Autophosphorylation ,plays a key role for CDK-activating kinases activity and complex formation in l
The Ee;CDKF;1, a leafy spurge (Euphorbia esula) CDK-activating kinase(CAK), shares 63% identity and 75% similarity with Arabidopsis CDK active kinase, CDKF (At;CDKF;1) .it has been proved that CDKF (At;CDKF;1) plays a major role in regulating cell division, cell elongation, and endo- reduplication. It is necessary to understand the function of Ee;CDKF;1 in leafy spurge.
In a previous study, Ying Jia.et al reported Ee;CDKF;1 were mutually responsible for intramolecular autophosphorylation and for phosphorylating CDK. What's more, the constitutive phosphorylation of Thr291 in vivo was verified. Here, they reported for the first time that Ee;CDKF;1 is critical for its phosphorylation capacity.
In this study, yeast two-hybrid system was used to test the possibility Protein–protein interaction of Ee; CDKF;1. YRG-2 harboring the combination of pAD-CDKF;1 and pBD-CDKF;1 grew well on all four types of SD plates indicated that full-length Ee;CDKF;1 interacted with another full length Ee;CDKF;1.Subsequent in GST-pull down experiment confirmed that the full-length Ee;CDKF;1 indeed interacted with Ee;CDKF;1 molecules.
The Gel exclusion chromatography and SDS PAGE illustrated that Ee;CDKF;1 could form homo protein complexes(Panobinostat).
They further discussed whether autophosphorylation have played an important function when Ee;CDKF;1 form complexes. Immunoblot and kinase analysis revealed that it is required for protein–protein interaction of Ee;CDKF;1. The mutant proteins were significant lower or even unable to form complex. Native PAGE analysis indicated that a mutation at the ATP-binding site or ATP-aligning site of Ee;CDKF;1 block protein complex formation.
However, There is no direct evidence indicating that AUY922 ;1 is the master regulator of this signal transduction pathway. It will be interesting to see the molecular mechanism of how Ee; CDKF;1 autophosphorylation fulfills its function in cell signal transduction.
References:
Ying Jia, James V. Andersonb ; Autophosphorylation is crucial for CDK-activating kinase (Ee;CDKF;1) activity and complex formation in leafy spurge ;Plant Science 180 (2011) 259–267;
Jone A. Stanley, JeHoon Lee. Chromium-VI arrests cell cycle and decreases granulosa cell proliferation by down-regulating cyclin-dependent kinases (CDK) and cyclins and up-regulating CDK-inhibitors. Reproductive Toxicology 32 (2011) 112– 123
Junaid M, Murthy RC, Saxena DK. Embryo- and fetotoxicity of chromium in pregestationally exposed mice. Bull Environ Contam Toxicol 1996;57:327–34.
Related posts:
http://www.cdkinhibitors.com/2011/09/cdkscyclin-dependent-kinase-and-cyclins_13.html
In a previous study, Ying Jia.et al reported Ee;CDKF;1 were mutually responsible for intramolecular autophosphorylation and for phosphorylating CDK. What's more, the constitutive phosphorylation of Thr291 in vivo was verified. Here, they reported for the first time that Ee;CDKF;1 is critical for its phosphorylation capacity.
In this study, yeast two-hybrid system was used to test the possibility Protein–protein interaction of Ee; CDKF;1. YRG-2 harboring the combination of pAD-CDKF;1 and pBD-CDKF;1 grew well on all four types of SD plates indicated that full-length Ee;CDKF;1 interacted with another full length Ee;CDKF;1.Subsequent in GST-pull down experiment confirmed that the full-length Ee;CDKF;1 indeed interacted with Ee;CDKF;1 molecules.
The Gel exclusion chromatography and SDS PAGE illustrated that Ee;CDKF;1 could form homo protein complexes(Panobinostat).
They further discussed whether autophosphorylation have played an important function when Ee;CDKF;1 form complexes. Immunoblot and kinase analysis revealed that it is required for protein–protein interaction of Ee;CDKF;1. The mutant proteins were significant lower or even unable to form complex. Native PAGE analysis indicated that a mutation at the ATP-binding site or ATP-aligning site of Ee;CDKF;1 block protein complex formation.
However, There is no direct evidence indicating that AUY922 ;1 is the master regulator of this signal transduction pathway. It will be interesting to see the molecular mechanism of how Ee; CDKF;1 autophosphorylation fulfills its function in cell signal transduction.
References:
Ying Jia, James V. Andersonb ; Autophosphorylation is crucial for CDK-activating kinase (Ee;CDKF;1) activity and complex formation in leafy spurge ;Plant Science 180 (2011) 259–267;
Jone A. Stanley, JeHoon Lee. Chromium-VI arrests cell cycle and decreases granulosa cell proliferation by down-regulating cyclin-dependent kinases (CDK) and cyclins and up-regulating CDK-inhibitors. Reproductive Toxicology 32 (2011) 112– 123
Junaid M, Murthy RC, Saxena DK. Embryo- and fetotoxicity of chromium in pregestationally exposed mice. Bull Environ Contam Toxicol 1996;57:327–34.
Related posts:
http://www.cdkinhibitors.com/2011/09/cdkscyclin-dependent-kinase-and-cyclins_13.html
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