scholarly journals Phosphorylation of p35 and p39 by Cdk5 determines the subcellular location of the holokinase in a phosphorylation-site-specific manner

2012 ◽  
Vol 125 (14) ◽  
pp. 3421-3429 ◽  
Author(s):  
A. Asada ◽  
T. Saito ◽  
S.-i. Hisanaga
Keyword(s):  
Phosphorylation Site ◽  
Subcellular Location ◽  
Site Specific ◽  
Specific Manner

scholarly journals Methamphetamine Administration Increases Proceptive Behavior by Activating Src Kinase and Upregulating Progesterone Receptor in the Medial Amygdala

2018 ◽  
Author(s):  
Katrina M Williams ◽  
Sarah A Rudzinskas ◽  
Jessica A Mong
Keyword(s):  
Progesterone Receptor ◽  
Phosphorylation Site ◽  
Progesterone Receptors ◽  
Receptor Expression ◽  
Medial Amygdala ◽  
Specific Manner ◽  
Receptor Action ◽  
Necessary And Sufficient ◽  
Motivated Behaviors

Methamphetamine, a psychostimulant drug of abuse, increases sexual motivation both in humans and in rodent models. The activation of dopamine type-1 receptors (D1Rs) within the medial amygdala, in the presence of ovarian hormones (EB+P), are both necessary and sufficient for increases in proceptive, or sexually motivated, behaviors. Here, we demonstrate that methamphetamine increases progesterone receptor expression in the medial amygdala independently of D1R activation, and that lentiviral overexpression of the progesterone receptor was able to recapitulate the methamphetamine-induced enhancement of proceptive behaviors. Furthermore, we found that within the medial amygdala, these progesterone receptors show an increase in phosphorylation of serine 294 of the progesterone receptor in a region-specific manner. The involvement of this phosphorylation site suggests a role for cytosolic kinases, which may be responsible for enhanced progesterone receptor action. The phosphorylation of serine 294 is blocked by D1R antagonists, and by inhibiting cSrc and ERK1/2, downstream of D1R signaling, we identified that Src and ERK1/2 are required for enhanced proceptive behavior. Taken together, we propose that within the medial amygdala, methamphetamine enhances progesterone receptors sensitivity to its cognate ligand via interaction with cSrc kinase and ERK1/2, as well as an increase total progesterone receptors, thus leading to enhanced proceptive behaviors in the rat.

An Enzyme-Linked Immunosorbent Assay for Protein Kinase D Activity Using Phosphorylation Site-Specific Antibodies

2007 ◽  
Vol 5 (5) ◽  
pp. 637-644 ◽  
Author(s):  
An Rykx ◽  
Sadia Vancauwenbergh ◽  
Line De Kimpe ◽  
Katrien Janssens ◽  
Sandy Vandoninck ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Immunosorbent Assay ◽  
Phosphorylation Site ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Kinase D ◽  
Site Specific ◽  
Specific Antibodies

Optimization of the posttranslational click modification of proteins

2011 ◽  
Vol 76 (9) ◽  
pp. 1089-1101
Author(s):  
Milan Vrabel ◽  
Emine Kaya ◽  
Stefan Prill ◽  
Veronika Ehmke ◽  
Thomas Carell
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Fluorescent Protein ◽  
Click Reaction ◽  
Yellow Fluorescent Protein ◽  
Trna Synthetase ◽  
Site Specific ◽  
Specific Manner ◽  
Modified Proteins ◽  
A Site

In order to develop efficient methods that would enable the synthesis of posttranslationaly modified proteins in a site-specific manner we have adopted the orthogonal pyrrolysyl-tRNA synthetase/tRNA pair to genetically encode various pyrrolysine analogs, which we were able to insert into the yellow fluorescent protein (YFP). These experiments showed that the alkene and alkyne containing amino acids 5 and 6 are superior substrates for the pyrrolysyl-tRNA synthetase and that they can be successfully incorporated into proteins. Using the Cu(I)-catalyzed Huisgen–Meldal–Sharpless click reaction, the alkyne containing YFP was finally glycosylated with various sugars. We confirmed the presence of the modified amino acids as well as the corresponding sugar modifications by HPLC-MS/MS mass spectrometry.

scholarly journals Characterization of Protein Kinase A and Protein Kinase C Phosphorylation of theN-Methyl-D-aspartate Receptor NR1 Subunit Using Phosphorylation Site-specific Antibodies

1997 ◽  
Vol 272 (8) ◽  
pp. 5157-5166 ◽  
Author(s):  
Whittemore G. Tingley ◽  
Michael D. Ehlers ◽  
Kimihiko Kameyama ◽  
Carol Doherty ◽  
Janine B. Ptak ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Phosphorylation Site ◽  
Site Specific ◽  
Specific Antibodies ◽  
Kinase C ◽  
Aspartate Receptor ◽  
Kinase A

scholarly journals Phosphorylation of the Oncofetal Variant of the Human Bile Salt-dependent Lipase

2001 ◽  
Vol 276 (15) ◽  
pp. 12356-12361 ◽  
Author(s):  
Alain Verine ◽  
Josette Le Petit-Thevenin ◽  
Laurence Panicot-Dubois ◽  
Annick Valette ◽  
Dominique Lombardo
Keyword(s):  
High Pressure ◽  
Bile Salt ◽  
Cho Cells ◽  
Phosphorylation Site ◽  
Chinese Hamster ◽  
Human Bile ◽  
Site Specific ◽  
Phosphorylation Motif ◽  
Extracellular Compartment ◽  
First Time

In this paper, we report, for the first time, the localization of the phosphorylation site of the fetoacinar pancreatic protein (FAPP), which is an oncofetal variant of the pancreatic bile salt-dependent lipase. Using Chinese hamster ovary (CHO) cells transfected with the cDNA encoding FAPP, we radiolabeled the enzyme with32P, and then the protein was purified by affinity chromatography on cholate-immobilized Sepharose column and submitted to a CNBr hydrolysis. Analysis of peptides by high pressure liquid chromatography, associated with the radioactivity profile, revealed that the phosphorylation site is located at threonine 340. Site-specific mutagenesis experiments, in which the threonine was replaced by an alanine residue, were used to invalidate the phosphorylation of FAPP and to study the influence of the modification on the activity and secretion of the enzyme. These studies showed that CHO cells, transfected with the mutated cDNA of FAPP, kept all of their ability to synthesize the protein, but the loss of the phosphorylation motif prevented the release of the protein in the extracellular compartment. However, the mutated enzyme, which was sequestrated in the transfected CHO cells, remains active on bile salt-dependent lipase substrates.

scholarly journals Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides

2010 ◽  
Vol 21 (1) ◽  
pp. 53-59 ◽  
Author(s):  
Young Sik Shin ◽  
Jeong Hee Moon ◽  
Myung Soo Kim
Keyword(s):  
Phosphorylation Site ◽  
Site Specific

scholarly journals Osterix Regulates Tooth Root Formation in a Site-specific Manner

2015 ◽  
Vol 94 (3) ◽  
pp. 430-438 ◽  
Author(s):  
T.H. Kim ◽  
C.H. Bae ◽  
J.C. Lee ◽  
J.E. Kim ◽  
X. Yang ◽  
...  
Keyword(s):  
Root Formation ◽  
Tooth Root ◽  
Site Specific ◽  
Specific Manner ◽  
A Site
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