scholarly journals Light Activation of Maize Phosphoenolpyruvate Carboxylase Protein-Serine Kinase Activity Is Inhibited by Mesophyll and Bundle Sheath-Directed Photosynthesis Inhibitors

1992 ◽  
Vol 98 (1) ◽  
pp. 152-156 ◽  
Author(s):  
Jin-an Jiao ◽  
Raymond Chollet
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Kinase Activity ◽  
Bundle Sheath ◽  
Light Activation ◽  
Serine Kinase

Factors involved in the rise of phosphoenolpyruvate carboxylase-kinase activity caused by salinity in sorghum leaves

Planta ◽  
2013 ◽  
Vol 237 (5) ◽  
pp. 1401-1413 ◽  
Author(s):  
José A. Monreal ◽  
Cirenia Arias-Baldrich ◽  
Francisco Pérez-Montaño ◽  
Jacinto Gandullo ◽  
Cristina Echevarría ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Kinase Activity ◽  
Phosphoenolpyruvate Carboxylase Kinase

scholarly journals Activation of the c-abl oncogene by viral transduction or chromosomal translocation generates altered c-abl proteins with similar in vitro kinase properties.

1985 ◽  
Vol 5 (1) ◽  
pp. 204-213 ◽  
Author(s):  
R L Davis ◽  
J B Konopka ◽  
O N Witte
Keyword(s):  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Leukemia Virus ◽  
Leukemia Cell ◽  
Chromosomal Translocation ◽  
Leukemia Cell Line ◽  
Tyrosine Kinase Activity ◽  
Serine Kinase ◽  
Abelson Murine Leukemia Virus

The v-abl protein of Abelson murine leukemia virus is a tyrosine-specific kinase. Its normal cellular homolog, murine c-abl, does not possess detectable tyrosine kinase activity in vitro. Previously, we have detected tyrosine kinase activity in vitro for an altered c-abl gene product (c-abl P210) in the K562 human chronic myelogenous leukemia cell line. The expression of this variant c-abl gene product correlates with chromosomal translocation and amplification of the c-abl gene in K562 cells. Like v-abl, c-abl P210 is a fusion protein containing non-abl sequences near the amino terminus of c-abl. We compared the in vitro tyrosine kinase activity of c-abl P210 with that of wild-type murine v-abl. The remarkable similarities of these two proteins with respect to cis-acting autophosphorylation, trans-acting phosphorylation of exogenous substrates, and kinase inhibition, using site-directed abl-specific antisera, suggested that c-abl P210 could function similarly to v-abl in vivo. In addition, c-abl P210 possessed an associated serine kinase activity in immunoprecipitates. The serine kinase activity was not inhibited by site-directed, abl-specific antisera that inhibit the tyrosine kinase activity, suggesting that the serine kinase activity is not an intrinsic property of c-abl P210. Thus, the activation of the c-abl gene in a human leukemia cell line may have functional consequences analogous to activation of the c-abl gene in Abelson murine leukemia virus.

scholarly journals Studies on an insulin-stimulated insulin receptor serine kinase activity: separation of the kinase activity from the insulin receptor and its reconstitution back to the insulin receptor

1995 ◽  
Vol 308 (3) ◽  
pp. 915-922 ◽  
Author(s):  
K A Asamoah ◽  
P G P Atkinson ◽  
W G Carter ◽  
G J Sale
Keyword(s):  
Myelin Basic Protein ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Basic Protein ◽  
Serine Phosphorylation ◽  
Serine Kinase ◽  
Insulin Receptor Tyrosine Kinase ◽  
Mitogen Activated Protein

In cells insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases. Recently we have achieved co-purification of the insulin receptor with insulin-stimulated insulin receptor serine kinase activity. We now show that the co-purified serine kinase activity can be removed by NaCl washing and reconstituted by adding back the NaCl eluate. Reconstitution enabled higher serine phosphorylation than achieved with the co-purified preparation. Myelin basic protein was discovered to be a potent substrate for insulin-stimulated serine phosphorylation by the co-purified preparation, with the activity responsible having similar properties to the serine kinase activity towards the receptor. Myelin basic protein was also phosphorylated on serine by the NaCl eluate. Myelin basic protein phosphorylated by the co-purified preparation or the NaCl eluate gave the same set of phosphoserine peptides. The major myelin basic protein serine kinase activity in the NaCl eluate co-purified exactly on Mono Q with the activity that restored insulin-stimulated insulin receptor serine phosphorylation. These results provide strong evidence for the true separation of the serine kinase from the insulin receptor and the distinctiveness of the serine kinase activity from the insulin receptor tyrosine kinase and mitogen-activated protein kinases. The procedures developed for the isolation of the serine kinase and the establishment of an effective in vitro substrate should allow purification of the kinase. The protocols also provide flexible systems for identifying the functions of the insulin-stimulated serine phosphorylations and the respective kinase(s).

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