PKCη is localized in the Golgi, ER and nuclear envelope and translocates to the nuclear envelope upon PMA activation and serum-starvation:

Maissel, Adva; Marom, Mairav; Shtutman, Marat; Shahaf, Galit; Livneh, Etta

doi:10.1016/j.cellsig.2005.09.003

Cited by 49 publications

(38 citation statements)

References 49 publications

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“…PKCη existed mainly in the Golgi apparatus with granular cytoplasmic distribution in the unstimulated cells (Fig.3I). PKCη expressed in COS7, was previously reported to be localized in the Golgi apparatus [11], further supporting our observation. TPA treatment induced the translocation of PKCη to the plasma membrane with cytoplasmic distribution (Fig.…”

Section: Tpa Induced Translocation Of Pkc Isoforms In Nih3t3 Cellssupporting

confidence: 92%

“…PKCη, a novel PKC, localized to the Golgi and other cytoplasmic membranous organelles and its TPA-induced translocation to the plasma membrane has also been supported by other investigators [11]. The Golgi localization of the inactive PKC isoforms was shown to be mediated by the C1b domain [10,11].…”

Section: Discussionmentioning

confidence: 59%

“…The Golgi localization of the inactive PKC isoforms was shown to be mediated by the C1b domain [10,11]. However it is not clear how the C1b domain mediates this localization.…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies have suggested that the stimulation of various PKC isoforms by PKC agonist phorbol esters results in the rapid translocation of the isoforms from the cytosolic sites to membrane-associated sites [11][12][13].To study the real time translocation of PKC isoform, we used the classical PKC isoform, PKCβ, which has two transcriptional variants (PKCβ1, PKCβ2) containing about 96% homology. NIH3T3 cells were transfected with pGFP3PKCβ1-WT and pGFP3-PKCβ2-WT, which encoded PKCβ1-GFP and PKCβ2-GFP, respectively.…”

Section: Real Time Analysis Of Pkcβ Translocation In Nih3t3 Cellsmentioning

confidence: 99%

“…PKCε exhibits a unique association with Golgi membranes via its C1 domain and modulates Golgi functions [10]. Another novel PKC isoform, PKCγ, was reported to localize at the Golgi apparatus, the endoplasmic reticulum and the nuclear envelope in COS-7 and MCF-7 cells, and TPA induced its translocation to the plasma membrane and the nuclear envelope [11]. These studies suggest that the subcellular localization of PKC isoforms is not only isoform or cell line specific, but also stimuli specific.…”

Section: Introductionmentioning

confidence: 99%

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Isoform-specific translocation of PKC isoforms in NIH3T3 cells by TPA

Kazi

Soh

2007

Biochemical and Biophysical Research Communications

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Protein kinase C (PKC), a multi-gene family of enzymes, plays key roles in the pathways of signal transduction, growth control and tumorigenesis. Variations in the intracellular localization of the individual isoforms are thought to be an important mechanism for the isoform-specific regulation of enzyme activity and substrate specificity. To provide a dynamic method of analyzing the localization of the specific isoforms of PKC in living cells, we generated fluorescent fusion proteins of the various PKC isoforms by using the green fluorescent protein (GFP) as a fluorescent marker at the carboxyl termini of these enzymes. The intracellular localization of the specific PKC isoforms was then examined by fluorescence microscopy after transient transfection of the respective PKC-GFP expression vector into NIH3T3 cells and subsequent TPA stimulation. We found that the specific isoforms of PKC display distinct localization patterns in untreated NIH3T3 cells. For example, PKCα is localized mainly in the cytoplasm while PKCε is localized mainly in the Golgi apparatus. We also observed that PKCα, β1, β2, γ, δ, ε, and η translocate to the plasma membrane within 10 min of the start of TPA treatment, while the cellular localizations of PKCζ and ι were not affected by TPA. Using a protein kinase inhibitor, we also showed that the kinase activity was not important for the translocation of PKC. These results suggest that specific PKC isoforms exert spatially distinct biological effects by virtue of their directed translocation to different intracellular sites.

show abstract

Section: Tpa Induced Translocation Of Pkc Isoforms In Nih3t3 Cellssupporting

confidence: 92%

Section: Discussionmentioning

confidence: 59%

“…The Golgi localization of the inactive PKC isoforms was shown to be mediated by the C1b domain [10,11]. However it is not clear how the C1b domain mediates this localization.…”

Section: Discussionmentioning

confidence: 99%

Section: Real Time Analysis Of Pkcβ Translocation In Nih3t3 Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Isoform-specific translocation of PKC isoforms in NIH3T3 cells by TPA

Kazi

Soh

2007

Biochemical and Biophysical Research Communications

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Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila

et al. 2021

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A total of 10-20% of plasma membrane proteins are anchored by glycosylphosphatidylinositol (GPI). GPI is attached to proteins by GPI transamidase (GPI-T), which contains five subunits named PIGK, PIGS, PIGT, PIGU, and GPAA1. We previously reported that PIGT localizes near the nucleus in Drosophila. However, localizations of the other four subunits remain unknown. Here, we show that a catalytic subunit of GPI-T, PIGK, mainly localizes to the endoplasmic reticulum (ER), while the other four subunits localize to the nuclear envelope (NE) and ER. The NE/ER localization ratio of PIGS differs between cell types and developmental stages. Our results suggest that GPI-T catalyzes GPI attachment in the ER and the other four subunits may have other unknown functions in the NE.

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C‐kit mutations and PKC crosstalks: PKC translocates to nucleous only in cells HMC^560,816

Tobío¹,

Alfonso²,

Botana³

2011

J of Cellular Biochemistry

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The human mast cell lines HMC-1(560) and HMC-1(560,816) were used to study histamine release, Ca(2+) signaling and protein kinase C (PKC) localization and expression, with phorbol 12-myristate 13-acetate (PMA). Both sublines carry activating mutations in the proto-oncogene of c-kit that cause autophosphorylation and permanent c-kit tyrosine kinase activation. Both have the Gly-560 → Val mutation but only the second carries the Asp-816 → Val mutation. In this study, it was observed that the stimulation of PKC has different effects in HMC-1(560) and HMC-1(560,816) and this would be related to the difference in activating mutations in both mast cell lines. PKC activation increases ionomycin-induced histamine release in HMC-1(560) . This article demonstrates an opposite histamine response in HMC-1(560,816) cells, even though classical PKCs are the family of isozymes responsible for this effect in both cellular lines. Furthermore, it can be observed that upon cell stimulation with PMA, primarily cytosolic PKC translocates to the nucleous in HMC-1(560,816) cells, but not in HMC-1(560) cell line.

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PKCη is localized in the Golgi, ER and nuclear envelope and translocates to the nuclear envelope upon PMA activation and serum-starvation:

Cited by 49 publications

References 49 publications

Isoform-specific translocation of PKC isoforms in NIH3T3 cells by TPA

Isoform-specific translocation of PKC isoforms in NIH3T3 cells by TPA

Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila

C‐kit mutations and PKC crosstalks: PKC translocates to nucleous only in cells HMC^560,816

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PKCη is localized in the Golgi, ER and nuclear envelope and translocates to the nuclear envelope upon PMA activation and serum-starvation:

Cited by 49 publications

References 49 publications

Isoform-specific translocation of PKC isoforms in NIH3T3 cells by TPA

Isoform-specific translocation of PKC isoforms in NIH3T3 cells by TPA

Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila

C‐kit mutations and PKC crosstalks: PKC translocates to nucleous only in cells HMC560,816

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C‐kit mutations and PKC crosstalks: PKC translocates to nucleous only in cells HMC^560,816