/18491048

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
186
pubmed:dateCreated
2008-5-20
pubmed:abstractText
The actin cytoskeleton is required for many important processes during embryonic development. In later stages of life, important homeostatic processes depend on the actin cytoskeleton, such as immune response, haemostasis and blood vessel preservation. Therefore, the function of the actin cytoskeleton must be tightly regulated, and aberrant regulation may cause disease. A growing number of proteins have been described to bind and regulate the actin cytoskeleton. Amongst them, Ena/VASP proteins function as anti-capping proteins, thereby directly modulating the actin ultrastructure. Ena/VASP function is regulated by their recruitment into protein complexes downstream of plasma membrane receptors and by phosphorylation. As regulators of the actin ultrastructure, Ena/VASP proteins are involved in crucial cellular functions, such as shape change, adhesion, migration and cell-cell interaction and hence are important targets for therapeutic intervention. In this chapter, we will first describe the structure, function and regulation of Ena/VASP proteins. Then, we will review the involvement of Ena/VASP proteins in the development of human diseases. Growing evidence links Ena/VASP proteins to important human diseases, such as thrombosis, cancer, arteriosclerosis, cardiomyopathy and nephritis. Finally, present and future perspectives for the development of therapeutic molecules interfering with Ena/VASP-mediated protein-protein interactions are presented.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0171-2004
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-65
pubmed:dateRevised
2011-3-30
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Role of Ena/VASP proteins in homeostasis and disease.
pubmed:affiliation
Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London, UK.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't