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. |