Abstract 4308: Phosphatidic acid binds to ERK3 and stimulates phosphorylation of the ERK3 activation loop
| Autor: | Amanda Myers, Hitham Aldharee, Shimpi Bedi, Weiwen Long |
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| Rok vydání: | 2019 |
| Předmět: | |
| Zdroj: | Cancer Research. 79:4308-4308 |
| ISSN: | 1538-7445 0008-5472 |
| DOI: | 10.1158/1538-7445.am2019-4308 |
| Popis: | Protein kinases modulate the activity of other proteins through phosphorylation and themselves are often regulated by phosphorylation of their activation loop. Extracellular signal-Regulated Kinase 3 (ERK3) is an atypical member of the ERK family of Mitogen-Activated Protein Kinases (MAPK), with a SerGlu-Gly (SEG) motif in its activation loop rather than the canonical Thr-Xaa-Tyr (TXY) motif of ERK1/2. Activation loop phosphorylation of ERK3 is not regulated by the signals known to activate ERK1/2, such as mitogenic growth factors. The cellular stimuli activating ERK3 kinase are virtually unknown. Some kinases, including mTOR and p21 activated kinase 1 and 2 (PAK1/2), are stimulated by binding to certain phospho-lipid signaling molecules, such as phosphatidic acids. Here, we show ERK3 binds to specific phospholipids in vitro, and the C-terminal domain may be important for this interaction. In addition, ERK3 can localize to the cell membrane. Further, phosphatidic acid stimulated phosphorylation of the activation loop in ERK3. Together, these results suggest that ERK3 kinase activity might be upregulated by specific phosphatidic acid species in cells. Citation Format: Amanda Myers, Hitham Aldharee, Shimpi Bedi, Weiwen Long. Phosphatidic acid binds to ERK3 and stimulates phosphorylation of the ERK3 activation loop [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 4308. |
| Databáze: | OpenAIRE |
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