Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-4-1
pubmed:abstractText
Survivin is a member of the inhibitor of apoptosis (IAP) family of negative regulators of programmed cell death that is frequently overexpressed in human tumors. Survivin is not only involved in the regulation of apoptosis, but is also known to play a role in the control of cell cycle progression at the G2/M phase. Survivin is a predominantly cytoplasmic protein expressed in a cell cycle-dependent manner, but the mechanism(s) that determine its nuclear-cytoplasmic localization have not been described. In this study, we report that Survivin is a nuclear shuttling protein that is actively exported from the nucleus via the CRM1-dependent pathway. Nuclear export of Survivin is independent of the export of other shuttling proteins that control the G2/M phase transition, such as cyclin B1 and cdc25. The carboxy-terminal domain of Survivin is both necessary and sufficient for its nuclear export, although this region does not contain a functional leucine-rich nuclear export signal. Differences in the amino acid sequence of this region determine the dramatically different localization of Survivin (in the cytoplasm) and its splicing variant Survivin-DeltaEx3 (in the nucleus). The carboxy-terminal end of Survivin-DeltaEx3 contains a bipartite nuclear localization signal, not present in Survivin, which mediates its strong nuclear accumulation. These data suggest that active transport between the nucleus and cytoplasm may constitute an important regulatory mechanism for Survivin function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/BIRC5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/Inhibitor of Apoptosis Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins, http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/exportin 1 protein
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Elsevier Science (USA).
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
44-53
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11925104-Alternative Splicing, pubmed-meshheading:11925104-Amino Acid Sequence, pubmed-meshheading:11925104-Biological Transport, Active, pubmed-meshheading:11925104-Cell Compartmentation, pubmed-meshheading:11925104-Cell Cycle Proteins, pubmed-meshheading:11925104-Chromosomal Proteins, Non-Histone, pubmed-meshheading:11925104-Cytoplasm, pubmed-meshheading:11925104-Humans, pubmed-meshheading:11925104-Inhibitor of Apoptosis Proteins, pubmed-meshheading:11925104-Karyopherins, pubmed-meshheading:11925104-Microtubule-Associated Proteins, pubmed-meshheading:11925104-Neoplasm Proteins, pubmed-meshheading:11925104-Nuclear Proteins, pubmed-meshheading:11925104-Protein Isoforms, pubmed-meshheading:11925104-Protein Structure, Tertiary, pubmed-meshheading:11925104-Receptors, Cytoplasmic and Nuclear
pubmed:year
2002
pubmed:articleTitle
CRM1-mediated nuclear export determines the cytoplasmic localization of the antiapoptotic protein Survivin.
pubmed:affiliation
Department of Medical Oncology, VU University Medical Center, Amsterdam, HV1081, The Netherlands. ja.rodriguez@vumc.nl
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't