FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dip, R.
Right arrow Articles by Naegeli, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dip, R.
Right arrow Articles by Naegeli, H.
(The FASEB Journal. 2005;19:704-715.)
© 2005 FASEB

More than just strand breaks: the recognition of structural DNA discontinuities by DNA-dependent protein kinase catalytic subunit

Ramiro Dip and Hanspeter Naegeli1

Institute of Veterinary Pharmacology and Toxicology, University of Zürich, Zürich, Switzerland

1 Correspondence: Institute of Veterinary Pharmacology and Toxicology, University of Zürich, Winterthurerstrasse 260, CH-8057 Zürich, Switzerland. E-mail: naegelih{at}vetpharm.unizh.ch

The DNA-dependent protein kinase (DNA-PK) is a trimeric factor originally identified as an enzyme that becomes activated upon incubation with DNA. Genetic defects in either the catalytic subunit (DNA-PKCS) or the two Ku components of DNA-PK result in immunodeficiency, radiosensitivity, and premature aging. This combined phenotype is generally attributed to the requirement for DNA-PK in the repair of DNA double strand breaks during various biological processes. However, recent studies revealed that DNA-PKCS, a member of the growing family of phosphatidylinositol 3-kinases, participates in signal transduction cascades related to apoptotic cell death, telomere maintenance and other pathways of genome surveillance. These manifold functions of DNA-PKCS have been associated with an increasing number of protein interaction partners and phosphorylation targets. Here we review the DNA binding properties of DNA-PKCS and highlight its ability to interact with an astounding diversity of nucleic acid substrates. This survey indicates that the large catalytic subunit of DNA-PK functions as a sensor of not only broken DNA molecules, but of a wider spectrum of aberrant, unusual, or specialized structures that interrupt the standard double helical conformation of DNA.—Dip, R., Naegeli, H. More than just strand breaks: the recognition of structural DNA discontinuities by DNA-dependent protein kinase catalytic subunit.


Key Words: genome • double strand break • DNA synthesis • eukaryote • DNA-PK




This article has been cited by other articles:


Home page
 J. Immunol.Home page
S. Yotsumoto, K. Saegusa, and Y. Aramaki
Endosomal Translocation of CpG-Oligodeoxynucleotides Inhibits DNA-PKcs-Dependent IL-10 Production in Macrophages
J. Immunol., January 15, 2008; 180(2): 809 - 816.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Drouet, P. Frit, C. Delteil, J.-P. de Villartay, B. Salles, and P. Calsou
Interplay between Ku, Artemis, and the DNA-dependent Protein Kinase Catalytic Subunit at DNA Ends
J. Biol. Chem., September 22, 2006; 281(38): 27784 - 27793.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Nabatiyan, D. Szuts, and T. Krude
Induction of CAF-1 Expression in Response to DNA Strand Breaks in Quiescent Human Cells.
Mol. Cell. Biol., March 1, 2006; 26(5): 1839 - 1849.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by The Federation of American Societies for Experimental Biology.