Document Detail

Nucleolar localization signals of LIM kinase 2 function as a cell-penetrating peptide.
MedLine Citation:
PMID:  20937035     Owner:  NLM     Status:  MEDLINE    
LIM Kinase 2 (LIMK2) is a LIM domain-containing protein kinase which regulates actin polymerization thorough phosphorylation of the actin depolymerizing factor cofilin. It is also known to function as a shuttle between the cytoplasm and nucleus in endothelial cells. A basic amino acid-rich motif in LIMK2 was previously identified to be responsible for this shuttling function, as a nucleolar localization signal (NoLS). Here it is shown that this nucleolar localization signal sequence also has the characteristic function of a cell-penetrating peptide (CPP). We synthesized LIMK2 NoLS-conjugated peptides and a protein and analyzed their cell-penetrating abilities in various types of cells. The BC-box motif of the Von Hippel-Lindau (VHL) protein was used for the peptide. This motif previously has been reported to be involved in the neural differentiation of bone marrow stromal cells and skin-derived precursor cells. Green fluorescence protein (GFP) was used as a large biologically active biomolecule for the protein. The LIMK2 NoLS-conjugated peptides and protein translocated across the cell membranes of fibroblast cells, neural stem cells, and even iPS cells. These results suggest that LIMK2 NoLS acts as a cell-penetrating peptide and its cell-penetrating ability is not restricted by cell type. Moreover, from an in vivo assay using a mouse brain, it was confirmed that NoLS has potential for transporting biomolecules across the blood-brain barrier.
Nahoko Kobayashi; Mikio Niwa; Yang Hao; Tetsuhiko Yoshida
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Protein and peptide letters     Volume:  17     ISSN:  1875-5305     ISO Abbreviation:  Protein Pept. Lett.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-11-25     Completed Date:  2011-02-25     Revised Date:  2011-03-31    
Medline Journal Info:
Nlm Unique ID:  9441434     Medline TA:  Protein Pept Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1480-8     Citation Subset:  IM    
Institute for Advanced Sciences, Toagosei Co., Ltd., Tsukuba 300-2611, Japan.
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MeSH Terms
Amino Acid Sequence
Blood-Brain Barrier / metabolism
Cell Nucleolus / metabolism*
Cell-Penetrating Peptides / chemistry*
Cells, Cultured
Fibroblasts / metabolism
Infant, Newborn
Lim Kinases / chemistry*
Mice, Inbred C57BL
Molecular Sequence Data
Neural Stem Cells / metabolism
Nuclear Localization Signals / chemistry*
Nuclear Proteins / chemistry*,  metabolism
Recombinant Fusion Proteins / chemistry,  metabolism
Reg. No./Substance:
0/Cell-Penetrating Peptides; 0/Nuclear Localization Signals; 0/Nuclear Proteins; 0/Recombinant Fusion Proteins; EC Kinases

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