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Protein-tyrosine sulfotransferase 2

TPST2, tyrosylprotein sulfotransferase-2
The protein encoded by this gene catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The encoded protein is a type II integral membrane protein found in the Golgi body. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: tyrosylprotein sulfotransferase, ACID, fibrillin-1, CD45, CAN
Papers on TPST2
Computational Evidence for the Catalytic Mechanism of Tyrosylprotein Sulfotransferases: A Density Functional Theory Investigation.
Calvaresi et al., Bologna, Italy. In Biochemistry, Aug 2015
In this paper we have examined the mechanism of tyrosine O-sulfonation catalyzed by human TPST-2.
Heterodimers of tyrosylprotein sulfotransferases suggest existence of a higher organization level of transferases in the membrane of the trans-Golgi apparatus.
Bayer et al., Essen, Germany. In J Mol Biol, Apr 2015
The sole two human enzymes that transfer sulfate moieties from 3'-phospho-adenosine-5'-phospho-sulfate onto tyrosine residues, TPST1 and TPST2, are anchored to the membranes of the trans-Golgi compartment with the catalytic domain oriented to the lumen.
Tyrosine sulfation in the second variable loop (V2) of HIV-1 gp120 stabilizes V2-V3 interaction and modulates neutralization sensitivity.
Lusso et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2014
Recombinant gp120 expressed in continuous cell lines displays low constitutive levels of V2 tyrosine sulfation, which can be enhanced markedly by overexpression of the tyrosyl sulfotransferase TPST2.
[Screening of host cell proteins that interact with Toxoplasma gondii ROP18 via yeast two-hybrid system].
Shen et al., In Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi, 2013
Using the selection procedures, eight novel host cell proteins were obtained: damage-specific DNA binding protein 1 (DDB1), torsin A interacting protein 1 (TOR1AIP1), integrin beta 1, solute carrier family 3 (SLC3A2), tyrosyl protein sulfotransferase (TPST2), OCIA domain containing 1 (OCIAD1), Derl-like domain family member 2 (DERL2), in addition to Homo sapiens activating transcription factor 6 beta(ATF6).
Salivary gland hypofunction in tyrosylprotein sulfotransferase-2 knockout mice is due to primary hypothyroidism.
Moore et al., Oklahoma City, United States. In Plos One, 2012
BACKGROUND: Protein-tyrosine sulfation is a post-translational modification of an unknown number of secreted and membrane proteins mediated by two known Golgi tyrosylprotein sulfotransferases (TPST-1 and TPST-2).
Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction.
Kakuta et al., Fukuoka, Japan. In Nat Commun, 2012
Post-translational protein modification by tyrosine sulfation has an important role in extracellular protein-protein interactions.
Mice expressing aberrant sperm-specific protein PMIS2 produce normal-looking but fertilization-incompetent spermatozoa.
Okabe et al., Suita, Japan. In Mol Biol Cell, 2012
Eight kinds of gene-disrupted mice (Clgn, Calr3, Pdilt, Tpst2, Ace, Adam1a, Adam2, and Adam3) show impaired sperm transition into the oviducts and defective sperm binding to the zona pellucida.
Interactions between the ROP18 kinase and host cell proteins that aid in the parasitism of Toxoplasma gondii.
Du et al., Hefei, China. In Acta Trop, 2012
Using these selection procedures, we identified seven host proteins that had not previously been reported to interact with ROP18 such as DDB1, TOR1AIP1, integrin, SLC3A2, TPST2, DERL2 and OCIAD1.
Protein tyrosine-O-sulfation in bovine ocular tissues.
Al-Ubaidi et al., Oklahoma City, United States. In Adv Exp Med Biol, 2011
TPSP1 and TPSP2 provide an important posttranslational modification for vision.
Differential developmental deficits in retinal function in the absence of either protein tyrosine sulfotransferase-1 or -2.
Al-Ubaidi et al., Oklahoma City, United States. In Plos One, 2011
To investigate the role(s) of protein-tyrosine sulfation in the retina and to determine the differential role(s) of tyrosylprotein sulfotransferases (TPST) 1 and 2 in vision, retinal function and structure were examined in mice lacking TPST-1 or TPST-2.
Identifying quantitative trait loci affecting resistance to congenital hypothyroidism in 129/SvJcl strain mice.
Agui et al., Sapporo, Japan. In Plos One, 2011
Tyrosylprotein sulfotransferase 2 (TPST2) is one of the enzymes responsible for tyrosine O-sulfation and catalyzes the sulfation of the specific tyrosine residue of thyroid stimulating hormone receptor (TSHR).
Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm.
Evans et al., Baltimore, United States. In J Biol Chem, 2011
Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm.
Tyrosine sulfation of native mouse Psgl-1 is required for optimal leukocyte rolling on P-selectin in vivo.
Moore et al., Oklahoma City, United States. In Plos One, 2010
Data show that Tpst1/Tpst2 DKO leukocytes bound less P-selectin than wild type leukocytes despite equivalent surface expression of Psgl-1.
Lack of protein-tyrosine sulfation disrupts photoreceptor outer segment morphogenesis, retinal function and retinal anatomy.
Al-Ubaidi et al., Oklahoma City, United States. In Eur J Neurosci, 2010
These results indicate that protein-tyrosine sulfation by Tpst1/2 is essential for proper outer segment morphogenesis and synaptic function, but is not critical for overall retinal structure or synapse formation.
Impaired insulin secretion from the pancreatic islets of hypothyroidal growth-retarded mice.
Kobayashi et al., Saitama, Japan. In J Endocrinol, 2010
Considering that Tpst2 is the responsible gene of grt mice, mutation of which is associated with a poor function of TSH receptor, the findings raise the possibility of involvement of factors including Tpst2 in the insulin hyposecretion in grt mice.
Hypothyroid phenotype of the Tpst2 mutant mouse is dependent upon genetic background.
Agui et al., Sapporo, Japan. In Biomed Res, 2010
demonstrated that the Tpst2 transgene rescues the mutant phenotypes both in vitro and in vivo
Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins.
Zhu et al., Australia. In N Biotechnol, 2009
Recent advances in our understanding of protein tyrosine sulfation have come about owing to the cloning of two human tyrosylprotein sulfotransferases (TPST-1 and TPST-2), the development of novel analytical and synthetic methodologies and detailed studies of proteins and peptides containing sulfotyrosine residues.
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