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A dysregulation of Ras-signaling has been found to be causative for the development of diseases, such as diverse cancer types, RASopathies, neurodegenerative diseases and ciliopathies. Ras-proteins cycle between a GTP-bound on-state and a GDP-bound off-state. Ras-proteins show low intrinsic rates for nucleotide exchange and nucleotide hydrolysis. They need guanine-nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) to accelerate both functions in order to act as true molecular switches in the physiological context. Ras-proteins and their regulators\/effectors are targets of post-translational modifications (PTMs) such as phosphorylation, ac(et)ylation, lipidation and ubiquitination. These PTMs regulate their activity, subcellular localization and turnover. In a biological perspective, PTMs are essential components for cellular signaling cascades and for molecular pattern formation. Bacterial pathogens use PTMs of Ras-proteins to allow efficient infection processes. Besides, modifications of Ras-proteins were shown to be of therapeutic potential in oncogenic variants such as Ras G12C. In this review, we summarize current knowledge on Ras-signaling, while emphasizing PTMs as dynamic signaling hubs for its precise spatiotemporal control.<\/jats:p>","DOI":"10.1515\/hsz-2025-0243","type":"journal-article","created":{"date-parts":[[2026,5,9]],"date-time":"2026-05-09T18:09:12Z","timestamp":1778350152000},"page":"25-66","source":"Crossref","is-referenced-by-count":3,"title":["Mechanistic insights on spatiotemporal control of Ras-signaling"],"prefix":"10.1515","volume":"407","author":[{"given":"Clotilde","family":"Charrier","sequence":"first","affiliation":[{"name":"Department of Synthetic and Structural Biochemistry , 425811 Institute of Biochemistry, University of Greifswald , Felix-Hausdorff-Str. 4, D-17489 Greifswald , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sascha","family":"Mrachacz","sequence":"additional","affiliation":[{"name":"Department of Synthetic and Structural Biochemistry , 425811 Institute of Biochemistry, University of Greifswald , Felix-Hausdorff-Str. 4, D-17489 Greifswald , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sabrina","family":"Schulze","sequence":"additional","affiliation":[{"name":"Department of Synthetic and Structural Biochemistry , 425811 Institute of Biochemistry, University of Greifswald , Felix-Hausdorff-Str. 4, D-17489 Greifswald , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4168-4640","authenticated-orcid":false,"given":"Michael","family":"Lammers","sequence":"additional","affiliation":[{"name":"Department of Synthetic and Structural Biochemistry , 425811 Institute of Biochemistry, University of Greifswald , Felix-Hausdorff-Str. 4, D-17489 Greifswald , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2026,5,4]]},"reference":[{"key":"2026050919420542880_j_hsz-2025-0243_ref_001","doi-asserted-by":"crossref","unstructured":"Abankwa, D., Gorfe, A.A., Inder, K., and Hancock, J.F. 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