Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes.

Domı́nguez, Isabel; Diaz-Meco, Marı́a T.; Municio, M M; Berra, Edurne; Herreros, A García de; Cornet, M E; Sanz, Laura; Moscat, Jorge

doi:10.1128/mcb.12.9.3776

Cited by 152 publications

(118 citation statements)

References 22 publications

Supporting

Mentioning

109

Contrasting

Order By: Relevance

“…First, PKCB was required for Ras-induced maturation in Xenopus oocytes (Dominguez et al, 1992) and serum-stimulated mitogenic signaling in mammalian cells (Berra et al, 1993). Second, the regulatory NH 2 -terminal fragment of PKCB showed preferential binding to Ras-GTP in vitro and a peptide corresponding to Ras residues 17 ± 44 blocked this interaction.…”

Section: Ras Mediates Its Actions Through Interaction With Multiple Ementioning

confidence: 99%

Increasing complexity of Ras signaling

et al. 1998

View full text Add to dashboard Cite

The initial discovery that ras genes endowed retroviruses with potent carcinogenic properties and the subsequent determination that mutated ras genes were present in a wide variety of human cancers, prompted a strong suspicion that the growth-promoting actions of mutated Ras proteins contribute to their aberrant regulation of growth stimulatory signaling pathways. In 1993, a remarkable convergence of experimental observations from genetic analyses of Drosophila, S. cerevisiae and C. elegans as well as biochemical and biological studies in mammalian cells came together to de®ne a clear role for Ras in signal transduction. What emerged was an elegant linear signaling pathway where Ras functions as a relay switch that is positioned downstream of cell surface receptor tyrosine kinases and upstream of a cytoplasmic cascade of kinases that included the mitogen-activated protein kinases (MAPKs). Activated MAPKs in turn regulated the activities of nuclear transcription factors. Thus, a signaling cascade where every component between the cell surface and the nucleus was de®ned and conserved in worms,¯ies and man. This was a remarkable achievement in our e orts to appreciate how the aberrant function of Ras proteins may contribute to the malignant growth properties of the cancer cell. However, the identi®cation of this pathway has proven to be just the beginning, rather than the culmination, of our understanding of Ras in signal transduction. Instead, we now appreciate that this simple linear pathway represents but a minor component of a very complex signaling circuitry. Ras signaling has emerged to involve a complex array of signaling pathways, where cross-talk, feedback loops, branch points and multi-component signaling complexes are recurring themes. The simplest concept of a signaling cascade, where each component simply relays the same message to the next, is clearly not the case. In this review, we summarize our current understanding of Ras signal transduction with an emphasis on new complexities associated with the recognition and/or activation of cellular e ectors, and the diverse array of signaling pathways mediated by interaction between Ras and Ras-subfamily proteins with multiple e ectors.

show abstract

Section: Ras Mediates Its Actions Through Interaction With Multiple Ementioning

confidence: 99%

Increasing complexity of Ras signaling

et al. 1998

View full text Add to dashboard Cite

show abstract

“…Cells overexpressing PKCqx did not show any further enhancement, indicating that the effect of insulin on cAMP accumulation was unique to the expression of PKC@ In contrast to the conventional PKC isoenzymes that are activated by Ca and diacylglycerol, PKC-~ is activated by arachidonic acid and phosphatidylinositol 3,4,5-triphosphate (PIP3) [9,10], which are products of insulin or other growth factor receptor stimulation [21,22]. Indeed, a recent study has shown that PKC-~ is involved in the physiological functions of insulin in vivo [11]. Stimulation of these receptors initiates a cascade of phosphorylation reaction within the cell, promoting cellular growth and differentiation [23].…”

Section: T-omentioning

confidence: 99%

“…These isoenzymes are difficult to study because of the lack of specific activators and inhibitors [7,8]. More recent studies have suggested that atypical isoenzymes are activated by extracellular stimuli such as insulin and other growth factors [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Regulation of type V adenylyl cyclase by PMA‐sensitive and ‐insensitive protein kinase C isoenzymes in intact cells

Kawabe¹,

Ebina²,

Toya³

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

“…Antibodies raised against peptides specific for the different isoforms of PKC have been used as a powerful tool to examine the presence of the members of the PKC family in different cells and tissues. Among them, the presence of aPKCc has received a growing interest since this PKC isoform has been shown to be involved in mitogenesis in several systems [5,6]. C-Terminus-directed antipeptide antibodies have been widely used to study *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Antipeptide antibodies directed against the C‐terminus of protein kinase Cζ (PKCζ) react with a Ca²⁺‐ and TPA‐sensitive PKC in HT‐29 human intestinal epithelial cells

1994

View full text Add to dashboard Cite

We have studied the PKC isoforms present in HT-29 M6 colon cancer cells, the differentiation of which to mucus-secreting cells is blocked by TPA. In addition to a major 72 kDa band, a 77 kDa PKC isoform was recognized by two different antibodies raised against a C-terminus-specific peptide for the TPA-insensitive isoform, PKCC. By different criteria (association to the membrane, down-regulation, PKC activity in immunoprecipitates) we conclude that, contrary to the 72 kDa band, the 77 kDa band corresponds to a Ca'+-and TPA-sensitive PKC. These results suggest that antipeptide antibodies directed against the C-terminus of PKC[ react in human cells with a member of the conventional PKC subfamily besides PKCC. Therefore, the data indicating that PKCC is sensitive to different agents in various cell lines should be carefully re-evaluated.

show abstract

Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes.

Cited by 152 publications

References 22 publications

Increasing complexity of Ras signaling

Increasing complexity of Ras signaling

Regulation of type V adenylyl cyclase by PMA‐sensitive and ‐insensitive protein kinase C isoenzymes in intact cells

Antipeptide antibodies directed against the C‐terminus of protein kinase Cζ (PKCζ) react with a Ca²⁺‐ and TPA‐sensitive PKC in HT‐29 human intestinal epithelial cells

Contact Info

Product

Resources

About

Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes.

Cited by 152 publications

References 22 publications

Increasing complexity of Ras signaling

Increasing complexity of Ras signaling

Regulation of type V adenylyl cyclase by PMA‐sensitive and ‐insensitive protein kinase C isoenzymes in intact cells

Antipeptide antibodies directed against the C‐terminus of protein kinase Cζ (PKCζ) react with a Ca2+‐ and TPA‐sensitive PKC in HT‐29 human intestinal epithelial cells

Contact Info

Product

Resources

About

Antipeptide antibodies directed against the C‐terminus of protein kinase Cζ (PKCζ) react with a Ca²⁺‐ and TPA‐sensitive PKC in HT‐29 human intestinal epithelial cells