A 67-kDa plasma-membrane-bound Ca 2+ -stimulated protein kinase active in sink tissue of higher plants

Planta ◽  
1998 ◽  
Vol 205 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Laurence D. P. Barker ◽  
Matthew D. Templeton ◽  
Ian B. Ferguson
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Higher Plants ◽  
Membrane Bound ◽  
Sink Tissue

scholarly journals Lipid-dependent Akt-ivity: where, when, and how

2019 ◽  
Vol 47 (3) ◽  
pp. 897-908 ◽  
Author(s):  
Katharina M. Siess ◽  
Thomas A. Leonard
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Kinase Domain ◽  
Target Of Rapamycin ◽  
Endomembrane System ◽  
Essential Protein ◽  
Mechanistic Target Of Rapamycin ◽  
Subcellular Compartments ◽  
Membrane Bound ◽  
Phosphoinositide 3 Kinase

Abstract Akt is an essential protein kinase activated downstream of phosphoinositide 3-kinase and frequently hyperactivated in cancer. Canonically, Akt is activated by phosphoinositide-dependent kinase 1 and mechanistic target of rapamycin complex 2, which phosphorylate it on two regulatory residues in its kinase domain upon targeting of Akt to the plasma membrane by PI(3,4,5)P3. Recent evidence, however, has shown that, in addition to phosphorylation, Akt activity is allosterically coupled to the engagement of PI(3,4,5)P3 or PI(3,4)P2 in cellular membranes. Furthermore, the active membrane-bound conformation of Akt is protected from dephosphorylation, and Akt inactivation by phosphatases is rate-limited by its dissociation. Thus, Akt activity is restricted to membranes containing either PI(3,4,5)P3 or PI(3,4)P2. While PI(3,4,5)P3 has long been associated with signaling at the plasma membrane, PI(3,4)P2 is gaining increasing traction as a signaling lipid and has been implicated in controlling Akt activity throughout the endomembrane system. This has clear implications for the phosphorylation of both freely diffusible substrates and those localized to discrete subcellular compartments.

Isolation of plasma-membrane-bound calcium/calmodulin-regulated protein kinase from pea using Western blotting

Planta ◽  
1985 ◽  
Vol 166 (2) ◽  
pp. 208-215 ◽  
Author(s):  
D. P. Blowers ◽  
A. Hetherington ◽  
A. Trewavas
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Western Blotting ◽  
Membrane Bound

scholarly journals Structure, organization, and functions of cellulose synthase complexes in higher plants

2007 ◽  
Vol 19 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Reginaldo A. Festucci-Buselli ◽  
Wagner C. Otoni ◽  
Chandrashekhar P. Joshi
Keyword(s):  
Cell Wall ◽  
Hydrogen Bonding ◽  
Plasma Membrane ◽  
Functional Organization ◽  
Higher Plants ◽  
Cellulose Synthase ◽  
Great Stability ◽  
Close Proximity ◽  
Cell Wall Polymers ◽  
Membrane Bound

Annually, plants produce about 180 billion tons of cellulose making it the largest reservoir of organic carbon on Earth. Cellulose is a linear homopolymer of beta(1-4)-linked glucose residues. The coordinated synthesis of glucose chains is orchestrated by specific plasma membrane-bound cellulose synthase complexes (CelS). The CelS is postulated to be composed of approximately 36 cellulose synthase (CESA) subunits. The CelS synthesizes 36 glucose chains in close proximity before they are further organized into microfibrils that are further associated with other cell wall polymers. The 36 glucose chains in a microfibril are stabilized by intra- and inter-hydrogen bonding which confer great stability on microfibrils. Several elementary microfibrils come together to form macrofibrils. Many CESA isoforms appear to be involved in the cellulose biosynthetic process and at least three types of CESA isoforms appear to be necessary for the functional organization of CelS in higher plants.

scholarly journals The plant calcium-dependent protein kinase CPK3 phosphorylates REM1.3 to restrict viral infection

2017 ◽  
Author(s):  
Artemis Perraki ◽  
Julien Gronnier ◽  
Paul Gouguet ◽  
Marie Boudsocq ◽  
Anne-Flore Deroubaix ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Cell Movement ◽  
Dependent Protein Kinase ◽  
Calcium Dependent ◽  
Intrinsically Disordered ◽  
Dependent Protein ◽  
Membrane Bound ◽  
Calcium Dependent Protein Kinase ◽  
Group 1

AbstractPlants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3-s phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.

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