A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2

Mitogen-activated protein kinases (MAPKs) are evolutionarily conserved signaling proteins involved in the regulation of most eukaryotic cellular processes. They are downstream components of essential signal transduction pathways activated by the external stimuli, in which the signal is conveyed thro...

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Bibliographic Details
Published in:International microbiology 2021-11, Vol.24 (4), p.531-543
Main Authors: González-Rubio, Gema, Sellers-Moya, Ángela, Martín, Humberto, Molina, María
Format: Article
Language:English
Subjects:
Applied Microbiology
Biomedical and Life Sciences
Cell Wall - metabolism
Cell walls
Eukaryotes
Eukaryotic Microbiology
External stimuli
Kinases
Life Sciences
MAP kinase
Medical Microbiology
Microbial Ecology
Microbiology
Mitogen-Activated Protein Kinases - genetics
Mitogen-Activated Protein Kinases - metabolism
Molecular structure
Phosphorylation
Protein kinase
Proteins
Review
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Signal processing
Signal Transduction
Signaling
Structure-function relationships
Transcription factors
Yeast
Yeasts
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Summary:Mitogen-activated protein kinases (MAPKs) are evolutionarily conserved signaling proteins involved in the regulation of most eukaryotic cellular processes. They are downstream components of essential signal transduction pathways activated by the external stimuli, in which the signal is conveyed through phosphorylation cascades. The excellent genetic and biochemical tractability of simple eukaryotes such as Saccharomyces cerevisiae has significantly contributed to gain fundamental information into the physiology of these key proteins. The budding yeast MAPK Slt2 was identified 30 years ago and was later revealed as a fundamental element of the cell wall integrity (CWI) pathway, one of the five MAPK routes of S. cerevisiae . As occurs with other MAPKs, whereas Slt2 displays the core typical structural traits of eukaryotic protein kinases, it also features conserved domains among MAPKs that allow an exquisite spatio-temporal regulation of their activity and binding to activating kinases, downregulatory phosphatases, or nuclear transcription factors. Additionally, Slt2 bears a regulatory extra C-terminal tail unique among S. cerevisiae MAPKs. Here, we review the structural and functional basis for the signaling role of Slt2 in the context of the molecular architecture of this important family of protein kinases.
ISSN:1139-6709
1618-1905
DOI:10.1007/s10123-021-00183-z