d-Serine controls epidermal vesicle release via NMDA receptor, allowing tissue migration during the metamorphosis of the chordate <i>Ciona</i>. Krasovec, G., Hozumi, A., Yoshida, T., Obita, T., Hamada, M., Shiraishi, A., Satake, H., Horie, T., Mori, H., & Sasakura, Y. Science Advances, 8(10):eabn3264, March, 2022.
d-Serine controls epidermal vesicle release via NMDA receptor, allowing tissue migration during the metamorphosis of the chordate <i>Ciona</i> [link]Paper  doi  abstract   bibtex   30 downloads  
d -Serine, a free amino acid synthesized by serine racemase, is a coagonist of N -methyl- d -aspartate–type glutamate receptor (NMDAR). d -Serine in the mammalian central nervous system modulates glutamatergic transmission. Functions of d -serine in mammalian peripheral tissues such as skin have also been described. However, d -serine’s functions in nonmammals are unclear. Here, we characterized d -serine–dependent vesicle release from the epidermis during metamorphosis of the tunicate Ciona . d -Serine leads to the formation of a pocket that facilitates the arrival of migrating tissue during tail regression. NMDAR is the receptor of d -serine in the formation of the epidermal pocket. The epidermal pocket is formed by the release of epidermal vesicles’ content mediated by d -serine/NMDAR. This mechanism is similar to observations of keratinocyte vesicle exocytosis in mammalian skin. Our findings provide a better understanding of the maintenance of epidermal homeostasis in animals and contribute to further evolutionary perspectives of d -amino acid function among metazoans. , Tunicates and mammals have a shared mechanism in the regulation of epidermal vesicle release mediated by d -serine and NMDAR.
@article{krasovec_d-serine_2022,
	title = {d-{Serine} controls epidermal vesicle release via {NMDA} receptor, allowing tissue migration during the metamorphosis of the chordate \textit{{Ciona}}},
	volume = {8},
	issn = {2375-2548},
	shorttitle = {{\textless}span style="font-variant},
	url = {https://www.science.org/doi/10.1126/sciadv.abn3264},
	doi = {10.1126/sciadv.abn3264},
	abstract = {d
              -Serine, a free amino acid synthesized by serine racemase, is a coagonist of
              N
              -methyl-
              d
              -aspartate–type glutamate receptor (NMDAR).
              d
              -Serine in the mammalian central nervous system modulates glutamatergic transmission. Functions of
              d
              -serine in mammalian peripheral tissues such as skin have also been described. However,
              d
              -serine’s functions in nonmammals are unclear. Here, we characterized
              d
              -serine–dependent vesicle release from the epidermis during metamorphosis of the tunicate
              Ciona
              .
              d
              -Serine leads to the formation of a pocket that facilitates the arrival of migrating tissue during tail regression. NMDAR is the receptor of
              d
              -serine in the formation of the epidermal pocket. The epidermal pocket is formed by the release of epidermal vesicles’ content mediated by
              d
              -serine/NMDAR. This mechanism is similar to observations of keratinocyte vesicle exocytosis in mammalian skin. Our findings provide a better understanding of the maintenance of epidermal homeostasis in animals and contribute to further evolutionary perspectives of
              d
              -amino acid function among metazoans.
            
          , 
            
              Tunicates and mammals have a shared mechanism in the regulation of epidermal vesicle release mediated by
              d
              -serine and NMDAR.},
	language = {en},
	number = {10},
	urldate = {2022-03-14},
	journal = {Science Advances},
	author = {Krasovec, Gabriel and Hozumi, Akiko and Yoshida, Tomoyuki and Obita, Takayuki and Hamada, Mayuko and Shiraishi, Akira and Satake, Honoo and Horie, Takeo and Mori, Hisashi and Sasakura, Yasunori},
	month = mar,
	year = {2022},
	pages = {eabn3264},
}

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