Proteomic Dataset: Mass Spectrometric Identification of Membrane Proteins that Interact with PRELP

Published: 20 January 2021| Version 1 | DOI: 10.17632/nmgrvjb9cw.1
Hirofumi Kosuge,
Makoto Nakakido,
Satoru Nagatoishi,
Tetsuya Fukuda,
Yasuhiko Bando,
Shin-ichi Ohnuma,
Kouhei Tsumoto


MS proteomics raw data files and a Scaffold file for the following research article. Kosuge H, Nakakido M, Nagatoishi S, Fukuda T, Bando Y, Ohnuma SI, Tsumoto K. (January 8, 2021) Proteomic Identification and Validation of Novel Interactions of the Putative Tumor Suppressor PRELP with Membrane Proteins Including IGFI-R and p75NTR. J. Biol. Chem. 10.1016/j.jbc.2021.100278. Epub ahead of print. Research in brief: Proline and arginine-rich end leucine-rich repeat protein (PRELP) is one of the small leucine-rich repeat proteoglycans (SLRPs), known as a multi-functional and multi-specific ligand. We hypothesized that PRELP interacts with various membrane proteins as is the case with other SLRPs, resulting in the modulation of cellular function. To discover membrane proteins that interact with PRELP, we carried out co-immunoprecipitation coupled with mass spectrometry. We prepared membrane fractions from Expi293 cells overexpressing FLAG-tagged PRELP or control cells and analyzed samples precipitated with anti-FLAG antibody by LC-MS/MS analysis. This data set contains the MS proteomics raw data as follows. PRELP_n1 sample: PRELP_130m_qe8.raw PRELP_n2 sample: PRELP_5ul_130m_qe8.raw Control_n1 sample: mock_130m_qe4.raw Control_n2 sample: mock_5ul_130m_qe4.raw This data set also contains the MS proteomics data analyzed by Scaffold software as follows. 190327_28_PRELP_Condensed_2.sf3



Tokyo Daigaku