The role of UBR5 on Mitogen‐activated protein kinase (MAPK) signalling and muscle mass regulation in mice

The MEK5 [MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase 5]/ERK5 pathway is the least well studied MAPK signalling module. It has been proposed to play a role in the pathology of cancer. In the present paper, we review the role of the MEK5/ERK5 pathway using the ‘hallmarks of cancer’ as a framework and consider how this pathway is deregulated. As well as playing a key role in endothelial cell survival and tubular morphogenesis during tumour neovascularization, ERK5 is also emerging as a regulator of tumour cell invasion and migration. Several oncogenes can stimulate ERK5 activity, and protein levels are increased by a novel amplification at chromosome locus 17p11 and by down-regulation of the microRNAs miR-143 and miR-145. Together, these finding underscore the case for further investigation into understanding the role of ERK5 in cancer.

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Role of Phosphatidylinositol 3-Kinase (PI3K), Mitogen-Activated Protein Kinase (MAPK), and Protein Kinase C (PKC) in Calcium Signaling Pathways Linked to the α1-Adrenoceptor in Resistance Arteries

Frontiers in Physiology ◽

10.3389/fphys.2019.00055 ◽

2019 ◽

Vol 10 ◽

Cited By ~ 3

Author(s):

Alejandro Gutiérrez ◽

Cristina Contreras ◽

Ana Sánchez ◽

Dolores Prieto

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Calcium Signaling ◽

Signaling Pathways ◽

Mitogen Activated Protein Kinase ◽

Resistance Arteries ◽

Phosphatidylinositol 3 Kinase ◽

Kinase C ◽

Mitogen Activated Protein

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Exercise-induced mitogen-activated protein kinase signalling in skeletal muscle

Proceedings of The Nutrition Society ◽

10.1079/pns2004346 ◽

2004 ◽

Vol 63 (2) ◽

pp. 227-232 ◽

Cited By ~ 48

Author(s):

Yun Chau Long ◽

Ulrika Widegren ◽

Juleen R. Zierath

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Muscle Contraction ◽

Mitogen Activated Protein Kinase ◽

Mapk Cascades ◽

Extracellular Signal ◽

Mapk Signalling ◽

Mitogen Activated Protein ◽

Exercise Induced ◽

Response To Exercise

Exercise training improves glucose homeostasis through enhanced insulin sensitivity in skeletal muscle. Muscle contraction through physical exercise is a physiological stimulus that elicits multiple biochemical and biophysical responses and therefore requires an appropriate control network. Mitogen-activated protein kinase (MAPK) signalling pathways constitute a network of phosphorylation cascades that link cellular stress to changes in transcriptional activity. MAPK cascades are divided into four major subfamilies, including extracellular signal-regulated kinases 1 and 2, p38 MAPK, c-Jun NH2-terminal kinase and extracellular signal-regulated kinase 5. The present review will present the current understanding of parallel MAPK signalling in human skeletal muscle in response to exercise and muscle contraction, with an emphasis on identifying potential signalling mechanisms responsible for changes in gene expression.

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Role of p38 Mitogen-Activated Protein Kinase in Thrombus Formation

Journal of Receptors and Signal Transduction ◽

10.1081/rrs-200040324 ◽

2004 ◽

Vol 24 (4) ◽

pp. 283-296 ◽

Cited By ~ 25

Author(s):

Kanako Sakurai ◽

Yuji Matsuo ◽

Tatsuhiko Sudo ◽

Yoh Takuwa ◽

Sadao Kimura ◽

...

Keyword(s):

Protein Kinase ◽

Thrombus Formation ◽

Mitogen Activated Protein Kinase ◽

Mitogen Activated Protein

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Dual-mode regulation of the APC/C by CDK1 and MAPK controls meiosis I progression and fidelity

The Journal of Cell Biology ◽

10.1083/jcb.201305049 ◽

2014 ◽

Vol 204 (6) ◽

pp. 891-900 ◽

Cited By ~ 24

Author(s):

Ibtissem Nabti ◽

Petros Marangos ◽

Jenny Bormann ◽

Nobuaki R. Kudo ◽

John Carroll

Keyword(s):

Protein Kinase ◽

Spindle Assembly Checkpoint ◽

Mitogen Activated Protein Kinase ◽

Cyclin Dependent Kinase ◽

Anaphase Promoting Complex ◽

Female Meiosis ◽

Dual Mode ◽

Mitogen Activated Protein ◽

Meiosis I

Female meiosis is driven by the activities of two major kinases, cyclin-dependent kinase 1 (Cdk1) and mitogen-activated protein kinase (MAPK). To date, the role of MAPK in control of meiosis is thought to be restricted to maintaining metaphase II arrest through stabilizing Cdk1 activity. In this paper, we find that MAPK and Cdk1 play compensatory roles to suppress the anaphase-promoting complex/cyclosome (APC/C) activity early in prometaphase, thereby allowing accumulation of APC/C substrates essential for meiosis I. Furthermore, inhibition of MAPK around the onset of APC/C activity at the transition from meiosis I to meiosis II led to accelerated completion of meiosis I and an increase in aneuploidy at metaphase II. These effects appear to be mediated via a Cdk1/MAPK-dependent stabilization of the spindle assembly checkpoint, which when inhibited leads to increased APC/C activity. These findings demonstrate new roles for MAPK in the regulation of meiosis in mammalian oocytes.

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