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Article

Dual role for membrane localization in yeast MAP kinase cascade activation and its contribution to signaling fidelity.

Current biology : CB - 21 Mar 2006

Lamson Rachel E, Takahashi Satoe, Winters Matthew J, Pryciak Peter M

Abstract excerpt

Distinct MAP kinase pathways in yeast share several signaling components , including the PAK Ste20 and the MAPKKK Ste11, yet signaling is specific. Mating pheromones trigger an initial step in which Ste20 activates Ste11 , and this requires plasma membrane recruitment of the MAP kinase cascade scaffold protein, Ste5 . Here, we demonstrate an additional role for Ste5 membrane localization. Once Ste11 is activated,...

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Identifiers

PMID: 16546088
DOI: 10.1016/j.cub.2006.02.060

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Dual role for membrane localization in yeast MAP kinase cascade activation and its contribution to signaling fidelity.PMID 16546088Read ↗

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Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade.Semantic proximity Read ↗

New Features Surrounding the Cdc42-Ste20 Module that Regulates MAP Kinase Signaling in YeastSemantic proximity Read ↗

Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7.Semantic proximity Read ↗

Control of MAPK signaling specificity by a conserved residue in the MEK-binding domain of the yeast scaffold protein Ste5.Semantic proximity Read ↗

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Function of the MAPK scaffold protein, Ste5, requires a cryptic PH domain.Semantic proximity Read ↗

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