Linked Life Data

11031232

Source:http://linkedlifedata.com/resource/pubmed/id/11031232

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2001-1-16
pubmed:abstractText
The ezrin-radixin-moesin (ERM) family of proteins have emerged as key regulatory molecules in linking F-actin to specific membrane proteins, especially in cell surface structures. Merlin, the product of the NF2 tumor suppressor gene, has sequence similarity to ERM proteins and binds to some of the same membrane proteins, but lacks a C-terminal F-actin binding site. In this review we discuss how ERM proteins and merlin are negatively regulated by an intramolecular association between their N- and C-terminal domains. Activation of at least ERM proteins can be accomplished by C-terminal phosphorylation in the presence of PIP2. We also discuss membrane proteins to which ERM and merlin bind, including those making an indirect linkage through the PDZ-containing adaptor molecules EBP50 and E3KARP. Finally, the function of these proteins in cortical structure, endocytic traffic, signal transduction, and growth control is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1081-0706
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-43
pubmed:dateRevised
2006-9-29
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
ERM-Merlin and EBP50 protein families in plasma membrane organization and function.
pubmed:affiliation
Department of Molecular Biology and Genetics, Biotechnology Building, Cornell University, Ithaca, New York 14853, USA. apb5@cornell.edu
pubmed:publicationType
Journal Article, Review