期刊
JOURNAL OF NEUROCHEMISTRY
卷 128, 期 3, 页码 391-402出版社
WILEY
DOI: 10.1111/jnc.12462
关键词
cytoskeletal regulation; cytoskeleton; molecular evolution; nerve cells; protein domain; protein function
资金
- BBSRC [BBD0178231]
- MRC
- BBSRC [BB/D017823/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D017823/1] Funding Source: researchfish
Calmodulin regulated spectrin-associated protein 1 (CAMSAP1) is a vertebrate microtubule-binding protein, and a representative of a family of cytoskeletal proteins that arose with animals. We reported previously that the central region of the protein, which contains no recognized functional domain, inhibited neurite outgrowth when over-expressed in PC12 cells [Baines etal., Mol. Biol. Evol. 26 (2009), p. 2005]. The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins (Baines etal. 2009). In the central region, three short well-conserved regions are characteristic of CAMSAP-family members. One of these, CAMSAP-conserved region 1 (CC1), bound to both II sigma 1-spectrin and Ca2+/calmodulin in vitro. The binding of Ca2+/calmodulin inhibited spectrin binding. Transient expression of CC1 in PC12 cells inhibited neurite outgrowth. siRNA knockdown of CAMSAP1 inhibited neurite outgrowth in PC12 cells or primary cerebellar granule cells: this could be rescued in PC12 cells by wild-type CAMSAP1-enhanced green fluorescent protein, but not by a CC1 mutant. We conclude that CC1 represents a functional region of CAMSAP1, which links spectrin-binding to neurite outgrowth.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据