Inhibitory effect of SPE-39 due to tyrosine phosphorylation and ubiquitination on the function of Vps33B in the EGF-stimulated cells.
Although SPE-39 is a binding protein to Vps33B that is one of the subunit in the mammalian HOPS complex, the elements of SPE-39 function remain unknown. Here, we show that tyrosine phosphorylation of SPE-39 following EGF stimulation plays a role in the stability of SPE-39 itself. Ubiquitination of the C-terminal ... region of SPE-39 was also elevated in response to EGF stimulation, and this process was regulated by the phosphorylation of Tyr-11 in SPE-39. However, association of Vps33B with SPE-39 inhibited the elevation of ubiquitination of SPE-39 following EGF stimulation, which might be responsible for the stabilization of SPE-39. Furthermore, an opposing functional relationship between SPE-39 and Vps33B on the downregulation of the EGF receptor was observed in EGF-stimulated COS-7 cells.
Mesh Terms:
Animals, COS Cells, Carrier Proteins, Chlorocebus aethiops, DNA, Complementary, Epidermal Growth Factor, Gene Expression Regulation, Humans, Microscopy, Fluorescence, Phosphorylation, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Time Factors, Tyrosine, Ubiquitin, Vesicular Transport Proteins
Animals, COS Cells, Carrier Proteins, Chlorocebus aethiops, DNA, Complementary, Epidermal Growth Factor, Gene Expression Regulation, Humans, Microscopy, Fluorescence, Phosphorylation, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Time Factors, Tyrosine, Ubiquitin, Vesicular Transport Proteins
FEBS Lett.
Date: Jul. 30, 2012
PubMed ID: 22677173
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