Arabidopsis COP1 protein specifically interacts in vitro with a cytoskeleton-associated protein, CIP1.

Matsui, Minami; Stoop, Chatanika; Arnim, Albrecht G. von; Wei, Ning; Deng, Xing‐Wang

doi:10.1073/pnas.92.10.4239

Cited by 71 publications

(53 citation statements)

References 22 publications

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“…However, it is equally plausible that the CLS of COP1 functions in cytoplasmic retention. Interestingly, the putative coiled-coil interaction surface between COP1 and CIP1, which is cytoplasmic and cytoskeleton associated (Matsui et al, 1995), overlaps with the CLS. It is conceivable that CIP1 plays a role in the cytoplasmic retention of COP1.…”

Section: Cop1 Reveals a Novel Clsmentioning

confidence: 99%

“…Dimerization of COP1 via its coiled-coil domain (Torii et al, 1998) may modulate the activity of the CLS or the NLS. Interaction of COP1 with the cytoplasmic CIP1 (Matsui et al, 1995) or the nuclear HY5 and CIP7 proteins Yamamoto et al, 1998) may also play a role. Future experiments will seek to resolve the significance of intramolecular and intermolecular interactions for the regulation of COP1 subcellular targeting.…”

Section: Interplay Between An Nls and A Cls Confers Light-responsivementioning

confidence: 99%

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Discrete Domains Mediate the Light-Responsive Nuclear and Cytoplasmic Localization of Arabidopsis COP1

Stacey¹,

Hicks²,

Arnim³

1999

The Plant Cell

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The Arabidopsis CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1) protein plays a critical role in the repression of photomorphogenesis during Arabidopsis seedling development. We investigated the control of COP1 partitioning between nucleus and cytoplasm, which has been implicated in the regulation of COP1 activity, by using fusion proteins between COP1 and ␤ -glucuronidase or the green fluorescent protein. Transient expression assays using onion epidermal cells and data from hypocotyl cells of stably transformed Arabidopsis demonstrated that COP1 carries a single, bipartite nuclear localization signal that functions independently of light. Nuclear exclusion was mediated by a novel and distinct signal, bordering the zinc-finger and coiled-coil motifs, that was able to redirect a heterologous nuclear protein to the cytoplasm. The cytoplasmic localization signal functioned in a light-independent manner. Light regulation of nuclear localization was reconstituted by combining the individual domains containing the nuclear localization signal and the cytoplasmic localization signal; the WD-40 repeat domain of COP1 was not required. However, phenotypic analysis of transgenic seedlings suggested that the constitutively nuclear-localized WD-40 repeat domain was able to mimic aspects of COP1 function, as indicated by exaggerated hypocotyl elongation under light conditions.

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Section: Cop1 Reveals a Novel Clsmentioning

confidence: 99%

Section: Interplay Between An Nls and A Cls Confers Light-responsivementioning

confidence: 99%

Discrete Domains Mediate the Light-Responsive Nuclear and Cytoplasmic Localization of Arabidopsis COP1

Stacey¹,

Hicks²,

Arnim³

1999

The Plant Cell

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“…COP1 is a RING-finger-type ubiquitin E3 ligase involved in ubiquitin-mediated proteolysis of photomorphogenesis-promoting factors, such as HY5 (Osterlund et al, 2000;Saijo et al, 2003), HYH (Holm et al, 2002), a MYB transcription factor, LONG AFTER FAR-RED LIGHT1 (Seo et al, 2003), and a bHLH transcription factor, LONG HY-POCOTYL IN FAR-RED1 (Duek et al, 2004;Jang et al, 2005;Yang et al, 2005). Other proteins have been identified that physically interact with COP1, including COP1-INTERACTING PROTEINs (Matsui et al, 1995;Yamamoto et al, 1998;Yamamoto et al, 2001), and several proteins with a zinc-binding B-box motif, namely CONSTANS (CO; Liu et al, 2008), CO-LIKE3 (COL3;Datta et al, 2006), SALT TOLERANCE (STO), and STO HOMOLOG1 (STH1; Holm et al, 2001). CO acts as a positive regulator of the floral transition in response to inductive photoperiods, whereas COL3 has been shown to act as a positive regulator of red light signaling (Putterill et al, 1995;Datta et al, 2006).…”

mentioning

confidence: 99%

BBX32, an Arabidopsis B-Box Protein, Functions in Light Signaling by Suppressing HY5-Regulated Gene Expression and Interacting with STH2/BBX21

et al. 2011

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A B-box zinc finger protein, B-BOX32 (BBX32), was identified as playing a role in determining hypocotyl length during a largescale functional genomics study in Arabidopsis (Arabidopsis thaliana). Further analysis revealed that seedlings overexpressing BBX32 display elongated hypocotyls in red, far-red, and blue light, along with reduced cotyledon expansion in red light. Through comparative analysis of mutant and overexpression line phenotypes, including global expression profiling and growth curve studies, we demonstrate that BBX32 acts antagonistically to ELONGATED HYPOCOTYL5 (HY5). We further show that BBX32 interacts with SALT TOLERANCE HOMOLOG2/BBX21, another B-box protein previously shown to interact with HY5. Based on these data, we propose that BBX32 functions downstream of multiple photoreceptors as a modulator of light responses. As such, BBX32 potentially has a native role in mediating gene repression to maintain dark adaptation.

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“…Recently, a cytoplasmic retention domain has been identified on the context of COP1 as CLS (Stacey et al 1999). In the search for COP1 interactive proteins, CIP1 protein was isolated and shown to be localized in the cytoplasm in an association of the cytoskeleton (Matsui et al 1995). CIP1 protein might be involved in the cytoplasmic retention of COP1.…”

Section: Cytosolic Retention Forcesmentioning

confidence: 99%

Protein nucleocytoplasmic transport and its light regulation in plants

Yamamoto

Deng

1999

Genes to Cells

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Light exerts a great influence on gene expression, physiology and development pattern in higher plants. Protein factors involved in these processes, such as the photoreceptor, phytochrome B, a key regulatory protein, COP1, and some bZIP transcription factors have been identified and their light-regulated movement between the cytoplasm and the nucleus has been demonstrated. These findings imply that nucleocytoplasmic transport plays a crucial role in light regulation in higher plants. This review summarizes recent investigations into plant nuclear transport systems and specific cases where nucleocytoplasmic transport is subject to light regulation.

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Arabidopsis COP1 protein specifically interacts in vitro with a cytoskeleton-associated protein, CIP1.

Cited by 71 publications

References 22 publications

Discrete Domains Mediate the Light-Responsive Nuclear and Cytoplasmic Localization of Arabidopsis COP1

Discrete Domains Mediate the Light-Responsive Nuclear and Cytoplasmic Localization of Arabidopsis COP1

BBX32, an Arabidopsis B-Box Protein, Functions in Light Signaling by Suppressing HY5-Regulated Gene Expression and Interacting with STH2/BBX21

Protein nucleocytoplasmic transport and its light regulation in plants

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