Protein Palmitoylation in Bovine Ovarian Follicle
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....
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2021
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oai:doaj.org-article:775b76bf2c23477687846637c133b3a82021-11-11T17:12:44ZProtein Palmitoylation in Bovine Ovarian Follicle10.3390/ijms2221117571422-00671661-6596https://doaj.org/article/775b76bf2c23477687846637c133b3a82021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11757https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Protein 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.Svetlana UzbekovaAna-Paula Teixeira-GomesAurélie MarestaingPeggy Jarrier-GaillardPascal PapillierEkaterina N. ShedovaGalina N. SinginaRustem UzbekovValerie LabasMDPI AGarticleprotein palmitoylationZDHHCgranulosacumulusoocytefollicular fluid extracellular vesiclesBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11757, p 11757 (2021) |
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protein palmitoylation ZDHHC granulosa cumulus oocyte follicular fluid extracellular vesicles Biology (General) QH301-705.5 Chemistry QD1-999 |
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protein palmitoylation ZDHHC granulosa cumulus oocyte follicular fluid extracellular vesicles Biology (General) QH301-705.5 Chemistry QD1-999 Svetlana Uzbekova Ana-Paula Teixeira-Gomes Aurélie Marestaing Peggy Jarrier-Gaillard Pascal Papillier Ekaterina N. Shedova Galina N. Singina Rustem Uzbekov Valerie Labas Protein Palmitoylation in Bovine Ovarian Follicle |
description |
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. |
format |
article |
author |
Svetlana Uzbekova Ana-Paula Teixeira-Gomes Aurélie Marestaing Peggy Jarrier-Gaillard Pascal Papillier Ekaterina N. Shedova Galina N. Singina Rustem Uzbekov Valerie Labas |
author_facet |
Svetlana Uzbekova Ana-Paula Teixeira-Gomes Aurélie Marestaing Peggy Jarrier-Gaillard Pascal Papillier Ekaterina N. Shedova Galina N. Singina Rustem Uzbekov Valerie Labas |
author_sort |
Svetlana Uzbekova |
title |
Protein Palmitoylation in Bovine Ovarian Follicle |
title_short |
Protein Palmitoylation in Bovine Ovarian Follicle |
title_full |
Protein Palmitoylation in Bovine Ovarian Follicle |
title_fullStr |
Protein Palmitoylation in Bovine Ovarian Follicle |
title_full_unstemmed |
Protein Palmitoylation in Bovine Ovarian Follicle |
title_sort |
protein palmitoylation in bovine ovarian follicle |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/775b76bf2c23477687846637c133b3a8 |
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