Diacylglycerol-evoked activation of PKC and PKD isoforms in regulation of glucose and lipid metabolism: a review

There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

Abstract

Protein kinase C (PKC) and Protein kinase D (PKD) isoforms can sense diacylglycerol (DAG) generated in the different cellular compartments in various physiological processes. DAG accumulates in multiple organs of the obese subjects, which leads to the disruption of metabolic homeostasis and the development of diabetes as well as associated diseases. Multiple studies proved that aberrant activation of PKCs and PKDs contributes to the development of metabolic diseases. DAG-sensing PKC and PKD isoforms play a crucial role in the regulation of metabolic homeostasis and therefore might serve as targets for the treatment of metabolic disorders such as obesity and diabetes.

Related collections

Most cited references 171

Record: found
Abstract: found
Article: not found

Signaling pathways in skeletal muscle remodeling.

Rhonda Bassel-Duby, Eric Olson (2006)

Skeletal muscle is comprised of heterogeneous muscle fibers that differ in their physiological and metabolic parameters. It is this diversity that enables different muscle groups to provide a variety of functional properties. In response to environmental demands, skeletal muscle remodels by activating signaling pathways to reprogram gene expression to sustain muscle performance. Studies have been performed using exercise, electrical stimulation, transgenic animal models, disease states, and microgravity to show genetic alterations and transitions of muscle fibers in response to functional demands. Various components of calcium-dependent signaling pathways and multiple transcription factors, coactivators and corepressors have been shown to be involved in skeletal muscle remodeling. Understanding the mechanisms involved in modulating skeletal muscle phenotypes can potentiate the development of new therapeutic measures to ameliorate muscular diseases.

0 comments Cited 214 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation.

T McKinsey, C. Zhang, J. Lu … (2000)

Members of the myocyte enhancer factor-2 (MEF2) family of transcription factors associate with myogenic basic helix-loop-helix transcription factors such as MyoD to activate skeletal myogenesis. MEF2 proteins also interact with the class II histone deacetylases HDAC4 and HDAC5, resulting in repression of MEF2-dependent genes. Execution of the muscle differentiation program requires release of MEF2 from repression by HDACs, which are expressed constitutively in myoblasts and myotubes. Here we show that HDAC5 shuttles from the nucleus to the cytoplasm when myoblasts are triggered to differentiate. Calcium/calmodulin-dependent protein kinase (CaMK) signalling, which stimulates myogenesis and prevents formation of MEF2-HDAC complexes, also induces nuclear export of HDAC4 and HDAC5 by phosphorylation of these transcriptional repressors. An HDAC5 mutant lacking two CaMK phosphorylation sites is resistant to CaMK-mediated nuclear export and acts as a dominant inhibitor of skeletal myogenesis, whereas a cytoplasmic HDAC5 mutant is unable to block efficiently the muscle differentiation program. Our results highlight a mechanism for transcriptional regulation through signal- and differentiation-dependent nuclear export of a chromatin-remodelling enzyme, and suggest that nucleo-cytoplasmic trafficking of HDACs is involved in the control of cellular differentiation.

0 comments Cited 185 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism.

Renate Schreiber, Christian Fledelius, Rudolf Zechner … (2006)

The mobilization of free fatty acids from adipose triacylglycerol (TG) stores requires the activities of triacylglycerol lipases. In this study, we demonstrate that adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL) are the major enzymes contributing to TG breakdown in in vitro assays and in organ cultures of murine white adipose tissue (WAT). To differentiate between ATGL- and HSL-specific activities in cytosolic preparations of WAT and to determine the relative contribution of these TG hydrolases to the lipolytic catabolism of fat, mutant mouse models lacking ATGL or HSL and a mono-specific, small molecule inhibitor for HSL (76-0079) were used. We show that 76-0079 had no effect on TG catabolism in HSL-deficient WAT but, in contrast, essentially abolished free fatty acid mobilization in ATGL-deficient fat. CGI-58, a recently identified coactivator of ATGL, stimulates TG hydrolase activity in wild-type and HSL-deficient WAT but not in ATGL-deficient WAT, suggesting that ATGL is the sole target for CGI-58-mediated activation of adipose lipolysis. Together, ATGL and HSL are responsible for more than 95% of the TG hydrolase activity present in murine WAT. Additional known or unknown lipases appear to play only a quantitatively minor role in fat cell lipolysis.

0 comments Cited 173 times – based on 0 reviews      Review now

Bookmark

All references

Author and article information

Contributors

Grzegorz Sumara:

ORCID: http://orcid.org/0000-0003-1502-6265

g.sumara@nencki.edu.pl

Journal

Journal ID (nlm-ta): Lipids Health Dis

Journal ID (iso-abbrev): Lipids Health Dis

Title: Lipids in Health and Disease

Publisher: BioMed Central (London )

ISSN (Electronic): 1476-511X

Publication date (Electronic): 28 May 2020

Publication date PMC-release: 28 May 2020

Publication date Collection: 2020

Volume: 19

Electronic Location Identifier: 113

Affiliations

GRID grid.419305.a, ISNI 0000 0001 1943 2944, Nencki Institute of Experimental Biology, Polish Academy of Sciences, ; 3 Pasteur Street, 02-093 Warszawa, Poland

Author information

Grzegorz Sumara http://orcid.org/0000-0003-1502-6265

Article

Publisher ID: 1286

DOI: 10.1186/s12944-020-01286-8

PMC ID: 7257441

PubMed ID: 32466765

SO-VID: ebbdc449-f5c8-42b5-aeb9-5ab2f592de51

License:

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

History

Date received : 18 March 2020

Date accepted : 14 May 2020

Funding

Funded by: FundRef http://dx.doi.org/10.13039/100010663, H2020 European Research Council;

Award ID: 678119 - SiCMetabol

Award Recipient : Grzegorz Sumara

Funded by: Polish Ministry of Science and Higher Education (MNiSW)

Award ID: Dioscuri Centre of Scientific Excellence

Award Recipient : Grzegorz Sumara

Funded by: FundRef http://dx.doi.org/10.13039/100004410, European Molecular Biology Organization;

Award ID: EMBO Installation Grant 2020 - GSumara

Award Recipient : Grzegorz Sumara

Custom metadata

ScienceOpen disciplines: Biochemistry

Keywords: diacylglycerol (dag) ,pkc ,pkd ,metabolism ,insulin signaling

Data availability:

ScienceOpen disciplines: Biochemistry

Keywords: diacylglycerol (dag) , pkc , pkd , metabolism , insulin signaling

Comments

Comment on this article

scite_

Cited by 29

See all cited by

Most referenced authors 5,130

See all reference authors

Diacylglycerol-evoked activation of PKC and PKD isoforms in regulation of glucose and lipid metabolism: a review

Read this article at

Abstract

Related collections

Journal of Circulating Biomarkers

Most cited references 171

Signaling pathways in skeletal muscle remodeling.

Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation.

Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism.

Author and article information

Contributors

Journal

Affiliations

Author information

Article

History

Funding

Categories

Custom metadata

Comments

Comment on this article

Similar content 431

Cited by 29

Most referenced authors 5,130