Snf1 protein kinase: a key player in the response to cellular stress in yeast

Sucrose non-fermenting 1 (Snf1) protein kinase, a yeast homologue of mammalian AMP-activated protein kinase, plays a main role in transcriptional activation and repression of gene expression. In addition, Snf1 kinase has a broad role in the cellular response to several forms of stress, such as nutrient limitation, salt stress and heat shock.

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Stimulation of GCMa Transcriptional Activity by Cyclic AMP/Protein Kinase A Signaling Is Attributed to CBP-Mediated Acetylation of GCMa

Molecular and Cellular Biology ◽

10.1128/mcb.25.19.8401-8414.2005 ◽

2005 ◽

Vol 25 (19) ◽

pp. 8401-8414 ◽

Cited By ~ 66

Author(s):

Ching-Wen Chang ◽

Hsiao-Ching Chuang ◽

Chenchou Yu ◽

Tso-Pang Yao ◽

Hungwen Chen

Keyword(s):

Gene Expression ◽

Protein Kinase ◽

Cyclic Amp ◽

Protein Kinase A ◽

Transcriptional Activation ◽

Transcriptional Activity ◽

Camp Signaling ◽

Transactivation Domain ◽

Dependent Protein ◽

Kinase A

ABSTRACT Human GCMa is a zinc-containing transcription factor primarily expressed in placenta. GCMa regulates expression of syncytin gene, which encodes for a placenta-specific membrane protein that mediates trophoblastic fusion and the formation of syncytiotrophoblast layer required for efficient fetal-maternal exchange of nutrients and oxygen. The adenylate cyclase activator, forskolin, stimulates syncytin gene expression and cell fusion in cultured placental cells. Here we present evidence that cyclic AMP (cAMP) signaling pathway activates the syncytin gene expression by regulating GCMa activity. We found that forskolin and protein kinase A (PKA) enhances GCMa-mediated transcriptional activation. Furthermore, PKA treatment stimulates the association of GCMa with CBP and increases GCMa acetylation. CBP primarily acetylates GCMa at lysine367, lysine406, and lysine409 in the transactivation domain (TAD). We found that acetylation of these residues is required to protect GCMa from ubiquitination and increases the TAD stability with a concomitant increase in transcriptional activity, supporting the importance of acetylation in PKA-dependent GCMa activation. Our results reveal a novel regulation of GCMa activity by cAMP-dependent protein acetylation and provide a molecular mechanism by which cAMP signaling regulates trophoblastic fusion.

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AMP-activated protein kinase: a remarkable contributor to preserve a healthy heart against ROS injury

Free Radical Biology and Medicine ◽

10.1016/j.freeradbiomed.2021.02.047 ◽

2021 ◽

Author(s):

Alice Marino ◽

Derek J. Hausenloy ◽

Ioanna Andreadou ◽

Sandrine Horman ◽

Luc Bertrand ◽

...

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Amp Activated Protein Kinase ◽

Kinase A

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Pituitary adenylate cyclase-activating polypeptide stimulates both c-fos gene expression and cell survival in rat cerebellar granule neurons through activation of the protein kinase A pathway

Neuroscience ◽

10.1016/s0306-4522(97)00545-9 ◽

1998 ◽

Vol 84 (3) ◽

pp. 801-812 ◽

Cited By ~ 81

Author(s):

D Vaudry ◽

B.J Gonzalez ◽

M Basille ◽

Y Anouar ◽

A Fournier ◽

...

Keyword(s):

Gene Expression ◽

Protein Kinase ◽

Adenylate Cyclase ◽

Cell Survival ◽

Protein Kinase A ◽

Cerebellar Granule Neurons ◽

Granule Neurons ◽

Cerebellar Granule ◽

Pituitary Adenylate Cyclase ◽

Kinase A

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FSH and LH Stimulation of Granulosa Cell Prodynorphin Gene Expression Abolished by Overexpression of a Nonfunctional Mutant of the RI Subunit of Protein Kinase A

Follicle Stimulating Hormone ◽

10.1007/978-1-4684-7103-8_35 ◽

1992 ◽

pp. 356-363

Author(s):

Alan H. Kaynard ◽

Cynthia T. McMurray ◽

James Douglass ◽

Michael H. Melner

Keyword(s):

Gene Expression ◽

Protein Kinase ◽

Protein Kinase A ◽

Granulosa Cell ◽

Prodynorphin Gene Expression ◽

Kinase A ◽

Stimulation Of

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Dilation of Porcine Retinal Arterioles to Cilostazol: Roles of eNOS Phosphorylation via cAMP/Protein Kinase A and AMP-Activated Protein Kinase and Potassium Channels

Investigative Opthalmology & Visual Science ◽

10.1167/iovs.12-10115 ◽

2013 ◽

Vol 54 (2) ◽

pp. 1443 ◽

Cited By ~ 13

Author(s):

Ichiro Tanano ◽

Taiji Nagaoka ◽

Tsuneaki Omae ◽

Akihiro Ishibazawa ◽

Takayuki Kamiya ◽

...

Keyword(s):

Protein Kinase ◽

Potassium Channels ◽

Protein Kinase A ◽

Retinal Arterioles ◽

Enos Phosphorylation ◽

Amp Activated Protein Kinase ◽

Kinase A

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Synergistic effects of cAMP–dependent protein kinase A and AMP-activated protein kinase on lipolysis in kinsenoside-treated C3H10T1/2 adipocytes

Phytomedicine ◽

10.1016/j.phymed.2018.06.043 ◽

2019 ◽

Vol 55 ◽

pp. 255-263 ◽

Cited By ~ 1

Author(s):

Yuan-Chii G. Lee ◽

Yuh-Mou Sue ◽

Ching-Kuo Lee ◽

Huei-Mei Huang ◽

Jhin-Jyun He ◽

...

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Synergistic Effects ◽

Dependent Protein Kinase ◽

Camp Dependent Protein Kinase ◽

Dependent Protein ◽

Amp Activated Protein Kinase ◽

Kinase A

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High glucose-associated osmolality promotes adipocytogenic differentiation of primary rat osteoblasts in a protein kinase A and phosphatidylinositol 3-kinase/Akt-dependent manner

Biologia ◽

10.1515/biolog-2015-0156 ◽

2015 ◽

Vol 70 (10) ◽

Author(s):

Yu Zhang ◽

Pu Feng ◽

Jianhong Yang

Keyword(s):

Gene Expression ◽

Protein Kinase ◽

Protein Kinase A ◽

Real Time ◽

High Glucose ◽

Marker Gene ◽

Dependent Manner ◽

Phosphatidylinositol 3 Kinase ◽

Marker Gene Expression ◽

Kinase A

AbstractIncreased risk of osteoporosis in patients with diabetes mellitus may be related to hyperglycemia. However, the potential mechanisms accounting for diabetic bone disorder remain unresolved. The present study investigated the effects of high glucose-associated osmolality on differentiation of primary rat calvarial osteoblasts. Osteoblastogenic differentiation was determined by bone nodule staining for mineralization assay, enzyme-linked immunosorbent assay for type I collagen production and real-time polymerase chain reaction (PCR) for osteoblastogenic marker gene expression. Adipocytogenic differentiation was assessed by oil red O staining for lipid accumulation and real-time PCR for adipocytogenic marker gene expression. The phosphorylations of protein kinase A (PKA) and Akt were measured with or without specific inhibitors to confirm osmolality involved signalling pathways. The results showed that high glucose-associated osmolality significantly promoted adipocytogenic differentiation, manifested by increased lipid droplet formation and gene expression of adipocytogenic markers including adipocyte fatty acid binding protein (aP2), adipsin and peroxisome proliferator-activated receptor gamma (PPARγ). Meanwhile, high glucose-associated osmolality inhibited osteoblastogenic differentiation, characterized by decreased collagen I protein production and cell mineralization, as well as gene expression of osteoblastogenic markers including collagen I, osteocalcin and runt-related transcription factor 2 (Runx2). More importantly, we demonstrated for the first time that high glucose-associated osmolality induced adipocytogenic differentiation and suppressed osteoblastogenic differentiation in a PKA and phosphatidylinositol 3-kinase (PI3K)/Akt-dependent manner. These results indicated that osmolality was involved in high glucose-induced osteoblast trans-differentiation into adipocyte-like cell and suppression of cellular osmolality could provide novel therapeutic approach for diabetic osteopenia.

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