PXD014716
PXD014716 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Effects of PGRMC1 phosphorylation status on MIA PaCa-2 cells |
Description | Progesterone Receptor Membrane Component 1 (PGRMC1) is expressed in many cancer cells, where it is associated with detrimental patient outcomes. Multiple different functions and cellular locations have been attributed to PGRMC1 in a variety of contexts, however the mechanisms underlying PGRMC1 biology remain obscure. The protein contains several phosphorylated residues including tyrosines which were acquired early in animal evolution and could be involved with animal cell differentiation mechanisms. Here we demonstrate that mutagenic manipulation of PGRMC1phosphorylation status in MIA PaCa-2 (MP) pancreatic cells exerts broad pleiotropic effects, influencing cell plasticity and tumorigenicity, as assayed by cell biological and proteomics measurements. Relative to MP cells over-expressing hemagglutinin (HA)-tagged wild-type PGRMC1- HA (WT), cells expressing a PGRMC1-HA-S57A/S181A double mutant (DM) exhibited reduced levels of proteins involved in energy metabolism and mitochondrial function. This was associated with Rho-kinase inhibitor (ROCKI)-sensitive changes including altered cell shape, motility, increased PI3K/Akt and JNK activity, and fragmented mitochondrial morphology. An S57A/Y180F/S181A triple mutant (TM) reduced PI3K/Akt and JNK activation, indicating involvement of Y180. Both TM cells and Y180F single mutant cells exhibited attenuated mouse xenograft tumor growth. Tyrosine 180 phosphorylation status of PGRMC1 exerts dramatic influence over cancer cell biology. |
HostingRepository | PRIDE |
AnnounceDate | 2020-03-03 |
AnnouncementXML | Submission_2020-05-27_04:38:29.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Dana Pascovici |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue; acetylated residue |
Instrument | TripleTOF 5600 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2019-07-23 05:51:44 | ID requested | |
1 | 2020-03-03 01:51:54 | announced | |
⏵ 2 | 2020-05-27 04:38:30 | announced | 2020-05-27: Updated publication reference for PubMed record(s): 32245408. |
Publication List
Thejer BM, Adhikary PP, Kaur A, Teakel SL, Van Oosterum A, Seth I, Pajic M, Hannan KM, Pavy M, Poh P, Jazayeri JA, Zaw T, Pascovici D, Ludescher M, Pawlak M, Cassano JC, Turnbull L, Jazayeri M, James AC, Coorey CP, Roberts TL, Kinder SJ, Hannan RD, Patrick E, Molloy MP, New EJ, Fehm TN, Neubauer H, Goldys EM, Weston LA, Cahill MA, PGRMC1 phosphorylation affects cell shape, motility, glycolysis, mitochondrial form and function, and tumor growth. BMC Mol Cell Biol, 21(1):24(2020) [pubmed] |
Keyword List
submitter keyword: proteomics, SWATH, pancreatic cancer, phosphorylation |
Contact List
Michael A. Cahill | |
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contact affiliation | School of Biomedical Sciences, Charles Sturt University, Wagga Wagga, NSW, 2650 |
contact email | mcahill@csu.edu.au |
lab head | |
Dana Pascovici | |
contact affiliation | Australian Proteome Analysis Facility |
contact email | dana.pascovici@mq.edu.au |
dataset submitter |
Full Dataset Link List
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PRIDE project URI |
Repository Record List
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