IDPs Enable Substrate Specificity of Protein Phosphatases
نویسندگان
چکیده
منابع مشابه
Substrate specificity and plasticity of FERM-containing protein tyrosine phosphatases.
Epidermal growth factor receptor (EGFR) pathway substrate 15 (Eps15) is a newly identified substrate for protein tyrosine phosphatase N3 (PTPN3), which belongs to the FERM-containing PTP subfamily comprising five members including PTPN3, N4, N13, N14, and N21. We solved the crystal structures of the PTPN3-Eps15 phosphopeptide complex and found that His812 of PTPN3 and Pro850 of Eps15 are respon...
متن کاملUse of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases.
Synthetic peptides incorporating various chemical moieties, for example, phosphate groups, are convenient tools for investigating protein modification enzymes, such as protein phosphatases (PPs). However, short peptides are sometimes poor substrates, and their binding to commonly used matrices is unpredictable and variable. In general, protein substrates for PPs are superior for enzymatic assay...
متن کاملPhosphotyrosine Substrate Sequence Motifs for Dual Specificity Phosphatases
Protein tyrosine phosphatases dephosphorylate tyrosine residues of proteins, whereas, dual specificity phosphatases (DUSPs) are a subgroup of protein tyrosine phosphatases that dephosphorylate not only Tyr(P) residue, but also the Ser(P) and Thr(P) residues of proteins. The DUSPs are linked to the regulation of many cellular functions and signaling pathways. Though many cellular targets of DUSP...
متن کاملPhysiological signaling specificity by protein tyrosine phosphatases.
Protein tyrosine phosphatases (PTPs) are now recognized to be involved in a multitude of signaling events that control fundamental biological processes such as cell growth, differentiation, apoptosis, and cell movement. PTPs, which were initially thought to be less discriminating in their actions compared with their protein tyrosine kinase counterparts, are now known to regulate these various b...
متن کاملSubstrate specificity of protein kinase C inhibitors.
In the August issue of TiPS, Epand and Lester analysed the effect of the physicochemical properties of the membrane on protein kinase C activity. In addition to those substrates discussed that require the presence of Ca2+ and phospholipids, other substrates can be phosphorylated in the absence of these activators. It is possible that this differential substrate requirement could be exploited ph...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2019
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2018.11.050