title: Synthesis of an inositol hexakisphosphate (IP6) affinity probe to study the interactome from a colon cancer cell line.
abstract: Inositol hexakisphosphate (InsP6 or IP6) is an important signalling molecule in vesicular trafficking, neurotransmission, immune responses, regulation of protein kinases and phosphatases, activation of ion channels, antioxidant functions and anticancer activities. An IP6 probe was synthesised from myo-inositol via a derivatised analogue, which was immobilised through a terminal amino group onto Dynabeads. Systematic analysis of the IP6 interactome has been performed using the IP6 affinity probe using cytosolic extracts from the LIM1215 colonic carcinoma cell line. LC/MS/MS analysis identified 77 proteins or protein complexes that bind to IP6 specifically, including AP-2 complex proteins and β-arrestins as well as a number of novel potential IP6 interacting proteins. Bioinformatic enrichment analysis of the IP6 interactome reinforced the concept that IP6 regulates a number of biological processes including cell cycle and division, signal transduction, intracellular protein transport, vesicle-mediated transport and RNA splicing.
authors: School of Chemistry, Bio21 Institute, The University of Melbourne, 30 Flemington Road, Parkville, Victoria 3052, Australia.
authors: Meng-Xin
authors: MX
authors: Yin
authors: Ludwig Institute for Cancer Research, Melbourne-Austin Branch, Olivia Newton-John Cancer & Wellness Centre, Studley Road, Heidelberg, Victoria 3084, Australia.
authors: Bruno
authors: B
authors: Catimel
authors: School of Chemistry, Bio21 Institute, The University of Melbourne, 30 Flemington Road, Parkville, Victoria 3052, Australia.
authors: Mark
authors: M
authors: Gregory
authors: Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia. tburgess@wehi.edu.au and Department of Medical Biology, University of Melbourne, Parkville, Victoria 3052, Australia.
authors: Melanie
authors: M
authors: Condron
authors: Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia. tburgess@wehi.edu.au and Department of Medical Biology, University of Melbourne, Parkville, Victoria 3052, Australia.
authors: Eugene
authors: E
authors: Kapp
authors: School of Chemistry, Bio21 Institute, The University of Melbourne, 30 Flemington Road, Parkville, Victoria 3052, Australia.
authors: Andrew B
authors: AB
authors: Holmes
authors: Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia. tburgess@wehi.edu.au and Department of Medical Biology, University of Melbourne, Parkville, Victoria 3052, Australia and Department of Surgery, RMH, University of Melbourne, Parkville, Victoria 3052, Australia.
authors: Antony W
authors: AW
authors: Burgess
mesh_terms: D000345:Affinity Labels / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D045744:Cell Line, Tumor; D003110:Colonic Neoplasms / Q000378:metabolism*; D006801:Humans; D055442:Metabolome; D009363:Neoplasm Proteins / Q000378:metabolism; D010833:Phytic Acid / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D060066:Protein Interaction Maps; D020543:Proteome / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D015398:Signal Transduction; D000071560:beta-Arrestin 2 / Q000378:metabolism
chemical_list: C000605254:ARRB2 protein, human; D000345:Affinity Labels; D002352:Carrier Proteins; D009363:Neoplasm Proteins; D020543:Proteome; D011994:Recombinant Proteins; D000071560:beta-Arrestin 2; D010833:Phytic Acid