Quantitative analysis of PPT1 interactome in human neuroblastoma cells
Enzo Scifo,
Agnieszka Szwajda,
Rabah Soliymani,
Francesco Pezzini,
Marzia Bianchi,
Arvydas Dapkunas,
Janusz Dębski,
Kristiina Uusi-Rauva,
Michał Dadlez,
Anne-Claude Gingras,
Jaana Tyynelä,
Alessandro Simonati,
Anu Jalanko,
Marc H. Baumann,
Maciej Lalowski
Affiliations
Enzo Scifo
Meilahti Clinical Proteomics Core Facility, Institute of Biomedicine, Biochemistry and Developmental Biology, University of Helsinki, Helsinki, Finland
Agnieszka Szwajda
Institute for Molecular Medicine (FIMM), University of Helsinki, Helsinki, Finland
Rabah Soliymani
Meilahti Clinical Proteomics Core Facility, Institute of Biomedicine, Biochemistry and Developmental Biology, University of Helsinki, Helsinki, Finland
Francesco Pezzini
Department of Neurological and Movement Sciences, University of Verona, Verona, Italy
Marzia Bianchi
Department of Neurological and Movement Sciences, University of Verona, Verona, Italy
Arvydas Dapkunas
Meilahti Clinical Proteomics Core Facility, Institute of Biomedicine, Biochemistry and Developmental Biology, University of Helsinki, Helsinki, Finland
Janusz Dębski
Mass Spectrometry Laboratory, Department of Biophysics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland
Kristiina Uusi-Rauva
Folkhälsan Institute of Genetics, Helsinki, Finland
Michał Dadlez
Mass Spectrometry Laboratory, Department of Biophysics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland
Anne-Claude Gingras
Centre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, and Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada
Jaana Tyynelä
Meilahti Clinical Proteomics Core Facility, Institute of Biomedicine, Biochemistry and Developmental Biology, University of Helsinki, Helsinki, Finland
Alessandro Simonati
Department of Neurological and Movement Sciences, University of Verona, Verona, Italy
Anu Jalanko
Institute for Molecular Medicine (FIMM), University of Helsinki, Helsinki, Finland
Marc H. Baumann
Meilahti Clinical Proteomics Core Facility, Institute of Biomedicine, Biochemistry and Developmental Biology, University of Helsinki, Helsinki, Finland
Maciej Lalowski
Meilahti Clinical Proteomics Core Facility, Institute of Biomedicine, Biochemistry and Developmental Biology, University of Helsinki, Helsinki, Finland
Mutations in the CLN1 gene that encodes Palmitoyl protein thioesterase 1 (PPT1) or CLN1, cause Infantile NCL (INCL, MIM#256730). PPT1 removes long fatty acid chains such as palmitate from modified cysteine residues of proteins. The data shown here result from isolated protein complexes from PPT1-expressing SH-SY5Y stable cells that were subjected to single step affinity purification coupled to mass spectrometry (AP-MS). Prior to the MS analysis, we utilised a modified filter-aided sample preparation (FASP) protocol. Based on label free quantitative analysis of the data by SAINT, 23 PPT1 interacting partners (IP) were identified. A dense connectivity in PPT1 network was further revealed by functional coupling and extended network analyses, linking it to mitochondrial ATP synthesis coupled protein transport and thioester biosynthetic process. Moreover, the terms: inhibition of organismal death, movement disorders and concentration of lipid were predicted to be altered in the PPT1 network. Data presented here are related to Scifo et al. (J. Proteomics, 123 (2015) 42–53).
