Chimeras of P4-ATPase and Guanylate Cyclase in Pathogenic Protists.


Journal

Trends in parasitology
ISSN: 1471-5007
Titre abrégé: Trends Parasitol
Pays: England
ID NLM: 100966034

Informations de publication

Date de publication:
04 2020
Historique:
received: 11 12 2019
revised: 29 01 2020
accepted: 29 01 2020
entrez: 20 3 2020
pubmed: 20 3 2020
medline: 28 11 2020
Statut: ppublish

Résumé

Apicomplexan parasites harbor chimeric proteins embodying P4-type ATPase and guanylate cyclase domains. Such proteins - serving as the actuator of cGMP signaling in this group of important pathogens - are indeed unusual in terms of their sheer size, modus operandi, and evolutionary repurposing. Much like the mythological Sphinx, a human-lion chimeric creature that posed challenging riddles, the P4-type ATPase-guanylate cyclase chimeras present both structural and functional conundrums. Here we review the function, topology, mechanism, and intramolecular coordination of the alveolate-specific chimeras in apicomplexan parasites. The steep technological challenge to understand these molecular Sphinxes will surely keep many interdisciplinary researchers busy in the next decades.

Identifiants

pubmed: 32191852
pii: S1471-4922(20)30019-2
doi: 10.1016/j.pt.2020.01.009
pii:
doi:

Substances chimiques

Protozoan Proteins 0
Adenosine Triphosphatases EC 3.6.1.-
Guanylate Cyclase EC 4.6.1.2

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

382-392

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

Auteurs

Özlem Günay-Esiyok (Ö)

Department of Molecular Parasitology, Institute of Biology, Faculty of Life Sciences, Humboldt University, Berlin, Germany. Electronic address: gueesiyo@hu-berlin.de.

Nishith Gupta (N)

Department of Molecular Parasitology, Institute of Biology, Faculty of Life Sciences, Humboldt University, Berlin, Germany. Electronic address: Gupta.Nishith@hu-berlin.de.

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Classifications MeSH