The PI(3)P interactome from a colon cancer cell
- Author(s)
- Catimel, B; Kapp, E; Yin, MX; Gregory, M; Wong, LSM; Condron, M; Church, N; Kershaw, N; Holmes, AB; Burgess, AW;
- Journal Title
- JOURNAL OF PROTEOMICS
- Publication Type
- Journal Article
- Abstract
- A comprehensive analysis of the phosphoinositide interactome has been performed using an omega-amino analogue of phosphatidylinositol 3-phosphate (PI(3)P immobilised onto Affi-10 beads for use as an affinity absorbent for cytosolic, membrane and nuclear extracts from the LIM1215 colonic carcinoma cell line. Affinity/LC/MS/MS experiments allowed the identification of 681 proteins/protein complexes which interact with PI(3)P. Protein domain enrichment analysis identified proteins possessing PI(3)P (e.g., FYVE, PX, PH), PIP and PIP/phospholipid binding domains along with small GTPases, GTPase regulators, kinases and SH2/SH3 containing proteins. Functional and pathway enrichment analyses highlighted the major role of PI(3)P in endocytosis dynamics and vesicular trafficking, intracellular cell signalling regulation, cell division and cytokinesis. Biological significance This study provides an initial detailed assessment of the phosphatidylinositol 3-phosphate (PI(3)P) interactome, highlights the major role of PI(3)P in endocytosis dynamics and vesicular trafficking, cell intracellular regulation, signalling and cytokinesis and suggests potential PI(3)P specificity for further biochemical and biological characterisation. (C) 2013 Elsevier B.V. All rights reserved.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- II PHOSPHOINOSITIDE 3-KINASE; PLECKSTRIN HOMOLOGY DOMAINS; PHOSPHATIDYLINOSITOL 3-KINASE; FYVE DOMAIN; ENRICHMENT ANALYSIS; SIGNALING PATHWAY; STRUCTURAL BASIS; BINDING DOMAINS; ALPHA-ISOFORM; BETA-CATENIN
- Research Division(s)
- Structural Biology
- Publisher's Version
- https://doi.org/10.1016/j.jprot.2013.01.031
- Terms of Use/Rights Notice
- Copyright © 2013 Elsevier B.V. All rights reserved.
Creation Date: 2013-04-26 12:00:00