English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

ETTER L Dear Editor, Protein tyrosine phosphorylation is one of the most prevalent forms of post-translational modification and plays a signifi cant role in the control of a variety of cellular processes, including signal transduction, and is implicated in many human diseases (Eckhart et al., 1979; Karisch et al., 2011). The human vac-cinia H1-related phosphatase (VHR), the fi rst human dual specifi city protein phos-phatase (DSP), hydrolyzes phosphate monoesters from phosphotyrosine, phosphothreonine, or phosphoserine residues (Aroca et al., 1995). DSPs function in signal transduction and in control of the cell cycle; more than 20 mamma-lian DSPs have so far been identifi ed. Although VHR can dephosphorylate both Erk and Jnk in vivo (Schumacher et al., 2002), it differs from other 'typi-cal' mitogen activated protein (MAP) kinase phosphatases (MKPs). With only 185 amino acids, VHR consists of only a catalytic domain with no recognizing or docking domain. As a member of the " atypical " DSPs, VHR has been widely used in attempts to elucidate the catalytic mechanism of DSPs. As a phosphatase, VHR has a critical role in managing the activities of the mitogen activated protein kinases (MAPKs) Erk and Jnk by dephosphorylating the phos-phor-Thr and phosphor-Tyr residues in their respective active sites during the cell cycle. As a predominant nuclear enzyme, a large number of researches have been done on VHR function of phosphatase activity, but comparatively little is known about its own phospho-rylation. This is largely because there is no way to site-specifi cally incorporate a phosphor-amino acid into a recombinant protein, so it has only been possible to conjecture about the phosphorylation site of VHR are from indirect results (Hoyt et al., 2007). Thus, the function and impact of VHR phosphorylation remain incompletely understood and hotly debated. In this manuscript, we report the fi rst successful site-specifi c incorporation of sulfotyrisine into VHR through the use of expanding genetic code, confi rm the site of phosphorylation, and describe the activities of the sulfation-modifi ed VHR. Expanding genetic code is a useful method that allows one to genetically encode unnatural amino acid (UAA) into protein during translation with high fi del-ity and effi ciency (Wang et al., 2001). The resulting protein contains UAA at any location specifi ed by a TAG codon, making this method significantly simpler and more versatile than competing methods such as in vitro enzymatic modifi cation, chemical modifi cation and peptide synthesis. Since this …

A genetically encoded sulfotyrosine for VHR function research