scholarly journals Impact of Ca2+on structure of soybean CDPKβ and accessibility of the Tyr-24 autophosphorylation site

2013 ◽  
Vol 8 (12) ◽  
pp. e27671 ◽  
Author(s):  
Man-Ho Oh ◽  
Xia Wu ◽  
Steven C Huber
Keyword(s):  
Autophosphorylation Site

scholarly journals Evidence for autoinhibitory regulation of the c-src gene product. A possible interaction between the src homology 2 domain and autophosphorylation site.

1993 ◽  
Vol 268 (2) ◽  
pp. 1132-1140
Author(s):  
Y. Fukami ◽  
K. Sato ◽  
K. Ikeda ◽  
K. Kamisango ◽  
K. Koizumi ◽  
...  
Keyword(s):  
Gene Product ◽  
Src Homology 2 ◽  
Src Gene ◽  
Src Homology ◽  
Src Homology 2 Domain ◽  
Autophosphorylation Site

Regulation by the autophosphorylation site in overexpressed pp60c-src

1988 ◽  
Vol 8 (10) ◽  
pp. 4541-4546
Author(s):  
T E Kmiecik ◽  
P J Johnson ◽  
D Shalloway
Keyword(s):  
Kinase Activity ◽  
Tyrosine Phosphatase ◽  
Phosphatase Inhibitor ◽  
Autophosphorylation Site

We show that overexpressed pp60c-src is phosphorylated at Tyr-416 and has increased specific kinase activity when isolated from cells incubated with vanadate, a tyrosine phosphatase inhibitor. This supports the hypothesis that transient Tyr-416 phosphorylation modulates the activity of overexpressed pp60c-src in vivo. Mutagenesis indicates that Tyr-416 modulates pp60v-src activity as well.

Cross-linking of T-cell surface molecules CD4 and CD8 stimulates phosphorylation of the lck tyrosine protein kinase at the autophosphorylation site

1990 ◽  
Vol 10 (10) ◽  
pp. 5305-5313
Author(s):  
K X Luo ◽  
B M Sefton
Keyword(s):  
T Cell ◽  
Tyrosine Phosphorylation ◽  
Cell Lines ◽  
Kinase Activity ◽  
Cross Linking ◽  
Cell Surface Molecules ◽  
Surface Molecules ◽  
Tyrosine Protein Kinase ◽  
Autophosphorylation Site

p56lck, a lymphocyte-specific tyrosine protein kinase, binds to the cytoplasmic tails of the T-cell surface molecules CD4 and CD8. Cross-linking of CD4 expressed on the surface of murine thymocytes, splenocytes, and CD4+ T-cell lines induced tyrosine phosphorylation of p56lck dramatically. Cross-linking of CD8 stimulated tyrosine phosphorylation of p56lck strongly in murine L3 and GA4 cells, slightly in splenocytes, but not detectably in thymocytes. Differing effects of cross-linking on in vitro tyrosine kinase activity of p56lck were observed. An increase in the in vitro kinase activity of p56lck, when assayed with [Val5]-angiotensin II as an exogenous substrate, was found to accompany cross-linking of CD4 in three cell lines. No stimulation of the in vitro kinase activity, however, was observed after cross-linking of CD8 in L3 cells. The phosphorylation of p56lck at Tyr-394, the autophosphorylation site, was stimulated by cross-linking in all cell lines examined. Tyr-394 was the predominant site of increased tyrosine phosphorylation in two leukemic cell lines. In the other two cell lines, the phosphorylation of both Tyr-394 and an inhibitory site, Tyr-505, was found to increase. In contrast to cross-linking with antibodies, no striking increase in the tyrosine phosphorylation of p56lck was stimulated by antigenic stimulation. Therefore, the effect of antibody-induced aggregation of CD4 and CD8 on the tyrosine phosphorylation of p56lck differs, at least quantitatively, from what occurs during antigen-induced T-cell activation.

scholarly journals Invariant Leu Preceding Turn Motif Phosphorylation Site Controls the Interaction of Protein Kinase C with Hsp70

2006 ◽  
Vol 281 (43) ◽  
pp. 32461-32468 ◽  
Author(s):  
Tianyan Gao ◽  
Alexandra C. Newton
Keyword(s):  
Protein Kinase C ◽  
Heat Shock ◽  
Protein Kinase ◽  
Phosphorylation Site ◽  
Insoluble Fraction ◽  
Down Regulation ◽  
Kinase C ◽  
Shock Proteins ◽  
Invariant Residue ◽  
Autophosphorylation Site

Heat shock proteins play important roles in regulating signal transduction in cells by associating with, and stabilizing, diverse signaling molecules, including protein kinases. Previously, we have shown that heat shock protein Hsp70 associates with protein kinase C (PKC) via an interaction that is triggered by dephosphorylation at the turn phosphorylation motif. Here we have identified an invariant residue in the carboxyl terminus of PKC that mediates the binding to Hsp70. Specifically, we show that Hsp70 binds to Leu (Leu-640) immediately preceding the conserved turn motif autophosphorylation site (Thr-641) in PKC βII. Co-immunoprecipitation experiments reveal that mutation of Leu-640 to Gly decreases the interaction of Hsp70 with PKC βII. This weakened interaction between Hsp70 and the mutant PKCs results in accumulation of dephosphorylated PKC in the detergent-insoluble fraction of cells. In addition, the Hsp70-binding mutant is considerably more sensitive to down-regulation compared with WT PKC: disruption of Hsp70 binding leads to accelerated dephosphorylation and enhanced ubiquitination of mutant PKC upon phorbol ester treatment. Last, pulse-chase experiments demonstrate that Hsp70 preferentially binds the species of mature PKC that has become dephosphorylated compared with the newly synthesized protein that has yet to be phosphorylated. Thus, Hsp70 binds a hydrophobic residue preceding the turn motif, protecting PKC from down-regulation and sustaining the signaling lifetime of the kinase.

scholarly journals Ser2 is the autophosphorylation site in the beta subunit from bicistronically expressed human casein kinase-2 and from native rat liver casein kinase-2beta

1993 ◽  
Vol 218 (2) ◽  
pp. 515-521 ◽  
Author(s):  
Brigitte BOLDYREFF ◽  
Peter JAMES ◽  
Werner STAUDENMANN ◽  
Olaf-Georg ISSINGER
Keyword(s):  
Rat Liver ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Beta Subunit ◽  
Autophosphorylation Site

scholarly journals Substitution of the Autophosphorylation Site Thr516with a Negatively Charged Residue Confers Constitutive Activity to Mouse 3-Phosphoinositide-dependent Protein Kinase-1 in Cells

2002 ◽  
Vol 277 (19) ◽  
pp. 16632-16638 ◽  
Author(s):  
Michael J. Wick ◽  
KeriLyn R. Wick ◽  
Hui Chen ◽  
Huili He ◽  
Lily Q. Dong ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Constitutive Activity ◽  
Dependent Protein Kinase ◽  
Charged Residue ◽  
Dependent Protein ◽  
Autophosphorylation Site ◽  
In Cells

scholarly journals Macrophage colony-stimulating factor-induced tyrosine phosphorylation of c-fms proteins expressed in FDC-P1 and BALB/c 3T3 cells.

1990 ◽  
Vol 10 (6) ◽  
pp. 2528-2538 ◽  
Author(s):  
P Tapley ◽  
A Kazlauskas ◽  
J A Cooper ◽  
L R Rohrschneider
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Phosphorylation Sites ◽  
Colony Stimulating Factor ◽  
Major Site ◽  
Tryptic Peptides ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor ◽  
Autophosphorylation Site

The c-fms protein is a receptor for macrophage colony-stimulating factor (M-CSF) with intrinsic protein-tyrosine kinase activity. We investigated the tyrosine phosphorylation of murine c-fms proteins expressed from a retroviral vector in factor-dependent myeloid FDC-P1 cells and in BALB/c 3T3 fibroblasts transformed by the expression of the c-fms gene. FDC-P1 cells expressing c-fms were able to grow and differentiate in response to M-CSF. Their c-fms proteins were normally phosphorylated on serine and became phosphorylated on tyrosine residues contained in five tryptic peptides when the cells were exposed to M-CSF. A subset of these peptides was constitutively phosphorylated in BALB/c cells expressing c-fms, consistent with the production of M-CSF by these cells. All the peptides detected in vivo were also phosphorylated in vitro. These peptides were analyzed by susceptibility to proteases, comparison with synthetic peptides, and site-directed mutagenesis. The identities of four of the tryptic peptides were determined; they arise from three unique tyrosine phosphorylation sites. One major site of tyrosine phosphorylation at residue 697 accounted for two of the tryptic peptides. A second major site was identified at tyrosine residue 706. These two tyrosine phosphorylation sites are located within the tyrosine kinase insert region. Tyrosine 807, which has homology to the major autophosphorylation site of the p60v-src tyrosine kinase, is a minor autophosphorylation site. Possible functional roles for these phosphorylations of the c-fms protein include interactions with substrate proteins, catalytic activity, and ligand-induced degradation.

scholarly journals Conversion of a phosphoseryl/threonyl phosphatase into a phosphotyrosyl phosphatase

1988 ◽  
Vol 256 (3) ◽  
pp. 1029-1034 ◽  
Author(s):  
J Goris ◽  
C J Pallen ◽  
P J Parker ◽  
J Hermann ◽  
M D Waterfield ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phosphatase Activity ◽  
Growth Factor Receptor ◽  
Xenopus Laevis Oocytes ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Epidermal Growth ◽  
Autophosphorylation Site

By use of the autophosphorylated epidermal-growth-factor receptor and the synthetic peptide RRLIE-DAEY(P)AARG, representing an autophosphorylation site of the transforming protein of Rous-sarcoma virus, it is demonstrated that the phosphotyrosyl phosphatase activity of the polycation-stimulated phosphatases is substantially increased by an enzyme-directed effect of ATP or PPi. Concomitant with this increase in phosphotyrosyl phosphatase activity, the phosphorylase phosphatase activity is decreased, thus dramatically changing the substrate specificity of these enzymes. The dephosphorylation of four different phosphotyrosyl sites of the epidermal-growth-factor receptor is neither consecutive nor at random, but a preferred dephosphorylation of the P1 site over the P3 greater than P2 greater than P4 sites is observed. This phosphatase activity represents a substantial fraction of the total phosphotyrosyl phosphatase activity in the post-mitochondrial supernatant of Xenopus laevis oocytes.

Synthesis and conformational studies on peptides corresponding to a putative autophosphorylation site of abl TPK*

2009 ◽  
Vol 41 (3) ◽  
pp. 291-299 ◽  
Author(s):  
PAOLO RUZZA ◽  
ANDREA CALDIIRAN ◽  
BRUNO FILIPPI ◽  
ARIANNA DONELLA-DEANA ◽  
LORENZO A. PINNA ◽  
...  
Keyword(s):  
Conformational Studies ◽  
Autophosphorylation Site

Linear and cyclic synthetic peptides related to the main autophosphorylation site of the Src tyrosine kinases as substrates and inhibitors of Lyn †

2009 ◽  
Vol 45 (6) ◽  
pp. 529-539 ◽  
Author(s):  
PAOLO RUZZA ◽  
ANDREA CALDERAN ◽  
BRUNO FILIPPI ◽  
BARBARA BIONDI ◽  
ARIANNA DONELLA DEANA ◽  
...  
Keyword(s):  
Tyrosine Kinases ◽  
Synthetic Peptides ◽  
Src Tyrosine Kinases ◽  
Autophosphorylation Site
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