Cited by 35Protein Kinase Regulation and GTPase SignalingFungal and yeast genetics researchCellular transport and secretion

Localization of Ras signaling complex in budding yeast

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Belotti, Fiorella, Tisi, Renata, Paiardi, Chiara, Rigamonti, Marco, Groppi, Silvia, Martegani, Enzo·2012·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Abstract

In Saccharomyces cerevisiae, cAMP/pKA pathway plays a major role in metabolism, stress resistance and proliferation control. cAMP is produced by adenylate cyclase, which is activated both by Gpr1/Gpa2 system and Ras proteins, regulated by Cdc25/Sdc25 guanine exchange factors and Ira GTPase activator proteins. Recently, both Ras2 and Cdc25 RasGEF were reported to localize not only in plasma membrane but also in internal membranes. Here, the subcellular localization of Ras signaling complex proteins was investigated both by fluorescent tagging and by biochemical cell membrane fractionation on sucrose gradients. Although a consistent minor fraction of Ras signaling complex components was found in plasma membrane during exponential growth on glucose, Cdc25 appears to localize mainly on ER membranes, while Ira2 and Cyr1 are also significantly present on mitochondria. Moreover, PKA Tpk1 catalytic subunit overexpression induces Ira2 protein to move from mitochondria to ER membranes. These data confirm the hypothesis that different branches of Ras signaling pathways could involve different subcellular compartments, and that relocalization of Ras signaling complex components is subject to PKA control.

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Crossref · 10.1016/j.bbamcr.2012.04.016

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  • In S. cerevisiae, Ira2 interacts with the protein kinase A regulatory subunit, and Cyr1 and Ira2 have both been found at the plasma membrane and on mitochondria.

    “In S. cerevisiae, Ira2 has been shown to interact with the protein kinase A regulatory subunit, and Cyr1 and Ira2 have both been found at the plasma membrane and on mitochondria [78]”

    From Mitochondrial Activity and Cyr1 Are Key Regulators of Ras1 Activation of C. albicans Virulence Pathways (2015) · cites this paper as [78]

    The Results and Discussion report that Cyr1 and Ira2 occur on mitochondria and that a minor fraction of both is associated with plasma-membrane fractions. They do not report an interaction between Ira2 and the PKA regulatory subunit; the PKA experiments instead concern overexpression of the catalytic subunit Tpk1. (LLM, conf=0.88)

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Authors
Belotti, F., Tisi, R., Paiardi, C., Rigamonti, M., Groppi, S., & Martegani, E.
Affiliations
University of Milano-Bicocca (IT)
Corresponding author
Martegani, Enzo
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2012-07
Volume
1823
Issue
7
Pages
1208-1216
ISSN
0167-4889 (ISSN-L)
OpenAlex
W1985464808
Cited by
35
References
59
Citations by year
2025: 2 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 4 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 6 · 2013: 2 · 2012: 1
FWCI
1.41
Type
journal article
Language
en
Open access
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
  • PubMed (publishedVersion)
  • BOA (University of Milano-Bicocca) (submittedVersion)
Funders
UNICELLSYS
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
subcellular localization, Saccharomyces cerevisiae, cAMP/PKA signaling, RAS2, Cdc25, IRA2, CYR1, TPK1, plasma membrane, endoplasmic reticulum membrane, mitochondria, guanine nucleotide exchange factor, adenylate cyclase, protein relocalization
MeSH terms
Endoplasmic Reticulum, Guanosine Diphosphate, Guanosine Triphosphate, Saccharomyces cerevisiae, Signal Transduction, Cyclic AMP-Dependent Protein Kinases, ras Proteins, Catalytic Domain, Protein Transport, Saccharomyces cerevisiae Proteins, Multiprotein Complexes, Mitochondrial Membranes

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