PMID- 21659603
OWN - NLM
STAT- MEDLINE
DCOM- 20110621
LR  - 20211203
IS  - 1095-9203 (Electronic)
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 332
IP  - 6035
DP  - 2011 Jun 10
TI  - A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting 
      protein required for ATR signaling.
PG  - 1313-7
LID - 10.1126/science.1203430 [doi]
AB  - The DNA damage response (DDR) is brought about by a protein kinase cascade that 
      orchestrates DNA repair through transcriptional and posttranslational mechanisms. 
      Cell cycle arrest is a hallmark of the DDR. We screened for cells that lacked 
      damage-induced cell cycle arrest and uncovered a critical role for Fanconi anemia 
      and homologous recombination proteins in ATR (ataxia telangiectasia and 
      Rad3-related) signaling. Three DDR candidates, the RNA processing protein INTS7, 
      the circadian transcription factor CLOCK, and a previously uncharacterized 
      protein RHINO, were recruited to sites of DNA damage. RHINO independently bound 
      the Rad9-Rad1-Hus1 complex (9-1-1) and the ATR activator TopBP1. RHINO was 
      recruited to sites of DNA damage by the 9-1-1 complex to promote Chk1 activation. 
      We suggest that RHINO functions together with the 9-1-1 complex and TopBP1 to 
      fully activate ATR.
FAU - Cotta-Ramusino, Cecilia
AU  - Cotta-Ramusino C
AD  - Department of Genetics, Harvard University Medical School, Howard Hughes Medical 
      Institute, Division of Genetics, Brigham and Women's Hospital, Boston, MA 02115, 
      USA.
FAU - McDonald, E Robert 3rd
AU  - McDonald ER 3rd
FAU - Hurov, Kristen
AU  - Hurov K
FAU - Sowa, Mathew E
AU  - Sowa ME
FAU - Harper, J Wade
AU  - Harper JW
FAU - Elledge, Stephen J
AU  - Elledge SJ
LA  - eng
GR  - R01 AG011085/AG/NIA NIH HHS/United States
GR  - R01 GM054137/GM/NIGMS NIH HHS/United States
GR  - R37 GM044664/GM/NIGMS NIH HHS/United States
GR  - HHMI/Howard Hughes Medical Institute/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (CXCL17 protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Chemokines)
RN  - 0 (Chemokines, CXC)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (HUS1 protein, human)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Nuclear Proteins)
RN  - 0 (RHNO1 protein, human)
RN  - 0 (TOPBP1 protein, human)
RN  - 139691-42-2 (rad9 protein)
RN  - EC 2.7.11.1 (ATR protein, human)
RN  - EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 3.1.- (Exonucleases)
RN  - EC 3.1.11.- (Rad1 protein, human)
SB  - IM
MH  - Ataxia Telangiectasia Mutated Proteins
MH  - Carrier Proteins/metabolism/*physiology
MH  - Cell Cycle/genetics
MH  - Cell Cycle Proteins/*metabolism
MH  - Cell Line, Tumor
MH  - Chemokines/genetics/*physiology
MH  - Chemokines, CXC
MH  - DNA Damage
MH  - *DNA Repair
MH  - DNA-Binding Proteins/metabolism
MH  - Exonucleases/metabolism
MH  - Humans
MH  - Multiprotein Complexes/metabolism
MH  - Nuclear Proteins/metabolism
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - *Signal Transduction
PMC - PMC4357496
MID - NIHMS403299
EDAT- 2011/06/11 06:00
MHDA- 2011/06/22 06:00
PMCR- 2015/03/12
CRDT- 2011/06/11 06:00
PHST- 2011/06/11 06:00 [entrez]
PHST- 2011/06/11 06:00 [pubmed]
PHST- 2011/06/22 06:00 [medline]
PHST- 2015/03/12 00:00 [pmc-release]
AID - 332/6035/1313 [pii]
AID - 10.1126/science.1203430 [doi]
PST - ppublish
SO  - Science. 2011 Jun 10;332(6035):1313-7. doi: 10.1126/science.1203430.