Interaction of secreted factor Agr2 with its potential receptors from the family of three-finger proteins
- Authors: Eroshkin F.M.1, Martynova N.Y.1, Bayramov A.V.1, Ermakova G.V.1, Ivanova A.S.1, Korotkova D.D.1, Zaraisky A.G.1
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Affiliations:
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
- Issue: Vol 43, No 3 (2017)
- Pages: 344-346
- Section: Letter to the Editor
- URL: https://journals.rcsi.science/1068-1620/article/view/228560
- DOI: https://doi.org/10.1134/S1068162017030049
- ID: 228560
Cite item
Abstract
Interactions of the secreted protein XAgr2 of the Agr (anterior gradient proteins) family with six submembrane proteins, Tfp1–6, from the family of three-finger proteins Ly6 were studied in Xenopus laevis embryos. Earlier, other authors have shown that the newt homologue of XAgr2 is able to bind the Prod1 three-finger protein, which participates in the establishment of the proximal-to-distal pattern of cell differentiation in the regenerating blastema of a newt’s limb bud. Here, we identified six homologues of Prod1 in Xenopus laevis genome named Tfp1–6. By co-immunoprecipitation, we demonstrated that among these homologues, Tfp4 is the most probable receptor of XAgr2. Further study of the revealed interactions between XAgr2 and Tfp4 is of significant interest because XAgr2 is involved in the signaling pathways that regulate neural system development and the body appendages regeneration.
Keywords
About the authors
F. M. Eroshkin
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Author for correspondence.
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997
N. Y. Martynova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997
A. V. Bayramov
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997
G. V. Ermakova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997
A. S. Ivanova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997
D. D. Korotkova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997
A. G. Zaraisky
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: xenopus.fe@gmail.com
Russian Federation, Moscow, 117997