PMID- 25496009
OWN - NLM
STAT- MEDLINE
DCOM- 20151201
LR  - 20200930
IS  - 1551-4005 (Electronic)
IS  - 1538-4101 (Print)
IS  - 1551-4005 (Linking)
VI  - 14
IP  - 4
DP  - 2015
TI  - The Slx4-Dpb11 scaffold complex: coordinating the response to replication fork 
      stalling in S-phase and the subsequent mitosis.
PG  - 488-94
LID - 10.4161/15384101.2014.989126 [doi]
AB  - Replication fork stalling at DNA lesions is a common problem during the process 
      of DNA replication. One way to allow the bypass of these lesions is via specific 
      recombination-based mechanisms that involve switching of the replication template 
      to the sister chromatid. Inherent to these mechanisms is the formation of DNA 
      joint molecules (JMs) between sister chromatids. Such JMs need to be disentangled 
      before chromatid separation in mitosis and the activity of JM resolution enzymes, 
      which is under stringent cell cycle control, is therefore up-regulated in 
      mitosis. An additional layer of control is facilitated by scaffold proteins. In 
      budding yeast, specifically during mitosis, Slx4 and Dpb11 form a cell cycle 
      kinase-dependent complex with the Mus81-Mms4 structure-selective endonuclease, 
      which allows efficient JM resolution by Mus81. Furthermore, Slx4 and Dpb11 
      interact even prior to joining Mus81 and respond to replication fork stalling in 
      S-phase. This S-phase complex is involved in the regulation of the DNA damage 
      checkpoint as well as in early steps of template switch recombination. Similar 
      interactions and regulatory principles are found in human cells suggesting that 
      Slx4 and Dpb11 may have an evolutionary conserved role organizing the cellular 
      response to replication fork stalling.
FAU - Princz, Lissa N
AU  - Princz LN
AD  - a Max-Planck Institute of Biochemistry ; DNA Replication and Genome Integrity ; 
      Martinsried , Germany.
FAU - Gritenaite, Dalia
AU  - Gritenaite D
FAU - Pfander, Boris
AU  - Pfander B
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cell Cycle
JT  - Cell cycle (Georgetown, Tex.)
JID - 101137841
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Chromosomal Proteins, Non-Histone)
RN  - 0 (DPB11 protein, S cerevisiae)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 3.1.- (Endodeoxyribonucleases)
RN  - EC 3.1.- (SLX4 protein, S cerevisiae)
SB  - IM
MH  - Cell Cycle Checkpoints/*physiology
MH  - Cell Cycle Proteins/*metabolism
MH  - Chromosomal Proteins, Non-Histone/*metabolism
MH  - DNA Replication/*physiology
MH  - Endodeoxyribonucleases/*metabolism
MH  - Mitosis/*physiology
MH  - Models, Biological
MH  - Multiprotein Complexes/metabolism
MH  - Nuclear Matrix/physiology
MH  - S Phase/*physiology
MH  - Saccharomyces cerevisiae Proteins/*metabolism
MH  - Saccharomycetales
PMC - PMC4612105
OTO - NOTNLM
OT  - DNA damage response
OT  - cell cycle
OT  - homologous recombination
OT  - joint molecule resolution
OT  - post-replicative repair
EDAT- 2014/12/17 06:00
MHDA- 2015/12/15 06:00
PMCR- 2015/12/12
CRDT- 2014/12/16 06:00
PHST- 2014/12/16 06:00 [entrez]
PHST- 2014/12/17 06:00 [pubmed]
PHST- 2015/12/15 06:00 [medline]
PHST- 2015/12/12 00:00 [pmc-release]
AID - 989126 [pii]
AID - 10.4161/15384101.2014.989126 [doi]
PST - ppublish
SO  - Cell Cycle. 2015;14(4):488-94. doi: 10.4161/15384101.2014.989126.