TY - JOUR
T1 - The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC
AU - Zhong, Jun
AU - Chaerkady, Raghothama
AU - Kandasamy, Kumaran
AU - Gucek, Marjan
AU - Cole, Robert N.
AU - Pandey, Akhilesh
PY - 2011/3/1
Y1 - 2011/3/1
N2 - 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.
AB - 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.
KW - Interacting proteins
KW - Odin (ANKS1A)
KW - Receptor tyrosine kinase
KW - SILAC
UR - http://www.scopus.com/inward/record.url?scp=78651487556&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78651487556&partnerID=8YFLogxK
U2 - 10.1016/j.jprot.2010.11.006
DO - 10.1016/j.jprot.2010.11.006
M3 - Article
C2 - 21081186
AN - SCOPUS:78651487556
SN - 1874-3919
VL - 74
SP - 294
EP - 303
JO - Journal of Proteomics
JF - Journal of Proteomics
IS - 3
ER -