Protein Palmitoylation in Bovine Ovarian Follicle.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
29 Oct 2021
Historique:
received: 10 09 2021
revised: 25 10 2021
accepted: 28 10 2021
entrez: 13 11 2021
pubmed: 14 11 2021
medline: 21 12 2021
Statut: epublish

Résumé

Protein palmitoylation is a reversible post-translational modification by fatty acids (FA), mainly a palmitate (C16:0). Palmitoylation allows protein shuttling between the plasma membrane and cytosol to regulate protein stability, sorting and signaling activity and its deficiency leads to diseases. We aimed to characterize the palmitoyl-proteome of ovarian follicular cells and molecular machinery regulating protein palmitoylation within the follicle. For the first time, 84 palmitoylated proteins were identified from bovine granulosa cells (GC), cumulus cells (CC) and oocytes by acyl-biotin exchange proteomics. Of these, 32 were transmembrane proteins and 27 proteins were detected in bovine follicular fluid extracellular vesicles (ffEVs). Expression of palmitoylation and depalmitoylation enzymes as palmitoyltransferases (ZDHHCs), acylthioesterases (LYPLA1 and LYPLA2) and palmitoylthioesterases (PPT1 and PPT2) were analysed using transcriptome and proteome data in oocytes, CC and GC. By immunofluorescence, ZDHHC16, PPT1, PPT2 and LYPLA2 proteins were localized in GC, CC and oocyte. In oocyte and CC, abundance of palmitoylation-related enzymes significantly varied during oocyte maturation. These variations and the involvement of identified palmitoyl-proteins in oxidation-reduction processes, energy metabolism, protein localization, vesicle-mediated transport, response to stress, G-protein mediated and other signaling pathways suggests that protein palmitoylation may play important roles in oocyte maturation and ffEV-mediated communications within the follicle.

Identifiants

pubmed: 34769186
pii: ijms222111757
doi: 10.3390/ijms222111757
pmc: PMC8583988
pii:
doi:

Substances chimiques

Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Russian Science Foundation
ID : 19-16-768 00115

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Auteurs

Svetlana Uzbekova (S)

CNRS, IFCE, INRAE, Université de Tours, PRC, 37380 Nouzilly, France.

Ana-Paula Teixeira-Gomes (AP)

INRAE, Université de Tours, ISP, 37380 Nouzilly, France.

Aurélie Marestaing (A)

CNRS, IFCE, INRAE, Université de Tours, PRC, 37380 Nouzilly, France.

Peggy Jarrier-Gaillard (P)

CNRS, IFCE, INRAE, Université de Tours, PRC, 37380 Nouzilly, France.

Pascal Papillier (P)

CNRS, IFCE, INRAE, Université de Tours, PRC, 37380 Nouzilly, France.

Ekaterina N Shedova (EN)

L.K. Ernst Federal Research Center for Animal Husbandry, Dubrovitzy 60, 142132 Podolsk, Russia.

Galina N Singina (GN)

L.K. Ernst Federal Research Center for Animal Husbandry, Dubrovitzy 60, 142132 Podolsk, Russia.

Rustem Uzbekov (R)

Laboratoire Biologie Cellulaire et Microscopie Électronique, Faculté de Médecine, Université de Tours, 37032 Tours, France.

Valerie Labas (V)

CNRS, IFCE, INRAE, Université de Tours, PRC, 37380 Nouzilly, France.

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Classifications MeSH