遗传 ›› 2023, Vol. 45 ›› Issue (4): 295-305.doi: 10.16288/j.yczz.22-366

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绵羊FecB突变对BMPR1B活性及BMP/SMAD通路的影响研究进展

龚一鸣(), 王翔宇, 贺小云, 刘玉芳, 余平, 储明星(), 狄冉()   

  1. 中国农业科学院北京畜牧兽医研究所,农业农村部动物遗传育种与繁殖重点实验室,北京 100193
  • 收稿日期:2022-11-17 修回日期:2023-02-06 出版日期:2023-04-20 发布日期:2023-03-28
  • 通讯作者: 储明星,狄冉 E-mail:g18080010835@163.com;dirangirl@163.com;mxchu@263.net
  • 作者简介:龚一鸣,在读硕士研究生,专业方向:动物遗传育种。E-mail: g18080010835@163.com
  • 基金资助:
    国家自然科学基金项目(32272838);国家自然科学基金项目(31861143012);财政部和农业农村部国家现代农业产业技术体系专项(CARS-38);中国农业科学院科技创新工程(CAAS-ZDRW202106);中国农业科学院科技创新工程(ASTIP-IAS13)

Progress on the effect of FecB mutation on BMPR1B activity and BMP/SMAD pathway in sheep

Yiming Gong(), Xiangyu Wang, Xiaoyun He, Yufang Liu, Ping Yu, Mingxing Chu(), Ran Di()   

  1. Key Laboratory of Animal Genetics, Breeding and Reproduction of Ministry of Agriculture and Rural Affairs, Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, China
  • Received:2022-11-17 Revised:2023-02-06 Online:2023-04-20 Published:2023-03-28
  • Contact: Chu Mingxing,Di Ran E-mail:g18080010835@163.com;dirangirl@163.com;mxchu@263.net
  • Supported by:
    National Natural Science Foundation of China(32272838);National Natural Science Foundation of China(31861143012);Earmarked Fund for China Agriculture Research System of MOF and MARA(CARS-38);Agricultural Science and Technology Innovation Program of China(CAAS-ZDRW202106);Agricultural Science and Technology Innovation Program of China(ASTIP-IAS13)

摘要:

BMPR1B是绵羊中被鉴定的第一个多羔主效基因,但该基因中FecB突变增加绵羊排卵数的分子机制尚未解析。近年来发现BMPR1B活性受小分子抑制蛋白FKBP1A调控,该蛋白充当了BMPR1B及BMP/SMAD通路活性控制开关的关键作用且FecB突变恰好位于FKBP1A与BMPR1B结合位点附近。本文首先总结了BMPR1B和FKBP1A的蛋白结构,阐明二者空间结合区域及FecB突变的位置,进而预测了FecB突变与二者结合强弱的关系,最终提出了FecB突变通过影响BMPR1B与FKBP1A结合强度改变BMP/SMAD通路活性的科学假设,为后续探明FecB突变影响绵羊排卵数的分子机制提供了新思路。

关键词: 绵羊, FecB突变, BMPR1B, FKBP1A, BMP/SMAD通路

Abstract:

BMPR1B is the first major gene of litter size identified in sheep. However, the molecular mechanism of the FecB mutation that increases the ovulation rate in sheep is still unclear. In recent years, it has been demonstrated that BMPR1B activity is regulated by the small molecule repressor protein FKBP1A, which acts as a key activity switch of the BMPR1B in the BMP/SMAD pathway. The FecB mutation is located close to the binding site of FKBP1A and BMPR1B. In this review, we summarize the structure of BMPR1B and FKBP1A proteins, and clarify the spatial interactive domains of the two proteins with respect to the location of the FecB mutation. Then the relationship between the FecB mutation and the degree of affinity of the two proteins are predicted. Finally, the hypothesis that FecB mutation causes change of activity in BMP/SMAD pathway by affecting the intensity of the interactions between BMPR1B and FKBP1A is proposed. This hypothesis provides a new clue to investigate the molecular mechanism of FecB mutation affecting ovulation rate and litter size in sheep.

Key words: sheep, FecB mutation, BMPR1B, FKBP1A, BMP/SMAD pathway