Phytochrome signalling is mediated through nucleoside diphosphate kinase 2

Choi, Giltsu; Yi, Hankuil; Lee, Jae-Ho; Kwon, Yong-Kook; Soh, Moon-Soo; Shin, Byongchul; Luka, Zigmund; Hahn, Tae‐Ryong; Song, Pill‐Soon

doi:10.1038/44176

Cited by 284 publications

(257 citation statements)

References 26 publications

Supporting

Mentioning

246

Contrasting

Unclassified

Order By: Relevance

“…More recently, a phytochrome-interacting molecule, NDPK2 (for nucleoside diphosphate kinase 2), has been reported to have a kinase activity and is involved in the response of both PhyA and PhyB. NDPK2-GFP fusion proteins are localized in both the nuclei and the cytoplasm (Choi et al, 1999). Considering the lightdependent subcellular partitioning of phytochrome and its possible interaction with those molecules in the cytoplasm or the nucleoplasm, phytochrome may have multiple sitespecific signaling mechanisms within the cell.…”

Section: Light-regulated Nuclear Import Of Phytochromesmentioning

confidence: 99%

Light-Induced Nuclear Translocation of Endogenous Pea Phytochrome A Visualized by Immunocytochemical Procedures

et al. 2000

View full text Add to dashboard Cite

Although the physiological functions of phytochrome A (PhyA) are now known, the distribution of endogenous PhyA has not been examined. We have visualized endogenous PhyA apoprotein (PHYA) by immunolabeling cryosections of pea tissue, using PHYA-deficient mutants as negative controls. By this method, we examined the distribution of PHYA in different tissues and changes in its intracellular distribution in response to light. In apical hook cells of etiolated seedlings, PHYA immunolabeling was distributed diffusely in the cytosol. Exposure to continuous far-red (cFR) light caused a redistribution of the immunolabeling to the nucleus, first detectable after 1.5 hr and greatest at 4.5 hr. During this time, the amounts of spectrally active phytochrome and PHYA did not decline substantially. Exposure to continuous red (cR) light or to a brief pulse of red light also resulted in redistribution of immunolabeling to the nucleus, but this occurred much more rapidly and with a different pattern of intranuclear distribution than it did in response to cFR light. Exposures to cR light resulted in loss of immunolabeling, which was associated with PHYA degradation. These results indicate that the light-induced intracellular location of PHYA is wavelength dependent and imply that this is important for PhyA activity. INTRODUCTIONThe phytochrome family of plant photoreceptors regulates various molecular and cellular processes of plant development in response to the light environment . Phytochromes are soluble chromoproteins that convert photoreversibly between two spectrally distinct forms when sequentially absorbing red (R) and far-red (FR) light, and this interconversion occurs immediately both in vivo and in vitro (Butler et al., 1959). Phytochromes are encoded by a small gene family (phytochrome genes PHYA to PHYE in Arabidopsis; Sharrock and Quail, 1989;Clack et al., 1994). Studies with mutants deficient in specific phytochromes have shown that phytochrome A (PhyA) and phytochrome B (PhyB) have distinct action spectra for the photoinduction of seed germination (Shinomura et al., 1996) and distinct fluence and wavelength requirements for expression of the chlorophyll a / b binding protein gene ( CAB ) (Hamazato et al., 1997). The fundamental molecular basis for these differences is of great interest but has not been elucidated. Recent genetic and molecular analyses have defined differences in PhyA and PhyB activities with respect to interacting factors and signaling intermediates. Those studies suggest that PhyA and PhyB signals are transduced by overlapping signal transduction pathways (Deng and Quail, 1999).To complement such approaches, one must also consider the ways in which the concentration, photochemical activity, and localization of each phytochrome are regulated in tissues and cells (Pratt, 1994). In tissues, this regulation may affect the transmission of the light signal from the site of photoperception to the responsive organ. An analysis of the way in which photoreceptors are redistributed within the cell in respon...

show abstract

Section: Light-regulated Nuclear Import Of Phytochromesmentioning

confidence: 99%

Light-Induced Nuclear Translocation of Endogenous Pea Phytochrome A Visualized by Immunocytochemical Procedures

et al. 2000

View full text Add to dashboard Cite

show abstract

“…Both phyA and phyB translocate to the nucleus in response to red or far-red light signals (Kircher et al, 1999;Yamaguchi et al, 1999). phyA or phyB have also been demonstrated to interact with PHYTO-CHROME INTERACTING FACTOR 3 (PIF3), PKS1, NPDK2, PIF4, ARR4, and ELF3 in vitro (Choi et al, 1999;Fankhauser et al, 1999;Ni et al, 1999;Liu et al, 2001;Sweere et al, 2001;Huq and Quail, 2002;Kim et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

HYPERSENSITIVE TO RED AND BLUE 1, a ZZ-Type Zinc Finger Protein, Regulates Phytochrome B–Mediated Red and Cryptochrome-Mediated Blue Light Responses

Kang

Chong

2005

Plant Cell

View full text Add to dashboard Cite

“…For example, in human erythrocytes dimers of nm23-H1 and of glyceraldehyde-3-phosphate dehydrogenase form a heterotetrameric complex that has Ser/Thr phosphotransferase activity (Engel et al, 1998). In Arabidopsis, interaction between phytochrome B and NDPK 2 has been shown to occur (Choi et al, 1999). Also commonly found but less studied is the interaction of NDPK with heat shock proteins.…”

mentioning

confidence: 99%

“…Besides this housekeeping function, recent reports have revealed the involvement of animal NDPKs in other vital processes such as control of cell proliferation (Cipollini et al, 1997), regulation of transcription (Postel et al, 1993;Ji et al, 1995), and protein phosphotransferase (Engel et al, 1998;Wagner and Vu, 2000). In plants, phytochrome B response (Choi et al, 1999), UV-B light signaling (Zimmermann et al, 1999), and hormone responses (Nato et al, 1997;Novikova et al, 1999) are among the processes in which NDPK isoforms have been shown to be involved.…”

mentioning

confidence: 99%

Heat Stress Response in Pea Involves Interaction of Mitochondrial Nucleoside Diphosphate Kinase with a Novel 86-Kilodalton Protein

et al. 2001

View full text Add to dashboard Cite

In this work we have further characterized the first mitochondrial nucleoside diphosphate kinase (mtNDPK) isolated from plants. The mitochondrial isoform was found to be especially abundant in reproductive and young tissues. Expression of the pea (Pisum sativum L. cv Oregon sugarpod) mtNDPK was not affected by different stress conditions. However, the pea mtNDPK was found to interact with a novel 86-kD protein, which is de novo synthesized in pea leaves upon exposure to heat. Thus, we have evidence for the involvement of mtNDPK in mitochondrial heat response in pea in vivo. Studies on oligomerization revealed that mtNDPK was found in complexes of various sizes, corresponding to the sizes of e.g. hexamers, tetramers, and dimers, indicating flexibility in oligomerization. This flexibility, also found for other NDPK isoforms, has been correlated with the ability of this enzyme to interact with other proteins. We believe that the mtNDPK is involved in heat stress response in pea, possibly as a modulator of the 86-kD protein.

show abstract

Phytochrome signalling is mediated through nucleoside diphosphate kinase 2

Cited by 284 publications

References 26 publications

Light-Induced Nuclear Translocation of Endogenous Pea Phytochrome A Visualized by Immunocytochemical Procedures

Light-Induced Nuclear Translocation of Endogenous Pea Phytochrome A Visualized by Immunocytochemical Procedures

HYPERSENSITIVE TO RED AND BLUE 1, a ZZ-Type Zinc Finger Protein, Regulates Phytochrome B–Mediated Red and Cryptochrome-Mediated Blue Light Responses

Heat Stress Response in Pea Involves Interaction of Mitochondrial Nucleoside Diphosphate Kinase with a Novel 86-Kilodalton Protein

Contact Info

Product

Resources

About