Linked Life Data

17047062

Source:http://linkedlifedata.com/resource/pubmed/id/17047062

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2006-10-18
pubmed:abstractText
Galectin-3 (Gal-3), a pleiotropic beta-galactoside-binding protein, was shown to be involved in several nuclear-dependent functions, including up-regulation of transcriptional factors, RNA processing, and cell cycle regulation. Gal-3 compartmentalization in the nucleus versus the cytoplasm affects, in part, the malignant phenotype of various cancers. However, to date, the mechanism by which Gal-3 translocates into the nucleus remains debatable. Thus, we have constructed and expressed a variety of fusion proteins containing deletion mutants of Gal-3 fused with monomers, dimers, and trimers of enhanced green fluorescent protein and searched for the Gal-3 sequence motifs essential for its nuclear localization in vivo. In addition, a digitonin-permeabilized, cell-free transport in vitro assay was used to directly examine the mechanism of Gal-3 nuclear import. Partial deletions of the COOH-terminal region (114-250) of the human Gal-3 significantly decreases its nuclear translocation, whereas a peptide (1-115) was transported to the nuclei. The in vitro nuclear import assay revealed that there are at least two independent nuclear pathways for shuttling Gal-3 into the nucleus: a passive diffusion and an active transport. This is the first article providing direct evidence for the nuclear import mechanisms of Gal-3 and suggests that Gal-3 nuclear translocation is governed by dual pathways, whereas the cytoplasmic/nuclear distribution may be regulated by multiple processes, including cytoplasmic anchorage, nuclear retention, and or nuclear export. These results may lead to the development of a therapeutic modality aiming at abrogating Gal-3 translocation into the nucleus and thus hampering its activity during cancer progression and metastasis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9995-10006
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed-meshheading:17047062-Active Transport, Cell Nucleus, pubmed-meshheading:17047062-Amino Acid Sequence, pubmed-meshheading:17047062-Animals, pubmed-meshheading:17047062-Antigens, Polyomavirus Transforming, pubmed-meshheading:17047062-Biological Transport, Active, pubmed-meshheading:17047062-Breast Neoplasms, pubmed-meshheading:17047062-COS Cells, pubmed-meshheading:17047062-Cell Line, Tumor, pubmed-meshheading:17047062-Cell Membrane Permeability, pubmed-meshheading:17047062-Cell Nucleus, pubmed-meshheading:17047062-Cercopithecus aethiops, pubmed-meshheading:17047062-Diffusion, pubmed-meshheading:17047062-Digitonin, pubmed-meshheading:17047062-Galectin 3, pubmed-meshheading:17047062-Green Fluorescent Proteins, pubmed-meshheading:17047062-HeLa Cells, pubmed-meshheading:17047062-Humans, pubmed-meshheading:17047062-Mutation, pubmed-meshheading:17047062-Recombinant Fusion Proteins, pubmed-meshheading:17047062-Structure-Activity Relationship, pubmed-meshheading:17047062-Subcellular Fractions, pubmed-meshheading:17047062-Transfection
pubmed:year
2006
pubmed:articleTitle
Characterization of the nuclear import pathways of galectin-3.
pubmed:affiliation
Tumor Progression and Metastasis Program, Karmanos Cancer Institute, Wayne State University, Detroit, Michigan 48201, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural