Multiple biological responses activated by nuclear protein kinase C

Martelli, Alberto M.; Sang, Nianli; Borgatti, Paola; Capitani, Silvano; Neri, Luca M.

doi:10.1002/(sici)1097-4644(19990915)74:4<499::aid-jcb1>3.0.co;2-x

Cited by 93 publications

(37 citation statements)

References 165 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Studies from independent laboratories have led to the identification of quite few nuclear proteins which are PKC substrates and to the characterization of nuclear PKC-binding proteins which may be critical for fine-tuning PKC function in this cell microenvironment. Several lines of evidence suggest that nuclear PKC isozymes are involved in the regulation of biological processes as important as cell proliferation and differentiation, gene expression, neoplastic transformation, and apoptosis (interested readers should refer to [249, 254]). As mentioned above, certain PKCs also accumulate in mitochondria.…”

Section: Protein Kinase Cmentioning

confidence: 99%

Protein Kinases and Phosphatases in the Control of Cell Fate

et al. 2011

View full text Add to dashboard Cite

Protein phosphorylation controls many aspects of cell fate and is often deregulated in pathological conditions. Several recent findings have provided an intriguing insight into the spatial regulation of protein phosphorylation across different subcellular compartments and how this can be finely orchestrated by specific kinases and phosphatases. In this review, the focus will be placed on (i) the phosphoinositide 3-kinase (PI3K) pathway, specifically on the kinases Akt and mTOR and on the phosphatases PP2a and PTEN, and on (ii) the PKC family of serine/threonine kinases. We will look at general aspects of cell physiology controlled by these kinases and phosphatases, highlighting the signalling pathways that drive cell division, proliferation, and apoptosis.

show abstract

Section: Protein Kinase Cmentioning

confidence: 99%

Protein Kinases and Phosphatases in the Control of Cell Fate

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Almost all the isoforms of PKC have been identified at nuclear level, except for the PKCμ isoform [39,151]. The distinct functions of PKCs in the nucleus may be a consequence of either, the activity of resident isoforms of the enzyme or the translocation of PKC from cytoplasm to the nucleus, which may occur in certain conditions and in a different cellular system, as a result of nuclear lipid signaling [39].…”

Section: Pkc Phosphorylates Nox Subunits For Ros Generationmentioning

confidence: 99%

“…Moreover, nuclear PKCs have been implicated in cell proliferation, differentiation, apoptosis, and cardiovascular diseases [39,160]. For a complete review of nuclear PKCs and their function in cells see [39,151,161]. …”

Section: Pkc Phosphorylates Nox Subunits For Ros Generationmentioning

confidence: 99%

Cell Signaling through Protein Kinase C Oxidation and Activation

Cosentino-Gomes

Rocco-Machado

Meyer‐Fernandes

2012

IJMS

213

150

View full text Add to dashboard Cite

Due to the growing importance of cellular signaling mediated by reactive oxygen species (ROS), proteins that are reversibly modulated by these reactant molecules are of high interest. In this context, protein kinases and phosphatases, which act coordinately in the regulation of signal transduction through the phosphorylation and dephosphorylation of target proteins, have been described to be key elements in ROS-mediated signaling events. The major mechanism by which these proteins may be modified by oxidation involves the presence of key redox-sensitive cysteine residues. Protein kinase C (PKC) is involved in a variety of cellular signaling pathways. These proteins have been shown to contain a unique structural feature that is susceptible to oxidative modification. A large number of scientific studies have highlighted the importance of ROS as a second messenger in numerous cellular processes, including cell proliferation, gene expression, adhesion, differentiation, senescence, and apoptosis. In this context, the goal of this review is to discuss the mechanisms by which PKCs are modulated by ROS and how these processes are involved in the cellular response.

show abstract

“…It has been reported that overall PKC activity in homogenates of LLC‐PK 1 cells decreased during confluence in parallel with activation of SGLT1 transcription, whereas in confluent LLC‐PK 1 cells phorbol ester‐mediated activation of PKC suppressed transcription of SGLT1 (19,31). These data suggest that phosphorylation of serine 370 in pRS1 is mediated by a specific PKC subtype that can be activated by phorbol esters (32,33) and/or that the regulation of SGLT1 transcription differs in subconfluent versus confluent cells. We investigated how inhibitors and activators of PKC influence nuclear location of the fusion proteins GFP‐pRS1 and βGal‐ (CK2‐RNS‐PKC‐PKC)‐GFP in subconfluent LLC‐PK 1 cells.…”

Section: Resultsmentioning

confidence: 80%

Novel Shuttling Domain in a Regulator (RSC1A1) of Transporter SGLT1 Steers Cell Cycle‐Dependent Nuclear Location

Filatova

Leyerer

Gorboulev

et al. 2009

Traffic

View full text Add to dashboard Cite

The gene product of RSC1A1, RS1, participates in the regulation of the Na+‐d‐glucose cotransporter SGLT1. RS1 inhibits release of SGLT1 from the trans Golgi network. In subconfluent LLC‐PK1 cells, RS1 migrates into the nucleus and modulates transcription of SGLT1, whereas most confluent cells do not contain RS1 in the nuclei. We showed that confluence‐dependent nuclear location of RS1 is because of different phases of the cell cycle and identified a RS1 nuclear shuttling domain (RNS) with an associated protein kinase C (PKC) phosphorylation site (RNS‐PKC) that mediates cell cycle‐dependent nuclear location. RNS‐PKC contains a novel non‐conventional nuclear localization signal interacting with importin β1, a nuclear export signal mediating export via protein CRM1 and a Ca2+‐dependent calmodulin binding site. PKC and calmodulin compete for binding to RNS‐PKC. Mutagenesis experiments and analyses of the phosphorylation status suggest the following sequences of events. Subconfluent cells without and with synchronization to the G2/M phase contain non‐phosphorylated RNS‐PKC that mediates nuclear import of RS1 but not its export. During confluence or synchronization of subconfluent cells to the G2/M phase, phosphorylation of RNS‐PKC mediates rapid nuclear export of RS1.

show abstract

Multiple biological responses activated by nuclear protein kinase C

Cited by 93 publications

References 165 publications

Protein Kinases and Phosphatases in the Control of Cell Fate

Protein Kinases and Phosphatases in the Control of Cell Fate

Cell Signaling through Protein Kinase C Oxidation and Activation

Novel Shuttling Domain in a Regulator (RSC1A1) of Transporter SGLT1 Steers Cell Cycle‐Dependent Nuclear Location

Contact Info

Product

Resources

About