Trypanosoma cruzi trans-sialidase induces STAT3 and ERK activation by prokineticin receptor 2 binding.


Journal

Cell biochemistry and function
ISSN: 1099-0844
Titre abrégé: Cell Biochem Funct
Pays: England
ID NLM: 8305874

Informations de publication

Date de publication:
Mar 2021
Historique:
received: 30 03 2020
revised: 15 07 2020
accepted: 01 08 2020
pubmed: 7 9 2020
medline: 7 7 2021
entrez: 6 9 2020
Statut: ppublish

Résumé

Tc85, as other members of trans-sialidase family, is involved in Trypanosoma cruzi parasite adhesion to mammalian cells. Particularly, Tc85 acts through specific interactions with prokineticin receptor 2, a G-protein coupled receptor involved in diverse physiological and pathological processes. In this manuscript, through biochemical analyses, we demonstrated that LamG, a Tc85 domain, physically interacts with the prokineticin receptor 2. Moreover, expressing prokineticin receptor 1 and 2 we demonstrated that LamG specifically activates prokineticin receptor 2 through a strong coupling with G

Identifiants

pubmed: 32892338
doi: 10.1002/cbf.3586
doi:

Substances chimiques

Glycoproteins 0
NFATC Transcription Factors 0
PROKR1 protein, human 0
PROKR2 protein, human 0
Protozoan Proteins 0
Receptors, G-Protein-Coupled 0
Receptors, Peptide 0
Recombinant Proteins 0
STAT3 Transcription Factor 0
Extracellular Signal-Regulated MAP Kinases EC 2.7.11.24
trans-sialidase EC 3.2.1.-
Neuraminidase EC 3.2.1.18

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

326-334

Subventions

Organisme : Sapienza Università di Roma
ID : AR21816436367468

Informations de copyright

© 2020 John Wiley & Sons Ltd.

Références

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Auteurs

Roberta Lattanzi (R)

Department of Physiology and Pharmacology "Vittorio Erspamer", Sapienza University of Rome, Rome, Italy.

Daniela Maftei (D)

Department of Physiology and Pharmacology "Vittorio Erspamer", Sapienza University of Rome, Rome, Italy.

Maria Rosaria Fullone (MR)

Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.

Rossella Miele (R)

Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.

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Classifications MeSH