The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC

Jun Zhong, Raghothama Chaerkady, Kumaran Kandasamy, Marjan Gucek, Robert N. Cole, Akhilesh Pandey

Research output: Contribution to journalArticlepeer-review

Abstract

Signal transduction pathways are tightly controlled by positive and negative regulators. We have previously identified Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; gene symbol ANKS1A) as a negative regulator of growth factor signaling; however, the mechanisms through which Odin regulates these pathways remain to be elucidated. To determine how Odin negatively regulates growth factor signaling, we undertook a proteomic approach to systematically identify proteins that interact with Odin using the SILAC strategy. In this study, we identified 18 molecules that were specifically associated in a protein complex with Odin. Our study established that the complete family of 14-3-3 proteins occur in a protein complex with Odin, which is also supported by earlier reports that identified a few members of the 14-3-3 family as Odin interactors. Among the novel protein interactors of Odin were CD2-associated protein, SH3 domain kinase binding protein 1 and DAB2 interacting protein. We confirmed 8 of the eighteen interactions identified in the Odin protein complex by co-immunoprecipitation experiments. Finally, a literature-based network analysis revealed that Odin interacting partners are involved in various cellular processes, some of which are key molecules in regulating receptor endocytosis.

Original languageEnglish (US)
Pages (from-to)294-303
Number of pages10
JournalJournal of Proteomics
Volume74
Issue number3
DOIs
StatePublished - Mar 1 2011

Keywords

  • Interacting proteins
  • Odin (ANKS1A)
  • Receptor tyrosine kinase
  • SILAC

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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