Regulation of C/N Interactions in Higher Plants by Protein Phosphorylation

1996 ◽  
pp. 87-112 ◽  
Author(s):  
Steven C. Huber ◽  
Werner M. Kaiser
Keyword(s):  
Protein Phosphorylation ◽  
Higher Plants

Regulation of phosphoenolpyruvate carboxylase: an example of signal transduction via protein phosphorylation in higher plants

1990 ◽  
Vol 30 ◽  
pp. 121-131 ◽  
Author(s):  
Hugh G. Nimmo ◽  
Pamela J. Carter ◽  
Charles A. Fewson ◽  
Gavin A.L. McNaughton ◽  
Gillian A. Nimmo ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Phosphorylation ◽  
Phosphoenolpyruvate Carboxylase ◽  
Higher Plants

scholarly journals Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems

2015 ◽  
Vol 43 (5) ◽  
pp. 966-974 ◽  
Author(s):  
Bibek Aryal ◽  
Christophe Laurent ◽  
Markus Geisler
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Abc Transporters ◽  
Higher Plants ◽  
Multi Drug Resistance ◽  
Protein Protein Interactions ◽  
Regulatory Domains ◽  
Transporter Family ◽  
Hsp 90 ◽  
Post Transcriptional Regulation

The ABC (ATP-binding cassette) transporter family in higher plants is highly expanded compared with those of mammalians. Moreover, some members of the plant ABC subfamily B (ABCB) display very high substrate specificity compared with their mammalian counterparts that are often associated with multi-drug resistance phenomena. In this review, we highlight prominent functions of plant and mammalian ABC transporters and summarize our knowledge on their post-transcriptional regulation with a focus on protein phosphorylation. A deeper comparison of regulatory events of human cystic fibrosis transmembrane conductance regulator (CFTR) and ABCB1 from the model plant Arabidopsis reveals a surprisingly high degree of similarity. Both physically interact with orthologues of the FK506-binding proteins that chaperon both transporters to the plasma membrane in an action that seems to involve heat shock protein (Hsp)90. Further, both transporters are phosphorylated at regulatory domains that connect both nt-binding folds. Taken together, it appears that ABC transporters exhibit an evolutionary conserved but complex regulation by protein phosphorylation, which apparently is, at least in some cases, tightly connected with protein–protein interactions (PPI).

scholarly journals Protein phosphorylation in intact cultured sycamore (Acer pseudoplatanus) cells and its response to fusicoccin

1986 ◽  
Vol 235 (1) ◽  
pp. 45-48 ◽  
Author(s):  
L Tognoli ◽  
R Colombo
Keyword(s):  
Protein Phosphorylation ◽  
Molecular Mass ◽  
Cultured Cells ◽  
Higher Plants ◽  
Acer Pseudoplatanus ◽  
Cell Fractionation ◽  
Soluble Fractions

Fusicoccin (FC), a natural diterpene glucoside able to stimulate electrogenic H+ extrusion in higher plants, has been shown to stimulate the phosphorylation of a polypeptide of molecular mass approx. 33 kDa in intact cultured cells of sycamore (Acer pseudoplatanus). The effect is specific, rapid and insensitive to cycloheximide. The presence of the 33 kDa polypeptide and the stimulation by FC have been observed in SDS-containing cell homogenates and in the microsomal and soluble fractions after cell fractionation.

The control of glycolysis and gluconeogenesis by protein phosphorylation

1983 ◽  
Vol 302 (1108) ◽  
pp. 27-32 ◽  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Physicochemical Properties ◽  
Protein Phosphorylation ◽  
Higher Plants ◽  
Dependent Protein Kinase ◽  
Potent Stimulator ◽  
Dependent Protein

Fructose 2,6-bisphosphate has been discovered as a potent stimulator of liver phosphofructokinase. It is also an inhibitor of fructose 1,6-biphosphatase and a stimulator of PP i : fructose 6-phosphate phosphotransferase from higher plants. It is formed from fructose 6-phosphate and ATP by a 6-phosphofructo 2-kinase and hydrolysed by a fructose 2,6-bisphosphatase. These two enzymes have very similar physicochemical properties and could not be separated from each other. They are substrates for cyclic-AMP-dependent protein kinase, which inactivates the first enzyme and activates the second.

scholarly journals Correction: Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems

2016 ◽  
Vol 44 (2) ◽  
pp. 663-673 ◽  
Author(s):  
Bibek Aryal ◽  
Christophe Laurent ◽  
Markus Geisler
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Abc Transporters ◽  
Higher Plants ◽  
Protein Protein Interactions ◽  
Regulatory Domains ◽  
Transporter Family ◽  
Fk506 Binding Proteins ◽  
Post Transcriptional Regulation ◽  
High Degree

The ABC (ATP-binding cassette) transporter family in higher plants is highly expanded compared with those of mammalians. Moreover, some members of the plant ABCB subfamily display very high substrate specificity compared with their mammalian counterparts that are often associated with multidrug resistance (MDR) phenomena. In this review we highlight prominent functions of plant and mammalian ABC transporters and summarize our knowledge on their post-transcriptional regulation with a focus on protein phosphorylation. A deeper comparison of regulatory events of human cystic fibrosis transmembrane conductance regulator (CFTR) and ABCB1 from the model plant Arabidopsis reveals a surprisingly high degree of similarity. Both physically interact with orthologues of the FK506-binding proteins (FKBPs) that chaperon both transporters to the plasma membrane in an action that seems to involve Hsp90. Further both transporters are phosphorylated at regulatory domains that connect both nucleotide-binding folds. Taken together it appears that ABC transporters exhibit an evolutionary conserved but complex regulation by protein phosphorylation, which apparently is, at least in some cases, tightly connected with protein–protein interactions (PPI).

In vitro and in vivo polysaccharides assembly: ultrastructural and cytochemical study of growing plant cell wall components.

1978 ◽  
Vol 36 (2) ◽  
pp. 434-435
Author(s):  
D. Reis ◽  
B. Vian ◽  
J. C. Roland
Keyword(s):  
Cell Wall ◽  
Self Assembly ◽  
Plant Cell Wall ◽  
Higher Plants ◽  
Three Dimensional ◽  
Cytochemical Study ◽  
Wall Components

Wall morphogenesis in higher plants is a problem still open to controversy. Until now the possibility of a transmembrane control and the involvement of microtubules were mostly envisaged. Self-assembly processes have been observed in the case of walls of Chlamydomonas and bacteria. Spontaneous gelling interactions between xanthan and galactomannan from Ceratonia have been analyzed very recently. The present work provides indications that some processes of spontaneous aggregation could occur in higher plants during the formation and expansion of cell wall.Observations were performed on hypocotyl of mung bean (Phaseolus aureus) for which growth characteristics and wall composition have been previously defined.In situ, the walls of actively growing cells (primary walls) show an ordered three-dimensional organization (fig. 1). The wall is typically polylamellate with multifibrillar layers alternately transverse and longitudinal. Between these layers intermediate strata exist in which the orientation of microfibrils progressively rotates. Thus a progressive change in the morphogenetic activity occurs.

Localization of Adenosine Triphosphatase Activity in the Phleom of Nicotiana Tabacum

1972 ◽  
Vol 30 ◽  
pp. 230-231
Author(s):  
James Cronshaw ◽  
Jamison E. Gilder
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Higher Plants ◽  
High Surface ◽  
Root Tip ◽  
Animal Cells ◽  
Physiological Processes ◽  
Tip Cells ◽  
Atpase Localization

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.

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