Activation of Protein Kinase C by Purified Bovine Brain 14‐3‐3: Comparison with Tyrosine Hydroxylase Activation

Tanji, Masanori; Horwitz, Robert J.; Rosenfeld, Gary C.; Waymire, Jack C.

doi:10.1046/j.1471-4159.1994.63051908.x

Cited by 56 publications

(22 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, several other studies have established that an interaction exists between 14-3-3 ζ and PKCs in rat retina, rodent brain and PC12 cells [102,103]. As mentioned above, there are contradictory reports regarding modulation of PKC activity by 14-3-3 proteins, with either inhibition [104,105,106] or activation [107,108] of PKCs, depending on the 14-3-3 and PKC isoforms involved and the cellular conditions.…”

Section: Role Of 14-3-3 Proteins In Autophagymentioning

confidence: 99%

14-3-3 Proteins are Regulators of Autophagy

Pozuelo-Rubio

2012

Cells

View full text Add to dashboard Cite

14-3-3 proteins are implicated in the regulation of proteins involved in a variety of signaling pathways. 14-3-3-dependent protein regulation occurs through phosphorylation-dependent binding that results, in many cases, in the release of survival signals in cells. Autophagy is a cell digestion process that contributes to overcoming nutrient deprivation and is initiated under stress conditions. However, whether autophagy is a cell survival or cell death mechanism remains under discussion and may depend on context. Nevertheless, autophagy is a cellular process that determines cell fate and is tightly regulated by different signaling pathways, some of which, for example MAPK, PI3K and mTOR, are tightly regulated by 14-3-3 proteins. It is therefore important to understand the role of 14-3-3 protein in modulating the autophagic process. Within this context, direct binding of 14-3-3 to mTOR regulatory proteins, such as TSC2 and PRAS40, connects 14-3-3 with autophagy regulatory processes. In addition, 14-3-3 binding to human vacuolar protein sorting 34 (hVps34), a class III phosphatidylinositol-3-kinase (PI3KC3), indicates the involvement of 14-3-3 proteins in regulating autophagosome formation. hVps34 is involved in vesicle trafficking processes such as autophagy, and its activation is needed for initiation of autophagy. Chromatography and overlay techniques suggest that hVps34 directly interacts with 14-3-3 proteins under physiological conditions, thereby maintaining hVps34 in an inactive state. In contrast, nutrient starvation promotes dissociation of the 14-3-3–hVps34 complex, thereby enhancing hVps34 lipid kinase activity. Thus, 14-3-3 proteins are regulators of autophagy through regulating key components of the autophagic machinery. This review summarizes the role of 14-3-3 protein in the control of target proteins involved in regulating the master switches of autophagy.

show abstract

Section: Role Of 14-3-3 Proteins In Autophagymentioning

confidence: 99%

14-3-3 Proteins are Regulators of Autophagy

Pozuelo-Rubio

2012

Cells

View full text Add to dashboard Cite

show abstract

“…68 The acidic 14-3-3⑀, 14-3-3, and 14-3-3␦ proteins have a very broad range of specificities, one of which is to bind and activate protein kinase C (PKC) and certain PKC isoforms. [69][70][71][72][73] Since the inhibition of PKC leads to activation of caspase networks and thus induction of apoptosis in APL and other leukemias, [74][75][76] the link between diminished PKC activity via the down-regulation of 14-3-3 proteins in NB4 and HL-60 provides additional information regarding the involvement of 14-3-3 proteins toward the mechanisms of caspase activation in these leukemias.…”

Section: Atra-induced Posttranscriptional Suppression During Initiatimentioning

confidence: 99%

Comparative proteomic analysis of all-trans-retinoic acid treatment reveals systematic posttranscriptional control mechanisms in acute promyelocytic leukemia

Harris

Özpolat

Abdi

et al. 2004

Blood

115

View full text Add to dashboard Cite

All-trans-retinoic acid (ATRA) induces growth inhibition, differentiation, and apoptosis in cancer cells, including acute promyelocytic leukemia (APL). In APL, expression of promyelocytic leukemia protein retinoic acid receptor-␣ (PML-RAR␣) fusion protein, owing to the t(15; 17) reciprocal translocation, leads to a block in the promyelocytic stage of differentiation. Here, we studied molecular mechanisms involved in ATRA-induced growth inhibition and myeloid cell differentiation in APL. By employing comprehensive high-throughput proteomic methods of 2-dimensional (2-D) gel electrophoresis and amino acid-coded mass tagging coupled with electrospray ionization (ESI) mass spectrometry, we systematically identified a total of 59 differentially expressed proteins that were consistently modulated in response to ATRA treatment. The data revealed significant downregulation of eukaryotic initiation and elongation factors, initiation factor 2 (IF2), eukaryotic initiation factor 4AI (eIF4AI), eIF4G, eIF5, eIF6, eukaryotic elongation factor 1A-1 (eEF1A-1), EF-1-␦, eEF1␥, 14-3-3⑀, and 14-3-3/␦ (P < .05). The translational inhibitor DAP5/p97/NAT1 (deathassociated protein 5) and PML isoform-1 were found to be up-regulated (P < .05). Additionally, the down-regulation of heterogeneous nuclear ribonucleoproteins (hnRNPs) C1/C2, UP2, K, and F; small nuclear RNPs (snRNPs) D3 and E; nucleoprotein tumor potentiating region (TPR); and protein phosphatase 2A (PP2A) were found (P < .05); these were found to function in pre-mRNA processing, splicing, and export events. Importantly, these pro-

show abstract

“…Moreover, 14-3-3 proteins have been implicated also in Ras/MAPK cascade signaling in vertebrates (Fantl et al 1994;Li et al 1995) and during pseudohyphal development in S. cerevisiae (Roberts et al 1997). Finally, vertebrate 14-3-3 proteins were shown to inhibit or activate protein kinase C (PKC), which is involved in many signaling processes (Toker et al 1990;Isobe et al 1992;Tanji et al 1994), and to stimulate the interaction between PKC and the mitogenstimulated Raf1 kinase that controls cell growth (Van Der Hoeven et al 2000).…”

mentioning

confidence: 99%

The Saccharomyces cerevisiae 14-3-3 Proteins Are Required for the G1/S Transition, Actin Cytoskeleton Organization and Cell Wall Integrity

et al. 2006

View full text Add to dashboard Cite

14-3-3 proteins are highly conserved polypeptides that participate in many biological processes by binding phosphorylated target proteins. The Saccharomyces cerevisiae BMH1 and BMH2 genes, whose concomitant deletion is lethal, encode two functionally redundant 14-3-3 isoforms. To gain insights into the essential function(s) shared by these proteins, we searched for high-dosage suppressors of the growth defects of temperature-sensitive bmh mutants. Both the protein kinase C1 (Pkc1) and its upstream regulators Wsc2 and Mid2 were found to act as high dosage suppressors of bmh mutants' temperature sensitivity, indicating a functional interaction between 14-3-3 and Pkc1. Consistent with a role of 14-3-3 proteins in Pkc1-dependent cellular processes, shift to the restrictive temperature of bmh mutants severely impaired initiation of DNA replication, polarization of the actin cytoskeleton, and budding, as well as cell wall integrity. Because Pkc1 acts in concert with the Swi4-Swi6 (SBF) transcriptional activator to control all these processes, the defective G 1 /S transition of bmh mutants might be linked to impaired SBF activity. Indeed, the levels of the G 1 cyclin CLN2 transcripts, which are positively regulated by SBF, were dramatically reduced in bmh mutants. Remarkably, budding and DNA replication defects of bmh mutants were suppressed by CLN2 expression from an SBF-independent promoter, suggesting that 14-3-3 proteins might contribute to regulating the late G 1 transcriptional program.

show abstract

Activation of Protein Kinase C by Purified Bovine Brain 14‐3‐3: Comparison with Tyrosine Hydroxylase Activation

Abstract: In the course of the purification of 14-3

Cited by 56 publications

References 20 publications

14-3-3 Proteins are Regulators of Autophagy

14-3-3 Proteins are Regulators of Autophagy

Comparative proteomic analysis of all-trans-retinoic acid treatment reveals systematic posttranscriptional control mechanisms in acute promyelocytic leukemia

The Saccharomyces cerevisiae 14-3-3 Proteins Are Required for the G1/S Transition, Actin Cytoskeleton Organization and Cell Wall Integrity

Contact Info

Product

Resources

About