PMID- 12466024
OWN - NLM
STAT- MEDLINE
DCOM- 20030314
LR  - 20191210
IS  - 1471-2121 (Electronic)
IS  - 1471-2121 (Linking)
VI  - 3
DP  - 2002 Dec 4
TI  - An initial biochemical and cell biological characterization of the mammalian 
      homologue of a central plant developmental switch, COP1.
PG  - 30
AB  - BACKGROUND: Constitutive photomorphogenic 1 (COP1) has been defined as a central 
      regulator of photomorphogenic development in plants, which targets key 
      transcription factors for proteasome-dependent degradation. Although COP1 
      mammalian homologue has been previously reported, its function and distribution 
      in animal kingdom are not known. RESULTS: Here we report the characterization of 
      full-length human and mouse COP1 cDNAs and the genomic structures of the COP1 
      genes from several different species. Mammalian COP1 protein binds to 
      ubiquitinated proteins in vivo and is itself ubiquitinated. Furthermore, 
      mammalian COP1 is predominantly nuclear localized and exists primarily as a 
      complex of over 700 kDa. Through mutagenesis studies, we have defined a 
      leucine-rich nuclear export signal (NES) within the coiled-coil domain of 
      mammalian COP1 and a nuclear localization signal (NLS), which is composed of two 
      clusters of positive-charged amino acids, bridged by the RING finger. Disruption 
      of the RING finger structure abolishes the nuclear import, while deletion of the 
      entire RING finger restores the nuclear import. CONCLUSIONS: Our data suggest 
      that mammalian COP1, similar to its plant homologue, may play a role in 
      ubiquitination. Mammalian COP1 contains a classic leucine-rich NES and a novel 
      bipartite NLS bridged by a RING finger domain. We propose a working model in 
      which the COP1 RING finger functions as a structural scaffold to bring two 
      clusters of positive-charged residues within spatial proximity to mimic a 
      bipartite NLS. Therefore, in addition to its well-characterized role in 
      ubiquitination, the RING finger domain may also play a structural role in nuclear 
      import.
FAU - Yi, Chunling
AU  - Yi C
AD  - Department of Molecular, Cellular and Developmental Biology, Yale University, New 
      Haven, CT 06520-8104, USA. chunling.yi@yale.edu
FAU - Wang, Haiyang
AU  - Wang H
FAU - Wei, Ning
AU  - Wei N
FAU - Deng, Xing Wang
AU  - Deng XW
LA  - eng
SI  - GENBANK/BK000438
GR  - 1-F32-GM20540/GM/NIGMS NIH HHS/United States
GR  - GM61812/GM/NIGMS NIH HHS/United States
GR  - R01 GM047850/GM/NIGMS NIH HHS/United States
GR  - GM47850/GM/NIGMS NIH HHS/United States
GR  - R37 GM047850/GM/NIGMS NIH HHS/United States
GR  - F32 GM020540/GM/NIGMS NIH HHS/United States
GR  - R01 GM061812/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.
DEP - 20021204
PL  - England
TA  - BMC Cell Biol
JT  - BMC cell biology
JID - 100966972
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (Protein Sorting Signals)
RN  - 0 (Proteins)
RN  - 0 (Ubiquitin)
RN  - EC 2.3.2.27 (AT2G32950 protein, Arabidopsis)
RN  - EC 2.3.2.27 (COP1 protein, human)
RN  - EC 2.3.2.27 (COP1 protein, mouse)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Amino Acid Sequence/genetics
MH  - Animals
MH  - Arabidopsis Proteins/chemistry/genetics
MH  - Carrier Proteins/*chemistry/genetics
MH  - Cytoplasm/chemistry
MH  - DNA, Complementary/chemistry/genetics
MH  - Evolution, Molecular
MH  - Humans
MH  - Macromolecular Substances
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nuclear Envelope/chemistry
MH  - Nuclear Proteins/*chemistry/genetics
MH  - Nucleic Acid Conformation
MH  - Plant Proteins/chemistry/genetics
MH  - Protein Sorting Signals/genetics
MH  - Protein Structure, Quaternary/genetics
MH  - Proteins/*chemistry/genetics
MH  - *Sequence Homology, Nucleic Acid
MH  - Ubiquitin/metabolism
MH  - *Ubiquitin-Protein Ligases
PMC - PMC138799
EDAT- 2002/12/06 04:00
MHDA- 2003/03/15 04:00
PMCR- 2002/12/04
CRDT- 2002/12/06 04:00
PHST- 2002/09/11 00:00 [received]
PHST- 2002/12/04 00:00 [accepted]
PHST- 2002/12/06 04:00 [pubmed]
PHST- 2003/03/15 04:00 [medline]
PHST- 2002/12/06 04:00 [entrez]
PHST- 2002/12/04 00:00 [pmc-release]
AID - 1471-2121-3-30 [pii]
AID - 10.1186/1471-2121-3-30 [doi]
PST - ppublish
SO  - BMC Cell Biol. 2002 Dec 4;3:30. doi: 10.1186/1471-2121-3-30. Epub 2002 Dec 4.