Variants of the yeast MAPK Mpk1 are fully functional independently of activation loop phosphorylation

• Published in: Molecular biology of the cell Vol. 27; no. 17; pp. 2771 - 2783
• Main Authors: Goshen-Lago, Tal, Goldberg-Carp, Anat, Melamed, Dganit, Darlyuk-Saadon, Ilona, Bai, Chen, Ahn, Natalie G, Admon, Arie, Engelberg, David
• Format: Journal Article
• Language: English
• Published: United States The American Society for Cell Biology 01.09.2016
• Subjects: 3T3 Cells; Amino Acid Motifs; Amino Acid Sequence; Animals; Cell Culture Techniques; Cell Wall - metabolism; Extracellular Signal-Regulated MAP Kinases - metabolism; HEK293 Cells; Humans; MAP Kinase Signaling System; Mice; Mitogen-Activated Protein Kinase Kinases - metabolism; Mitogen-Activated Protein Kinases - genetics; Mitogen-Activated Protein Kinases - metabolism; Mutation; Phosphorylation; Protein-Serine-Threonine Kinases - metabolism; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Signal Transduction - physiology

MAP kinases of the ERK family are conserved from yeast to humans. Their catalytic activity is dependent on dual phosphorylation of their activation loop's TEY motif, catalyzed by MAPK kinases (MEKs). Here we studied variants of Mpk1, a yeast orthologue of Erk, which is essential for cell wall i...