Linked Life Data

16475184

Source:http://linkedlifedata.com/resource/pubmed/id/16475184

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-6-29
pubmed:abstractText
It is known that Fas death domain-associated protein (Daxx) possesses both putative nuclear and cytoplasmic functions. However, the nuclear transport mechanism is largely unknown. This study examined the nuclear location signal (NLS) of Daxx and whether the nuclear transport of Daxx was mediated by small ubiquitin-related modifier (SUMO). Two NLS motifs of Daxx, leucine (L)-rich nuclear export signal (NES)-like motif (188IXXLXXLLXL197) and C-terminal lysine (K) rich NLS2 (amino acids 627-634) motif, were identified and the K630 and K631 on the NLS2 motif were characterized as the major sumoylation sites of Daxx by in vitro sumoylation analysis. Proteins of inactive SUMO (SUMO-delta), a sumoylation-incompetent mutant, and Daxx NLS mutants (Daxx-NES(mut) and Daxx NLS2(mut)) were dispersed in cytoplasm. The cytoplasmic dispersed Daxx mutants could be relocalized to nucleus by cotransfection with active SUMO, but not with inactive SUMO-delta, demonstrating the role of SUMO on regulating the cytoplasmonuclear transport of Daxx. However, inactive SUMO-delta could also be relocalized to nucleus during cotransfection with wild-type Daxx, suggesting that SUMO regulation of the cytoplasmonuclear transport of its target protein Daxx does not need covalent modification. This study shows that cytoplasmic SUMO has a biological role in enhancing the cytoplasmonuclear transport of its target protein Daxx and it may be done through the non-sumoylation interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0730-2312
pubmed:author
pubmed:copyrightInfo
2006 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
895-911
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
SUMO regulates the cytoplasmonuclear transport of its target protein Daxx.
pubmed:affiliation
Center for Nanoscience, Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung, Taiwan. achen@mail.nsysu.edu.tw
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't