Abstract
The survival of eukaryotic organisms during environmental changes is largely dependent on the adaptive responses elicited by signal transduction cascades, including those regulated by the Mitogen-Activated Protein Kinase (MAPK) pathways. The Cell Integrity Pathway (CIP), one of the three MAPK pathways found in the simple eukaryote fission of yeast Schizosaccharomyces pombe, shows strong homology with mammalian Extracellular signal-Regulated Kinases (ERKs). Remarkably, studies over the last few decades have gradually positioned the CIP as a multi-faceted pathway that impacts multiple functional aspects of the fission yeast life cycle during unperturbed growth and in response to stress. They include the control of mRNA-stability through RNA binding proteins, regulation of calcium homeostasis, and modulation of cell wall integrity and cytokinesis. Moreover, distinct evidence has disclosed the existence of sophisticated interplay between the CIP and other environmentally regulated pathways, including Stress-Activated MAP Kinase signaling (SAPK) and the Target of Rapamycin (TOR). In this review we present a current overview of the organization and underlying regulatory mechanisms of the CIP in S. pombe, describe its most prominent functions, and discuss possible targets of and roles for this pathway. The evolutionary conservation of CIP signaling in the dimorphic fission yeast S. japonicus will also be addressed.
Highlights
MAPK kinase kinase (MAPKKK) are usually activated through phosphorylation in response to environmental changes by upstream signaling cascades composed by GTPases of the Rho or Ras families together with different kinases, they can become activated through oligomerization or changes in subcellular location
Cell Integrity Pathway (CIP) signaling is involved in the regulation of essential cellular processes in fission yeast, such as the RNA binding proteins (RBPs)-mediated control of mRNA-stability, ionic homeostasis, cell wall (CW) integrity, and cytokinesis
Studies completed during the last 30 years have depicted the complexity and pleiotropism of environmentally controlled CIP signaling during the fission yeast life cycle, which is likely due to the existence of a wide number of effector substrates
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The highly conserved Mitogen Activated Protein Kinase (MAPK) pathways are specialized signal transduction cascades that detect environmental signals at the cell surface, which are transmitted to a set of downstream cytoplasmic and nuclear effectors to control multiple aspects of cell function, including metabolism, division, death, differentiation, and movement [1,2,3]. MAPKs of the ERK group are activated in response to mitogenic signals elicited by growth factors and phorbol esters and regulate several aspects of cellular functions including proliferation, survival, growth, metabolism, migration, and differentiation in response to extracellular cues [10]. In this review we present an exhaustive and updated description of the organization, components, and multiple biological roles of the CIP in S. pombe, from its discovery almost 30 years ago to the present day
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