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

  1. Gema González Rubio 1
  2. Ángela Sellers Moya 1
  3. Humberto Martín Brieva 1
  4. María Molina Martín 1
  1. 1 Universidad Complutense de Madrid
    info

    Universidad Complutense de Madrid

    Madrid, España

    ROR 02p0gd045

Journal:
International microbiology: official journal of the Spanish Society for Microbiology

ISSN: 1618-1905

Year of publication: 2021

Volume: 24

Issue: 2

Pages: 1

Type: Article

More publications in: International microbiology: official journal of the Spanish Society for Microbiology

Metrics

JCR (Journal Impact Factor)

  • Year 2021
  • Journal Impact Factor: 3.097
  • Journal Impact Factor without self cites: 3.081
  • Article influence score: 0.494
  • Best Quartile: Q3
  • Area: MICROBIOLOGY Quartile: Q3 Rank in area: 90/137 (Ranking edition: SCIE)
  • Area: BIOTECHNOLOGY & APPLIED MICROBIOLOGY Quartile: Q3 Rank in area: 101/159 (Ranking edition: SCIE)

SCImago Journal Rank

  • Year 2021
  • SJR Journal Impact: 0.559
  • Best Quartile: Q3
  • Area: Microbiology Quartile: Q3 Rank in area: 99/165
  • Area: Microbiology (medical) Quartile: Q3 Rank in area: 70/127

Scopus CiteScore

  • Year 2021
  • CiteScore of the Journal : 4.3
  • Area: Microbiology (medical) Percentile: 51
  • Area: Microbiology Percentile: 39

Journal Citation Indicator (JCI)

  • Year 2021
  • Journal Citation Indicator (JCI): 0.5
  • Best Quartile: Q3
  • Area: BIOTECHNOLOGY & APPLIED MICROBIOLOGY Quartile: Q3 Rank in area: 116/168
  • Area: MICROBIOLOGY Quartile: Q3 Rank in area: 110/158

Abstract

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.