PXD033878 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Phosphatases modified by LH signaling in ovarian follicles: testing their role in regulating the NPR2 guanylyl cyclase |
Description | In response to luteinizing hormone (LH), multiple proteins in rat and mouse granulosa cells are rapidly dephosphorylated, but the responsible phosphatases remain to be identified. Because the phosphorylation state of phosphatases can regulate their interaction with substrates, we searched for phosphatases that might function in LH signaling by using quantitative mass spectrometry. We identified all proteins in rat ovarian follicles whose phosphorylation state changed detectably in response to a 30-min exposure to LH, and within this list, identified protein phosphatases or phosphatase regulatory subunits that showed changes in phosphorylation. Phosphatases in the phosphoprotein phosphatase (PPP) family were of particular interest because of their requirement for dephosphorylating the natriuretic peptide receptor 2 (NPR2) guanylyl cyclase in the granulosa cells, which triggers oocyte meiotic resumption. Among the PPP family regulatory subunits, PPP1R12A and PPP2R5D showed the largest increases in phosphorylation, with 4–10 fold increases in signal intensity on several sites. Although follicles from mice in which these phosphorylations were prevented by serine-to-alanine mutations in either Ppp1r12a or Ppp2r5d showed normal LH-induced NPR2 dephosphorylation, these regulatory subunits and others could act redundantly to dephosphorylate NPR2. Our identification of phosphatases and other proteins whose phosphorylation state is rapidly modified by LH provides clues about multiple signaling pathways in ovarian follicles. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-20 |
AnnouncementXML | Submission_2023-11-20_07:57:01.087.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Henning Urlaub |
SpeciesList | scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116; |
ModificationList | phosphorylated residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-05-12 10:16:55 | ID requested | |
⏵ 1 | 2023-11-20 07:57:01 | announced | |
Publication List
Keyword List
submitter keyword: ovarian follicle, chondrocytes, luteinizing hormone, NPR2, fibroblast growth factor, phosphorylation, cyclic GMP |
Contact List
Prof. Dr. |
contact affiliation | 1. Bioanalytical Mass Spectrometry Group, Max-Planck Institute for Multidisciplinary Sciencies, Am Fassberg 11, 37077 Goettingen, Germany; 2. Clinical Chemistry, University Medical Center Goettingen, Robert-Koch-Str. 40, 37075 Goettingen, Germany. |
contact email | henning.urlaub@mpinat.mpg.de |
lab head | |
Henning Urlaub |
contact affiliation | Max-Plank Institute for Biophysical Chemistry |
contact email | msbio.goettingen@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD033878
- Label: PRIDE project
- Name: Phosphatases modified by LH signaling in ovarian follicles: testing their role in regulating the NPR2 guanylyl cyclase