Dephosphorylation of cofilin is regulated through Ras and requires the combined activities of the Ras-effectors MEK and PI3K
Remodeling of the actin cytoskeleton is crucial for a multitude of cellular functions including cell movement, intracellular transport as well as signal transduction and gene expression processes. Cofilin has been identified as a key mediator of actin reorganization. Its activity is regulated via re...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2004
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| In: |
Cellular signalling
Year: 2004, Volume: 16, Issue: 2, Pages: 235-243 |
| ISSN: | 1873-3913 |
| DOI: | 10.1016/s0898-6568(03)00133-5 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: http://dx.doi.org/10.1016/s0898-6568(03)00133-5 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0898656803001335 |
| Author Notes: | Gabriele Nebl, Sabine Fischer, Roland Penzel, Yvonne Samstag |
| Summary: | Remodeling of the actin cytoskeleton is crucial for a multitude of cellular functions including cell movement, intracellular transport as well as signal transduction and gene expression processes. Cofilin has been identified as a key mediator of actin reorganization. Its activity is regulated via reversible phosphorylation of ser-3. In a variety of cell types stimulation through particular surface receptors fastly induces the dephosphorylation/activation of cofilin. Yet, the signal transduction cascades linking receptor stimulation with cofilin activation have not been identified so far. Here we show that the GTPase Ras acts as a central regulator of the cofilin dephosphorylation pathway. Thus, stimulation of Ras through platelet-derived growth factor (PDGF) or transient expression of activated Ras-proteins induces the dephosphorylation of cofilin. Importantly, the cooperation of two Ras-initiated signaling pathways is required to induce cofilin dephosphorylation: a Ras-Raf-MAPkinase/Erk-kinase (MEK)- and a Ras-phosphatidylinositol-3-kinase (PI3K)-effector cascade. |
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| Item Description: | Gesehen am 22.02.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1873-3913 |
| DOI: | 10.1016/s0898-6568(03)00133-5 |