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Publication : Evidence for functional conservation of a mammalian homologue of the light-responsive plant protein COP1.

First Author  Wang H Year  1999
Journal  Curr Biol Volume  9
Issue  13 Pages  711-4
PubMed ID  10395541 Mgi Jnum  J:56261
Mgi Id  MGI:1340709 Doi  10.1016/s0960-9822(99)80314-5
Citation  Wang H, et al. (1999) Evidence for functional conservation of a mammalian homologue of the light-responsive plant protein COP1. Curr Biol 9(13):711-4
abstractText  Identified in Arabidopsis as a repressor of light-regulated development, the COP1 (constitutively photomorphogenic 1) protein is characterized by a RING-finger motif and a WD40 repeat domain [1]. The subcellular localization of COP1 is light-dependent. COP1 acts within the nucleus to repress photomorphogenic development, but light inactivates COP1 and diminishes its nuclear abundance [2]. Here, we report the identification of a mammalian COP1 homologue that contains all the structural features present in Arabidopsis COP1 (AtCOP1). When expressed in plant cells, a fusion protein comprising mammalian COP1 and beta-glucuronidase (GUS) responded to light by changing its subcellular localization pattern in a manner similar to AtCOP1. Whereas the mammalian COP1 was unable to rescue the defects of Arabidopsis cop1 mutants, expression of the amino-terminal half of mammalian COP1 in Arabidopsis interfered with endogenous COP1 function, resulting in a hyperphotomorphogenic phenotype. Therefore, the regulatory modules in COP1 proteins that are responsible for the signal-dependent subcellular localization are functionally conserved between higher plants and mammals, suggesting that mammalian COP1 may share a common mode of action with its plant counterpart in regulating development and cellular signaling.
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