- Research article
EHDS are serine phosphoproteins: EHD1 phosphorylation is enhanced by serum stimulation
Cellular & Molecular Biology Letters volume 13, pages 632–648 (2008)
Endocytic processes are mediated by multiple protein-protein interacting modules and regulated by phosphorylation and dephosphorylation. The Eps15 homology domain containing protein 1 (EHD1) has been implicated in regulating recycling of proteins, internalized both in clathrin-dependent and clathrin-independent endocytic pathways, from the recycling compartment to the plasma membrane. EHD1 was found in a complex with clathrin, adaptor protein complex-2 (AP-2) and insulin-like growth factor-1 receptor (IGF-1R), and was shown to interact with Rabenosyn-5, SNAP29, EHBP1 (EH domain binding protein 1) and syndapin I and II. In this study, we show that EHD1, like the other human EHDs, undergoes serine-phosphorylation. Our results also indicate that EHD1 is a serum-inducible serine-phosphoprotein and that PKC (protein kinase C) is one of its kinases. In addition, we show that inhibitors of clathrin-mediated endocytosis decrease EHD1 phosphorylation, while inhibitors of caveolinmediated endocytosis do not affect EHD1 phosphorylation. The results of experiments in which inhibitors of endocytosis were employed strongly suggest that EHD1 phosphorylation occurs between early endosomes and the endocytic recycling compartment.
adaptor protein complex-2
bovine serum albumin
Chinese hamster ovary
counts per minute
Dulbecco modified eagle medium
EH domain binding protein 1
fetal calf serum
insulin-like growth factor-1 receptor
mouse dihydrofolate reductase
minimal essential medium-alpha
open reading frame
phosphate buffered saline
protein kinase C
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Fichtman, B., Ravid, L., Rapaport, D. et al. EHDS are serine phosphoproteins: EHD1 phosphorylation is enhanced by serum stimulation. Cell Mol Biol Lett 13, 632–648 (2008). https://doi.org/10.2478/s11658-008-0027-4
- EH domain