Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2005-11-21
pubmed:abstractText
The COP1 (constitutive photomorphogenic 1) protein, comprising RING finger, coiled-coil and WD40 domains, is conserved in both higher plants and vertebrates. In plants, COP1 acts as an E3 ubiquitin ligase to repress light signaling by targeting photoreceptors and downstream transcription factors for ubiquitylation and degradation. The activity of COP1 in plant cells correlates with its cytoplasmic and nuclear partitioning according to dark or light conditions. In addition, various signaling molecules have been shown to directly interact with COP1 and modulate its activity. Recently, scientists have begun to probe the function and regulation of COP1 in mammalian systems. Initial studies have pointed at possible roles for mammalian COP1 in tumorigenesis and the stress response through regulating the activities of p53 and c-Jun.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0962-8924
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
618-25
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
COP1 - from plant photomorphogenesis to mammalian tumorigenesis.
pubmed:affiliation
Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, N.I.H., Extramural