Disease relevance of STYX

• Protein tyrosine phosphatase-like protein IA2-antibodies plus glutamic acid decarboxylase 65 antibodies (GADA) indicates autoimmunity as frequently as islet cell antibodies assay in children with recently diagnosed diabetes mellitus [1].
• BACKGROUND: Autoantibodies for the 65-kDa form of glutamic acid decarboxylase (GAD65) and protein tyrosine phosphatase-like protein (IA-2) are measured for risk prediction and diagnosis of autoimmune diabetes mellitus [2].

High impact information on STYX

• STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo [3].
• The archetype STYX/dead-phosphatase complexes with a spermatid mRNA-binding protein and is essential for normal sperm production [4].
• We demonstrate that the phosphoserine, -threonine or -tyrosine, interaction protein, Styx, complexes with a testicular RNA-binding protein and is essential for normal spermiogenesis [4].
• Ablation of Styx expression in mouse disrupts round and elongating spermatid development, resulting in a >1,000-fold decrease in spermatozoa production [4].
• Immunoprecipitation of Styx with Crhsp-24, a phosphorylated RNA-binding protein implicated in translational repression of histone mRNAs, provides a strategy for regulating posttranscriptional gene expression [4].

Biological context of STYX

• Bacterially expressed STYX is incapable of hydrolyzing Tyr(P)-containing substrates; however, mutation of Gly120 to Cys (G120C), which structurally mimics the active site of dsPTPases, confers phosphatase activity to this molecule [5].
• Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation [3].
• Pasticcino2 is a protein tyrosine phosphatase-like involved in cell proliferation and differentiation in Arabidopsis [6].
• Macronuclear DNA synthesis occupies a substantial part of the interdivision interval, and micronuclear DNA synthesis in Styx sp. takes place in early prophase at a time when macronuclear DNA synthesis is in its terminal phase [7].

Anatomical context of STYX

• Here we describe a novel human member of the protein tyrosine phosphatase-like B (PTPLB) family, an integral protein of the endoplasmic reticulum membrane with four membrane-spanning alpha helices, as a BAP31-interacting protein [8].
• Identification of protein tyrosine phosphatase-like IA2 (islet cell antigen 512) as the insulin-dependent diabetes-related 37/40K autoantigen and a target of islet-cell antibodies [9].
• In decidual cells and alveolar macrophages, the activity is due to specific osteoclastic/macrophagic tartrate-resistant acid phosphatase, in lymphocytes to specific protein tyrosine phosphatases, and in endothelial and mesangial cells to a protein tyrosine phosphatase-like acid phosphatase [10].

Associations of STYX with chemical compounds

• It is unclear whether high levels of antigen-specific islet antibodies [GADA (glutamic acid decarboxylase 65 antibodies) and IA2-ab (protein tyrosine phosphatase-like protein antibodies)] predict beta-cell failure in patients with onset of diabetes in adult age [11].
• We have cloned a new family of novel protein tyrosine phosphatase-like genes, the Ptpl (protein tyrosine phosphatase-like; proline instead of catalytic arginine) gene family [12].
• The previously unreported 27-methyl-5,9-octacosadienoic acid [1] and 26-methyl-5,9-octacosadienoic acid [2] were identified in the phospholipids of the Caribbean sponges Chondrosia remiformis and Myrmekioderma styx [13].

Other interactions of STYX

• Polymerase chain reaction amplification of reverse-transcribed poly(A+) RNA revealed an alternatively spliced form of STYX containing a unique carboxyl terminus [5].
• Myotubularin is the archetype of a family of highly conserved protein-tyrosine phosphatase-like enzymes [14].
• The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B [8].
• Autoantibodies in insulin-dependent diabetes recognize distinct cytoplasmic domains of the protein tyrosine phosphatase-like IA-2 autoantigen [15].
• Recently, autoantibodies against ICA512, which has identity with the protein tyrosine phosphatase-like protein IA2, were reported [9].

Analytical, diagnostic and therapeutic context of STYX

• Molecular cloning, chromosomal mapping, and developmental expression of a novel protein tyrosine phosphatase-like gene [12].
• The combination of glutamic acid decarboxylase (GAD) 65 antibodies (GADA) and protein tyrosine phosphatase-like protein IA2 antibodies (IA2-ab), measured by radioligand binding assays, has been suggested to replace islet cell antibodies (ICA), measured by indirect immunofluorescence, as a marker for autoimmune type I diabetes [16].
• Radioimmunoassay was applied to detect antibodies to glutamic acid decarboxylase (GAD-Ab), intracellular part of protein tyrosine phosphatase-like protein (IA2ic-Ab), and autoantibodies to insulin (IAA) [17].
• The synthesis of DNA in two hypotrichous ciliates, Styx sp. and an amicronucleated strain of Oxytricha sp., was studied by high voltage (1000 kV) electron microscopy [7].

References