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PXD078272

PXD078272 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleResearch data to support manuscript titled: Mapping Phosphorylation-Specific Pin1-CRMP2 Interactions using an Integrated Mass Spectrometry Approach
DescriptionABSTRACT: Abnormal protein phosphorylation is a fundamental trigger in the pathogenesis of Alzheimer’s Disease, leading to the formation of neurofibrillary tangles. Thus, molecular determination of the critical factors in controlling phosphorylation is desirable. Pin1, a cis-trans prolyl isomerase has recently been implicated in Alzheimer’s Disease progression. Moreover, Pin1 specifically targets phosphoproteins, regulating their function. Here, we reveal a novel interaction interface between Pin1 and the Collapsin Response Mediator Protein-2 (CRMP2); a protein found hyperphosphorylated alongside tau within neurofibrillary tangles. Using native mass spectrometry, we show that Pin1 binds to the disordered C-terminus of CRMP2 in a phosphorylation-dependent manner with residues Thr509 and Thr514 on CRMP2 important for enhanced binding affinity. Hydrogen-deuterium exchange mass spectrometry experiments further localized this binding site to the WW-domain of Pin1. Together, these findings provide novel insight into a putative regulatory role of Pin1 in modulating hyper-phosphorylation of CRMP2.
HostingRepositoryPRIDE
AnnounceDate2026-05-20
AnnouncementXMLSubmission_2026-05-20_05:48:27.085.xml
DigitalObjectIdentifierhttps://doi.org/10.6019/PXD078272
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterAneika Leney
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationListNo PTMs are included in the dataset
InstrumentOrbitrap Eclipse
Dataset History
RevisionDatetimeStatusChangeLog Entry
02026-05-13 07:19:10ID requested
12026-05-20 05:48:27announced
Publication List
10.6019/PXD078272;
10.1021/ACSCHEMBIO.6C00227;
Keyword List
submitter keyword: native mass spectrometry, hydrogen-deuterium exchange mass spectrometry, protein-ligand binding,peptidyl prolyl isomerase
Contact List
Aneika Leney
contact affiliationSchool of Biosciences, University of Birmingham, UK
contact emaila.leney@bham.ac.uk
lab head
Aneika Leney
contact affiliationUniversity of Birmingham
contact emaila.leney@bham.ac.uk
dataset submitter
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Dataset FTP location
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