Linked Life Data

9841908

Source:http://linkedlifedata.com/resource/pubmed/id/9841908

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-5-26
pubmed:abstractText
Lamellipodia, filopodia, microspikes and retraction fibers are characteristic features of a dynamic and continuously changing cell surface architecture and moesin, ezrin and radixin are thought to function in these microextensions as reversible links between plasma membrane proteins and actin microfilaments. Full-length and truncated domains of the three proteins were fused to green fluorescent protein (GFP), expressed in NIH3T3 cells, and distribution and behaviour of cells were analysed by using digitally enhanced differential interference contrast (DIC) and fluorescence video microscopy. The amino-terminal (N-)domains of all three proteins localize to the plasma membrane and fluorescence recordings parallel the dynamic changes in cell surface morphology observed by DIC microscopy of cultured cells. Expression of this domain, however, significantly affects cell surface architecture by the formation of abnormally long and fragile filopodia that poorly attach and retract abnormally. Even more striking are abundant irregular, branched and motionless membraneous structures that accumulate during retraction of lamellipodia. These are devoid of actin, endogenous moesin, ezrin and radixin, but contain the GFP-labeled domain. While a large proportion of endogenous proteins can be extracted with non-ionic detergents as in untransfected control cells, >90% of N-moesin and >60% of N-ezrin and N-radixin remain insoluble. The minimal size of the domain of moesin required for membrane localization and change in behavior includes residues 1-320. Deletions of amino acid residues from either end result in diffuse intracellular distribution, but also in normal cell behavior. Expression of GFP-fusions of full-length moesin or its carboxy-terminal domain has no effect on cell behavior during the observation period of 6-8 hours. The data suggest that, in the absence of the carboxy-terminal domain, N-moesin, -ezrin and -radixin interact tightly with the plasma membrane and interfere with normal functions of endogeneous proteins mainly during retraction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
112 ( Pt 1)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-25
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:9841908-3T3 Cells, pubmed-meshheading:9841908-Actin Cytoskeleton, pubmed-meshheading:9841908-Animals, pubmed-meshheading:9841908-Blood Proteins, pubmed-meshheading:9841908-Cell Adhesion, pubmed-meshheading:9841908-Cell Membrane, pubmed-meshheading:9841908-Cytoskeletal Proteins, pubmed-meshheading:9841908-Fibroblasts, pubmed-meshheading:9841908-Green Fluorescent Proteins, pubmed-meshheading:9841908-Image Processing, Computer-Assisted, pubmed-meshheading:9841908-Luminescent Proteins, pubmed-meshheading:9841908-Membrane Proteins, pubmed-meshheading:9841908-Mice, pubmed-meshheading:9841908-Microfilament Proteins, pubmed-meshheading:9841908-Microscopy, Fluorescence, pubmed-meshheading:9841908-Microscopy, Interference, pubmed-meshheading:9841908-Phosphoproteins, pubmed-meshheading:9841908-Recombinant Fusion Proteins, pubmed-meshheading:9841908-Subcellular Fractions, pubmed-meshheading:9841908-Transfection
pubmed:year
1999
pubmed:articleTitle
Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrin: in vivo imaging with GFP fusion proteins.
pubmed:affiliation
Molecular Mechanisms of Disease Laboratories, Department of Pathology, Stanford University Medical Center, Palo Alto, California 94304-5324, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't