Dimerization is Required for Sh3px1 Tyrosine Phosphorylation in Response to Epidermal Growth Factor Signalling and Interaction with Ack2.
From: Weis Center for Research, Geisinger Clinic, 100 N. Academy Avenue, Danville, PA 17822, USA.
The Biochemical journal
- Publish Date: Mar 2006
- ISSN: 1470-8728
- Volume: 394
- Issue: Pt 3
- Pages: 693-8
- Medium: Internet
- Language: English
- Citation (JAMA): Childress Chandra, Lin Qiong, Yang Wannian, et al. Dimerization is Required for Sh3px1 Tyrosine Phosphorylation in Response to Epidermal Growth Factor Signalling and Interaction with Ack2.. Biochem. J. Mar 2006;394:693-8
Abstract
SH3PX1 [SNX9 (sorting nexin 9)] is a member of SNX super-family that is recognized by sharing a PX (phox homology) domain. We have previously shown that SH3PX1, phosphorylated by ACK2 (activated Cdc42-associated tyrosine kinase 2), regulates the degradation of EGF (epidermal growth factor) receptor. In mapping the tyrosine phosphorylation region, we found that the C-terminus of SH3PX1 is required for its tyrosine phosphorylation. Further analysis indicates that this region, known as the coiled-coil domain or the BAR (Bin-amphiphysin-Rvs homology) domain, is the dimerization domain of SH3PX1. Truncation of as little as 13 amino acid residues at the very C-terminus in the coiled-coil/BAR domain of SH3PX1 resulted in no dimerization, no ACK2-catalysed and EGF-stimulated tyrosine phosphorylation and no interaction with ACK2. The intracellular localization of SH3PX1 became dysfunctional upon truncation in the BAR domain. Taken together, our results indicate that the dimerization, which is mediated by the BAR domain, is essential for the intracellular function of SH3PX1.
Mesh Headings (Keywords): Animals, COS Cells, Carrier Proteins, Cercopithecus aethiops, Dimerization, Epidermal Growth Factor, Humans, Mutation, Phosphorylation, Phosphotyrosine, Protein Binding, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Signal Transduction, Vesicular Transport Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16316319
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.