ERK and p38 MAPK-Activated Protein Kinases: a Family of Protein Kinases with Diverse Biological Functions

By Philippe P Roux, J. Blenis. Microbiology and Molecular Biology Reviews, 2004

2,565 citations recorded by the source corpus.

Subfields: Molecular Biology, Pathology and Forensic Medicine

View Paper: https://www.semanticscholar.org/paper/2ed2632971630a65f308121d712f30ff6173bf3f

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In Molecular Biology

1. R. Seger
2. J. Blenis
3. R. Anjum
4. Yoav D. Shaul
5. Austin G Smith
6. Jason Wray
7. S. Meloche
8. E. Jacinto

In Pathology and Forensic Medicine

1. R. Seger
2. Yoav D. Shaul
3. J. Blenis

Citations in the corpus

• Translational control of long-lasting synaptic plasticity and memory. (2009, neutral): “ERK can also impact mTOR function further downstream by phosphosphorylating TSC2 either directly or indirectly via RSK (Ma et al., 2005; Roux and Blenis, 2004).”
• p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage. (2007, background): “In contrast to the DNA-damage-specific activation of Chk1 and Chk2, the p38MAPK pathway is a general stress-activated kinase pathway that responds to various cellular stimuli, including cytokines, hyperosmolarity, and UV irradiation (Roux and Blenis, 2004).”
• Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival (2008, background): “tyrosine (TGY) sequence in the activation domain of the kinase (4, 35, 43).”
• The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions (2006, background): “Finally, asides from the RSK1/2 in the MAPKAPK tier, ERKs can also phosphorylate and activate also RSK3/4 (Roux and Blenis 2004), mitogen- and stress-activated kinase (MSK; (Deak et al.”
• SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. (2006, background): “TSC2 is also phosphorylated and inactivated by other kinases such as AMPK, ERK1/2, and RSK at sites other than the Akt target residues to positively regulate TORC1 signaling (Inoki et al., 2003; Ma et al., 2005; Roux and Blenis, 2004).”
• Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease. (2009, background): “When phosphorylated, ERK1/2 dissociates from MEK1 and translocates to the nucleus, where it phosphorylates a number of substrates (SRC-1, Pax6, NF-AT, Elk-1, MEF2, c-Fos, c-Myc, and STAT3) involved in the activation of a complex transcriptional program (120, 121).”
• The RSK family of kinases: emerging roles in cellular signalling (2008, background): “1 ) and two structurally related homologues, RSK-like protein kinase ( RLPK ; also known as mitogen- and stress-activated kinase-1 (MSK1)) and RSKB (also known as MSK2”
• Signal transduction in cancer. (2015, background): “Multiple kinases in the ribosomal S6 kinase (RSK), mitogen- and stress-activated kinase (MSK), and mitogen-activated protein kinase (MAPK)-interacting kinase (MNK) families are also phosphorylated by ERK, and these kinases, in turn, phosphorylate transcription factors that regulate cell cycle progre”
• The MEK/ERK cascade: from signaling specificity to diverse functions. (2007, background): “Finally, MAPKAPK3 [80], and MK5 [81] are only slightly activated by ERKs, as they are more responsive to p38s [82].”
• p38 MAP-kinases pathway regulation, function and role in human diseases. (2007, background): “2, these have been shown to be transcription factors, other protein kinases which in turn phosphorylate transcription factors, cytoskeletal proteins, and translational machinery components, and other proteins such as metabolic enzyme, glycogen synthase or cytosolic phospholipase A2 [30,32,83].”