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Article

Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking.

The Journal of biological chemistry - 13 Jul 2001

Xu Be, Stippec S, Robinson F L, Cobb M H

Abstract excerpt

Docking between MEK1 and ERK2 is required for their stable interaction and efficient signal transmission. The MEK1 N terminus contains the ERK docking or D domain that consists of conserved hydrophobic and basic residues. We mutated the hydrophobic and basic residues individually and found that loss of either type reduced MEK1 phosphorylation of ERK2 in vitro and its ability to bind to ERK2 in vivo. Moreover,...

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Source

Identifiers

PMID: 11352917
DOI: 10.1074/jbc.M102769200

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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