Not your Mother's MAPKs: Apicomplexan MAPK function in daughter cell budding.

Autor: O'Shaughnessy WJ; Department of Pharmacology, University of Texas, Southwestern Medical Center, Dallas, Texas, United States of America., Dewangan PS; Department of Pharmacology, University of Texas, Southwestern Medical Center, Dallas, Texas, United States of America., Paiz EA; Department of Pharmacology, University of Texas, Southwestern Medical Center, Dallas, Texas, United States of America., Reese ML; Department of Pharmacology, University of Texas, Southwestern Medical Center, Dallas, Texas, United States of America.; Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas, Texas, United States of America.
Jazyk: angličtina
Zdroj: PLoS pathogens [PLoS Pathog] 2022 Oct 13; Vol. 18 (10), pp. e1010849. Date of Electronic Publication: 2022 Oct 13 (Print Publication: 2022).
DOI: 10.1371/journal.ppat.1010849
Abstrakt: Reversible phosphorylation by protein kinases is one of the core mechanisms by which biological signals are propagated and processed. Mitogen-activated protein kinases, or MAPKs, are conserved throughout eukaryotes where they regulate cell cycle, development, and stress response. Here, we review advances in our understanding of the function and biochemistry of MAPK signaling in apicomplexan parasites. As expected for well-conserved signaling modules, MAPKs have been found to have multiple essential roles regulating both Toxoplasma tachyzoite replication and sexual differentiation in Plasmodium. However, apicomplexan MAPK signaling is notable for the lack of the canonical kinase cascade that normally regulates the networks, and therefore must be regulated by a distinct mechanism. We highlight what few regulatory relationships have been established to date, and discuss the challenges to the field in elucidating the complete MAPK signaling networks in these parasites.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
Nepřihlášeným uživatelům se plný text nezobrazuje