Search engine for discovering works of Art, research articles, and books related to Art and Culture
ShareThis
Javascript must be enabled to continue!

Characterisation of a plant 3‐phosphoinositide‐dependent protein kinase‐1 homologue which contains a pleckstrin homology domain

View through CrossRef
A plant homologue of mammalian 3‐phosphoinositide‐dependent protein kinase‐1 (PDK1) has been identified in Arabidopsis and rice which displays 40% overall identity with human 3‐phosphoinositide‐dependent protein kinase‐1. Like the mammalian 3‐phosphoinositide‐dependent protein kinase‐1, Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 and rice 3‐phosphoinositide‐dependent protein kinase‐1 possess a kinase domain at N‐termini and a pleckstrin homology domain at their C‐termini. Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 can rescue lethality in Saccharomyces cerevisiae caused by disruption of the genes encoding yeast 3‐phosphoinositide‐dependent protein kinase‐1 homologues. Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P, PtdIns(3,4,5)P3 and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P. Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 is able to activate human protein kinase Bα (PKB/AKT) in the presence of PtdIns(3,4,5)P3. Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 is only the second plant protein reported to possess a pleckstrin homology domain and the first plant protein shown to bind 3‐phosphoinositides.
Title: Characterisation of a plant 3‐phosphoinositide‐dependent protein kinase‐1 homologue which contains a pleckstrin homology domain
Description:
A plant homologue of mammalian 3‐phosphoinositide‐dependent protein kinase‐1 (PDK1) has been identified in Arabidopsis and rice which displays 40% overall identity with human 3‐phosphoinositide‐dependent protein kinase‐1.
Like the mammalian 3‐phosphoinositide‐dependent protein kinase‐1, Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 and rice 3‐phosphoinositide‐dependent protein kinase‐1 possess a kinase domain at N‐termini and a pleckstrin homology domain at their C‐termini.
Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 can rescue lethality in Saccharomyces cerevisiae caused by disruption of the genes encoding yeast 3‐phosphoinositide‐dependent protein kinase‐1 homologues.
Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P, PtdIns(3,4,5)P3 and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P.
Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 is able to activate human protein kinase Bα (PKB/AKT) in the presence of PtdIns(3,4,5)P3.
Arabidopsis 3‐phosphoinositide‐dependent protein kinase‐1 is only the second plant protein reported to possess a pleckstrin homology domain and the first plant protein shown to bind 3‐phosphoinositides.

Related Results

Protein kinase activities in rat pancreatic islets of Langerhans
Protein kinase activities in rat pancreatic islets of Langerhans
1. Protein kinase activities in homogenates of rat islets of Langerhans were studied. 2. On incubation of homogenates with [gamma-32P]ATP, incorporation of 32P into protein occurre...
Cover Picture: Proteomics 17'09
Cover Picture: Proteomics 17'09
AbstractBlue on blueFew protein analysis techniques approach the resolution of, or the tedium of preparing for, large‐format 2‐D gel electrophoresis. Then you find the first dimens...
Reflexive homology
Reflexive homology
Reflexive homology is the homology theory associated to the reflexive crossed simplicial group; one of the fundamental crossed simplicial groups. It is the most general way to exte...
Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
The second messenger phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] is generated by the action of phosphoinositide 3-kinase (PI 3-kinase), and regulates a plethora of c...
Endothelial Protein C Receptor
Endothelial Protein C Receptor
IntroductionThe protein C anticoagulant pathway plays a critical role in the negative regulation of the blood clotting response. The pathway is triggered by thrombin, which allows ...
TPIP: a novel phosphoinositide 3-phosphatase
TPIP: a novel phosphoinositide 3-phosphatase
The PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor is a phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] 3-phosphatase that plays a cr...
PDK Enhances Ral-GEF Catalytic Activity
PDK Enhances Ral-GEF Catalytic Activity
Ral is a member of the Ras family of guanosine triphosphatases (GTPases). Ral is also a downstream target for Ras through interactions between Ras and Ral guanine exchange factors ...

Back to Top