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Published on: January 26, 2013
The sulfotransferase XB5850668.L is required to apportion embryonic ectodermal domains
Alexander Marchak1, Karen M Neilson1, Himani D Majumdar1
1Department of Anatomy and Cell Biology, George Washington University, School of Medicine and Health Sciences, Washington, District of Columbia, USA.
Six1 regulates XB5850668.L, a sulfotransferase (SULT2) important for embryonic ectoderm patterning. Its activity influences neural plate, neural crest, and placode development during embryogenesis.
Area of Science:
- Developmental biology
- Molecular biology
- Biochemistry
Background:
- Sulfotransferase superfamily (SULT) enzymes modulate diverse biological molecules but their roles in embryonic development are not well understood.
- Six1, a key developmental regulator, was found to up-regulate LOC100037047, encoding the uncharacterized sulfotransferase XB5850668.L.
Purpose of the Study:
- To investigate the function of the uncharacterized sulfotransferase XB5850668.L in embryonic ectoderm patterning.
- To determine the role of XB5850668.L in processes regulated by the developmental gene Six1.
Main Methods:
- Loss- and gain-of-function assays were employed to study XB5850668.L.
- Gene expression domains for neural plate, neural crest, cranial placode, and otic vesicles were analyzed.
- Mutagenesis of the sulfotransferase catalytic domain was performed to assess the role of enzymatic activity.
Main Results:
- Knockdown of XB5850668.L led to reduced expression of epidermal, neural crest, cranial placode, and otic vesicle genes, with concurrent neural plate expansion.
- Overexpression of XB5850668.L had minor effects, occasionally expanding neural plate and neural crest domains while reducing placode and otic vesicle domains.
- Mutating key catalytic residues of XB5850668.L diminished the effects observed with wild-type protein overexpression.
Conclusions:
- XB5850668.L, a member of the SULT2 family, is crucial for embryonic ectoderm patterning.
- The observed effects of XB5850668.L on development are, in part, dependent on its sulfotransferase enzymatic activity.
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