Linked Life Data

19530175

Source:http://linkedlifedata.com/resource/pubmed/id/19530175

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2009-10-21
pubmed:abstractText
Short polypeptides from intermediate filament (IF) proteins containing one of the two IF-consensus motifs interfere severely with filament assembly in vitro. We now have systematically investigated a series of larger fragments of the muscle-specific IF protein desmin representing entire functional domains such as coil1 or coil 2. "Half molecules" comprising the amino-terminal portion of desmin, such as DesDeltaC240 and the "tagged" derivative Des(ESA)DeltaC244, assembled into large, roundish aggregates already at low ionic strength, DesDeltaC250 formed extended, relatively uniform filaments, whereas DesDeltaC265 and DesDeltaC300 were soluble under these conditions. Surprisingly, all mutant desmin fragments assembled very rapidly into long thick filaments or spacious aggregates when the ionic strength was raised to standard assembly conditions. In contrast, when these desmin mutants were assembled in the presence of wild-type (WT) desmin, their assembly properties were completely changed: The elongation of the two shorter desmin fragments was completely inhibited by WT desmin, whereas DesDeltaC250, DesDeltaC265 and DesDeltaC300 coassembled with desmin into filaments, but these mixed filaments were distinctly disturbed and exhibited a very different phenotype for each mutant. After transfection into fibroblasts and cardiomyocytes, the truncated mutant Des (ESA)DeltaC244 localized largely to the cytoplasm, as revealed by a tag-specific monoclonal antibody, and also partially colocalized there with the collapsed endogenous vimentin and desmin systems indicating its interference with IF-organizing processes. In contrast, in cells without an authentic cytoplasmic IF system such as line SW13, Des(ESA)DeltaC242 entered the nucleus and was deposited in small dot-like structures in chromatin-free spaces without any noticeable effect on nuclear morphology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1097-0169
pubmed:author
pubmed:copyrightInfo
(c) 2009 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
986-99
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Interference of amino-terminal desmin fragments with desmin filament formation.
pubmed:affiliation
Department of Cardiology, University of Heidelberg, Heidelberg, Germany. h.baer@dkfz.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't