Odin (ANKS1A) modulates EGF receptor recycling and stability

The ANKS1A gene product, also known as Odin, was first identified as a tyrosine-phosphorylated component of the epidermal growth factor receptor network. Here we show that Odin functions as an effector of EGFR recycling. In EGF-stimulated HEK293 cells tyrosine phosphorylation of Odin was induced pri...

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Bibliographic Details
Published in:PloS one 2013-06, Vol.8 (6), p.e64817-e64817
Main Authors: Tong, Jiefei, Sydorskyy, Yaroslav, St-Germain, Jonathan R, Taylor, Paul, Tsao, Ming S, Moran, Michael F
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Biochemistry
Biology
Cancer
Cell Line
Cell Line, Tumor
Cell surface
Chemistry
Concentration gradient
Degradation
Endosomes
Endosomes - metabolism
Epidermal growth factor
Epidermal growth factor receptors
Epidermal growth factors
ErbB Receptors - genetics
ErbB Receptors - metabolism
Flow Cytometry
Gene amplification
Health care networks
Hospitals
Humans
Immunoprecipitation
Internalization
Kinases
Ligands
Lung cancer
Lung carcinoma
Lysosomes
Mass Spectrometry
Medicine
Non-small cell lung carcinoma
Overexpression
Phosphorylation
Protein transport
Protein Transport - genetics
Protein Transport - physiology
Protein turnover
Proteins
Proteomics
Receptors
Scientific imaging
Signal transduction
Signaling
Small cell lung carcinoma
Tyrosine
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Summary:The ANKS1A gene product, also known as Odin, was first identified as a tyrosine-phosphorylated component of the epidermal growth factor receptor network. Here we show that Odin functions as an effector of EGFR recycling. In EGF-stimulated HEK293 cells tyrosine phosphorylation of Odin was induced prior to EGFR internalization and independent of EGFR-to-ERK signaling. Over-expression of Odin increased EGF-induced EGFR trafficking to recycling endosomes and recycling back to the cell surface, and decreased trafficking to lysosomes and degradation. Conversely, Odin knockdown in both HEK293 and the non-small cell lung carcinoma line RVH6849, which expresses roughly 10-fold more EGF receptors than HEK293, caused decreased EGFR recycling and accelerated trafficking to the lysosome and degradation. By governing the endocytic fate of internalized receptors, Odin may provide a layer of regulation that enables cells to contend with receptor cell densities and ligand concentration gradients that are physiologically and pathologically highly variable.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0064817