PMID- 17218258
OWN - NLM
STAT- MEDLINE
DCOM- 20070212
LR  - 20231213
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 128
IP  - 1
DP  - 2007 Jan 12
TI  - PICH, a centromere-associated SNF2 family ATPase, is regulated by Plk1 and 
      required for the spindle checkpoint.
PG  - 101-14
AB  - We identify PICH (Plk1-interacting checkpoint "helicase"), a member of the SNF2 
      ATPase family, as an interaction partner and substrate of Plk1. Following 
      phosphorylation of PICH on the Cdk1 site T1063, Plk1 is recruited to PICH and 
      controls its localization. Starting in prometaphase, PICH accumulates at 
      kinetochores and inner centromeres. Moreover, it decorates threads that form 
      during metaphase before increasing in length and progressively diminishing during 
      anaphase. PICH-positive threads connect sister kinetochores and are dependent on 
      tension, sensitive to DNase, and exacerbated in response to premature loss of 
      cohesins or inhibition of topoisomerase II, suggesting that they represent 
      stretched centromeric chromatin. Depletion of PICH causes the selective loss of 
      Mad2 from kinetochores and completely abrogates the spindle checkpoint, resulting 
      in massive chromosome missegregation. These data identify PICH as a novel 
      essential component of checkpoint signaling. We propose that PICH binds to 
      catenated centromere-related DNA to monitor tension developing between sister 
      kinetochores.
FAU - Baumann, Christoph
AU  - Baumann C
AD  - Department of Cell Biology, Max Planck Institute of Biochemistry, D-82152 
      Martinsried, Germany.
FAU - Korner, Roman
AU  - Korner R
FAU - Hofmann, Kay
AU  - Hofmann K
FAU - Nigg, Erich A
AU  - Nigg EA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (MAD2L1 protein, human)
RN  - 0 (Mad2 Proteins)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Repressor Proteins)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 3.6.4.- (DNA Helicases)
RN  - EC 3.6.4.12 (ERCC6L protein, human)
RN  - EC 5.99.1.3 (DNA Topoisomerases, Type II)
SB  - IM
CIN - Cell. 2007 Jan 12;128(1):20-1. doi: 10.1016/j.cell.2006.12.022. PMID: 17218250
MH  - Amino Acid Sequence
MH  - Calcium-Binding Proteins/metabolism
MH  - Cell Cycle Proteins/*metabolism
MH  - Centromere/*metabolism
MH  - DNA Helicases/chemistry/deficiency/*metabolism
MH  - DNA Topoisomerases, Type II/metabolism
MH  - DNA-Binding Proteins/chemistry/deficiency/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Kinetochores/metabolism
MH  - Mad2 Proteins
MH  - Mitosis
MH  - Models, Biological
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Protein Structure, Tertiary
MH  - Protein Transport
MH  - Proto-Oncogene Proteins/*metabolism
MH  - Repressor Proteins/metabolism
MH  - Signal Transduction
MH  - Spindle Apparatus/*metabolism
MH  - Substrate Specificity
MH  - Polo-Like Kinase 1
EDAT- 2007/01/16 09:00
MHDA- 2007/02/13 09:00
CRDT- 2007/01/16 09:00
PHST- 2006/06/07 00:00 [received]
PHST- 2006/09/06 00:00 [revised]
PHST- 2006/11/02 00:00 [accepted]
PHST- 2007/01/16 09:00 [pubmed]
PHST- 2007/02/13 09:00 [medline]
PHST- 2007/01/16 09:00 [entrez]
AID - S0092-8674(06)01551-0 [pii]
AID - 10.1016/j.cell.2006.11.041 [doi]
PST - ppublish
SO  - Cell. 2007 Jan 12;128(1):101-14. doi: 10.1016/j.cell.2006.11.041.