Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro

Gschwendt, Michael; Kielbassa, Kirsten; Kittstein, Walter; Marks, Friedrich

doi:10.1016/0014-5793(94)00514-1

Cited by 99 publications

(103 citation statements)

References 26 publications

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“…PKC␦ is phosphorylated on tyrosine in Ras (35), v-Src (28), or insulin-like growth factor-1 (36) -transformed cells; in 12-O-tetradecanoylphorbol-13-acetate (16), platelet-derived growth factor (16), epidermal growth factor (25), thrombin (26), or carbachol (37) -stimulated cells; and upon cross-linking of the high-affinity receptor for IgE in rat basophilic leukemia cells (24). Similarly, Src family protein kinases were found to phosphorylate PKC␦ in vitro (27,38). In addition, PKC␣ was found to become tyrosine phosphorylated in insulin-stimulated cells (39), and tyrosine phosphorylation of several PKC isoforms (PKC␣, -␤I, -␥, -␦, -⑀, and -) was observed in COS cells in response to H 2 O 2 stimulation (40).…”

Section: Discussionmentioning

confidence: 99%

Regulation of Protein Kinase Cθ Function during T Cell Activation by Lck-mediated Tyrosine Phosphorylation

Liu

Witte

Liu

et al. 2000

Journal of Biological Chemistry

114

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Protein kinase C (PKC) is a novel Ca2؉ -independent PKC isoform, which is selectively expressed in skeletal muscle and hematopoietic cells, especially T cells. In T cells, it colocalizes with the T cell antigen receptor (TCR)⅐CD3 complex in antigen-stimulated T cells and is involved in the transcriptional activation of the interleukin-2 gene. In the present study, we report that PKC is tyrosine phosphorylated in Jurkat T cells upon TCR⅐CD3 activation. The Src family protein-tyrosine kinase, Lck, was critical in TCR-induced tyrosine phosphorylation of PKC. Lck phosphorylated and was associated with the regulatory domain of PKC both in vitro and in intact cells. This association was constitutive, but it was enhanced by T cell activation, with both Srchomology 2 and Src-homology 3 domains of Lck contributing to it. Tyrosine 90 (Tyr-90) in the regulatory domain of PKC was identified as the major phosphorylation site by Lck. A constitutively active mutant of PKC (A148E) could enhance proliferation of Jurkat T cells and synergized with ionomycin to induce nuclear factor of T cells activity. However, mutation of Tyr-90 into phenylalanine markedly reduced (or abolished) these activities. These results suggest that Lck plays an important role in tyrosine phosphorylation of PKC, which may in turn modulate the physiological functions of PKC during TCR-induced T cell activation. Protein kinase C (PKC)1 is a family of serine/threonine kinases that play critical roles in the regulation of differentiation and proliferation in many cell types and in the response to diverse stimuli (reviewed in Refs. 1 and 2). Products of the 10 known mammalian PKC genes are classified into four subfamilies of Ca 2ϩ -dependent (or conventional, PKC␣, -␤, and -␥), Ca 2ϩ -independent (or novel, PKC␦, -⑀, -, and -), atypical (PKC and /), and PKC/D enzymes. Activity of PKC enzymes is regulated by phosphorylation and binding of defined cofactors. Enzyme activation is associated with its redistribution among different cellular compartments, commonly from the cytosolic to the particulate (membrane) fraction. Studies indicate that PKC is also important during T cell activation. This is indicated by the ability of physiological T cell receptor (TCR) ligands to activate PKC and induce its translocation from the cytosol to the particulate fraction; by the ability of PKC inhibitors, or PKC depletion by prolonged phorbol ester treatment, to block lymphocyte signaling and activation; by the requirement for persistent PKC activation during mitogenic T cell activation; and, finally, by the diminished TCR⅐CD3-mediated proliferation in PKC-deficient T cells (reviewed in Ref. 3).PKC is a novel Ca 2ϩ

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Section: Discussionmentioning

confidence: 99%

Regulation of Protein Kinase Cθ Function during T Cell Activation by Lck-mediated Tyrosine Phosphorylation

Liu

Witte

Liu

et al. 2000

Journal of Biological Chemistry

114

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“…1). In vitro, Src is reported to phosphorylate PKC-8, but acts only on the activated form of the enzyme, following PMA activation [18], And, PKC-8 is reported to associate with FceRIfl chain and to phosphorylate the y-chain on threonine in vivo [19]. It is possible that other PKC isoforms are also activated by FcyRIIa cross-linking.…”

Section: Lateral Mobility In Pma-treated Cellsmentioning

confidence: 99%

Lateral mobility of FcγRIIa is reduced by protein kinase C activation

Zhang¹,

Yang²,

Odin³

et al. 1995

FEBS Letters

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“…Upon activation by diacylglycerol and phospholipid co-factors, PKC undergoes further autophosphorylation on serine and threonine residues Mitchell et al, 1989). A number of PKC isoforms, including d, e, Z, x (Denning et al, 1996) and a, b, g (Gschwendt et al, 1994) can also be phosphorylated on tyrosine residues in vitro. However, PKC d is the only PKC isoform to undergo phosphorylation on tyrosine in vivo (Li et al, 1994a;Gschwendt et al, 1994) and is the only PKC isoform whose kinase activity is in¯uenced by tyrosine phosphorylation (Gschwendt et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

“…A number of PKC isoforms, including d, e, Z, x (Denning et al, 1996) and a, b, g (Gschwendt et al, 1994) can also be phosphorylated on tyrosine residues in vitro. However, PKC d is the only PKC isoform to undergo phosphorylation on tyrosine in vivo (Li et al, 1994a;Gschwendt et al, 1994) and is the only PKC isoform whose kinase activity is in¯uenced by tyrosine phosphorylation (Gschwendt et al, 1994). All reports are in agreement with the fact that PKC d is phosphorylated on tyrosine in response to in vivo agonist treatment or PMA (Li et al, 1994a;Denning et al, 1993Denning et al, , 1996Gschwendt et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Association of PKC δ and active Src in PMA-treated MCF-7 human breast cancer cells

et al. 1998

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Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro

Cited by 99 publications

References 26 publications

Regulation of Protein Kinase Cθ Function during T Cell Activation by Lck-mediated Tyrosine Phosphorylation

Regulation of Protein Kinase Cθ Function during T Cell Activation by Lck-mediated Tyrosine Phosphorylation

Lateral mobility of FcγRIIa is reduced by protein kinase C activation

Association of PKC δ and active Src in PMA-treated MCF-7 human breast cancer cells

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