PMID- 10411507
OWN - NLM
STAT- MEDLINE
DCOM- 19990804
LR  - 20190619
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 285
IP  - 5426
DP  - 1999 Jul 16
TI  - Identification of a vertebrate sister-chromatid separation inhibitor involved in 
      transformation and tumorigenesis.
PG  - 418-22
AB  - A vertebrate securin (vSecurin) was identified on the basis of its biochemical
      analogy to the Pds1p protein of budding yeast and the Cut2p protein of fission
      yeast. The vSecurin protein bound to a vertebrate homolog of yeast separins Esp1p
      and Cut1p and was degraded by proteolysis mediated by an anaphase-promoting
      complex in a manner dependent on a destruction motif. Furthermore, expression of 
      a stable Xenopus securin mutant protein blocked sister-chromatid separation but
      did not block the embryonic cell cycle. The vSecurin proteins share extensive
      sequence similarity with each other but show no sequence similarity to either of 
      their yeast counterparts. Human securin is identical to the product of the gene
      called pituitary tumor-transforming gene (PTTG), which is overexpressed in some
      tumors and exhibits transforming activity in NIH 3T3 cells. The oncogenic nature 
      of increased expression of vSecurin may result from chromosome gain or loss,
      produced by errors in chromatid separation.
FAU - Zou, H
AU  - Zou H
AD  - Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, 
      MA 02115, USA.
FAU - McGarry, T J
AU  - McGarry TJ
FAU - Bernal, T
AU  - Bernal T
FAU - Kirschner, M W
AU  - Kirschner MW
LA  - eng
SI  - GENBANK/AF220426
GR  - GM26875/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (CCNB1 protein, human)
RN  - 0 (Ccnb1 protein, mouse)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Cut2 protein, S pombe)
RN  - 0 (Cyclin B)
RN  - 0 (Cyclin B1)
RN  - 0 (Fungal Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Oncogene Proteins)
RN  - 0 (PDS1 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Schizosaccharomyces pombe Proteins)
RN  - 0 (Securin)
RN  - 0 (pituitary tumor-transforming protein 1, human)
RN  - EC 2.3.2.23 (Ubiquitin-Protein Ligase Complexes)
RN  - EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 2.7.11.22 (CDC2 Protein Kinase)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.22.49 (Separase)
RN  - EC 6.- (Ligases)
SB  - IM
CIN - Science. 1999 Jul 16;285(5426):344-5. PMID: 10438298
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - *Anaphase
MH  - Anaphase-Promoting Complex-Cyclosome
MH  - Animals
MH  - CDC2 Protein Kinase/metabolism
MH  - Cell Cycle Proteins/chemistry/metabolism
MH  - *Cell Transformation, Neoplastic
MH  - Chromatids/*physiology
MH  - Conserved Sequence
MH  - Cyclin B/metabolism
MH  - Cyclin B1
MH  - *Endopeptidases
MH  - Fungal Proteins/chemistry/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Ligases/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Neoplasm Proteins/chemistry/genetics/*metabolism
MH  - Neoplasms/etiology
MH  - Nuclear Proteins/chemistry/metabolism
MH  - Oncogene Proteins/chemistry/genetics/*metabolism
MH  - Oncogenes
MH  - *Saccharomyces cerevisiae Proteins
MH  - *Schizosaccharomyces pombe Proteins
MH  - Securin
MH  - Separase
MH  - Spindle Apparatus/metabolism
MH  - *Ubiquitin-Protein Ligase Complexes
MH  - Ubiquitin-Protein Ligases
MH  - Xenopus
EDAT- 1999/07/20 00:00
MHDA- 1999/07/20 00:01
CRDT- 1999/07/20 00:00
PHST- 1999/07/20 00:00 [pubmed]
PHST- 1999/07/20 00:01 [medline]
PHST- 1999/07/20 00:00 [entrez]
AID - 7655 [pii]
AID - 10.1126/science.285.5426.418 [doi]
PST - ppublish
SO  - Science. 1999 Jul 16;285(5426):418-22. doi: 10.1126/science.285.5426.418.