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Di Paola"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065280"],"tissue":["Heart"],"sample_protocol":["Hearts were harvested 4 weeks post-AAV9 injection and subjected to subcellular fractionation, involving lysis in a sucrose/Tris-HCl/EDTA lysis buffer (with protease inhibitors). Sequential centrifugation steps were used to isolate microsomal, mitochondrial and cytosolic fractions. Microsomal and mitochondrial fractions were solubilized in 8M urea (with protease inihibitors), whereas the cytosolic fraction remained in sucrose lysis buffer. All fractions were digested with trypsin prior to desalting using Evotips."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA-MS was performed using an Evosep One LC system couple to a Q Excative Plus mass spectrometer. DIA data were acquired with 30 isolation windows covering 400-950 m/z. RAW files were processed using DIA-NN v1.81 against a Uniprot mouse (Feb 2024) FASTA in silico spectral library. Search parameters included: one missed cleavage, fixed carbamidomethylation of cysteines, variable methionine oxidation, 0.01 FDR, and quantification using \"Robust LC\" and \"RT & signal-dep\" settings. Match-between-runs, isotopologue use and unrelated run alignment features were enabled."],"omics_type":["Proteomics"],"labhead":["Anthony Orlando"],"instrument_platform":[""],"labhead_affiliation":["University of Toronto"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["michelle.dipaola@mail.utoronto.ca"],"publication":["41672147 Di Paola M, Reitz CJ, Kuzmanov U, Jia K, Gramolini AO. Subcellular Proteomic Analyses Reveal REEP5 Knockdown in the Mouse Heart Disrupts Mitochondrial Networks. Mol Cell Proteomics. 2026 25(3):101527 10.1016/j.mcpro.2026.101527"],"submitter_affiliation":["Univeristy of Toronto"],"submitter_country":["Canada"],"pubmed_abstract":["Receptor Expression-Enhancing Protein 5 (REEP5) is a cardiac-enriched, membrane-shaping protein localized to the sarco(endo)plasmic reticulum (SR/ER), where it supports membrane network architecture and cardiomyocyte function. While REEP5 has been implicated in calcium handling and contractility, its role in regulating inter-organelle communication and mitochondrial homeostasis remains less well-understood. In this study, we used recombinant adeno-associated virus serotype 9(rAAV9)-mediated shRNA knockdown of Reep5 in mouse hearts, combined with subcellular fractionation and data-independent acquisition mass spectrometry (DIA-MS), to define proteomic remodeling across microsomal (SR/ER), mitochondrial, and cytosolic compartments. Loss of REEP5 altered the composition of SR/ER membrane-shaping proteins, including upregulation of RTN4, ATL3, and CKAP4, suggesting a partial compensatory response. Microsomal, mitochondrial and cytosolic proteomes exhibited broad reorganization, with enrichment of proteins involved in redox adaptation and proteostasis, alongside depletion of mitochondrial import machinery and antioxidant enzymes. Imaging of isolated cardiomyocytes confirmed fragmented mitochondrial networks and increased reactive oxygen species (ROS), consistent with proteomic signatures of disrupted mitochondrial dynamics and oxidative stress. Gene ontology enrichment across all fractions highlighted widespread dysregulation in organelle-specific processes, including translation, protein localization, and metabolic remodeling. Notably, several altered pathways converged on mitochondria-associated membranes (MAMs), suggesting that REEP5 may support SR/ER-mitochondria tethering and functional crosstalk. These findings position REEP5 as a key regulator of organelle homeostasis in the heart and underscore how its loss disrupts mitochondrial integrity and inter-organelle communication across cellular compartments."],"pubmed_title":["Subcellular proteomic analyses reveal REEP5 knockdown in the mouse heart disrupts mitochondrial networks."],"pubmed_authors":["Di Paola Michelle M, Reitz Cristine J CJ, Kuzmanov Uros U, Jia Kateleen K, Gramolini Anthony O AO"],"additional_accession":[]},"is_claimable":false,"name":"Subcellular Proteomic Analyses Reveal REEP5 Knockdown in the Mouse Heart Disrupts Mitochondrial Networks","description":"This study investigates the role of REEP5 in maintaining organelle integrity and redox homeostasis in cardiac tissue (specifically cardiomyocytes). Using AAV9-mediated shRNA knockdown in postnatal mice, we acheived a cardiac-specific depletion of REEP5. Hearts were harvested 4 weeks post-injection and subjected to subcellular fractionation to isolate microsomal (SR/ER-enriched), mitochondrial, and cytosolic cellular compartmetns. Each fraction was analyzed using data-independent acquisition (DIA) LC-MS/MS on a Q Exactive Plus instrument and the resulting dataset caputres an organelle-specific proteomic profile following depletion of REEP5. Loss of REEP5 leads to changes in the proteomic profiles of targets involved in regulating SR/ER membrane dynamics, ER-mitochondrial communications, mitochondrial morphology and oxidative stress. This work highlights REEP5 as an important regulator of ER-mitochondrial communication and cardiac 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