期刊
SCIENTIFIC REPORTS
卷 6, 期 -, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/srep27456
关键词
-
资金
- Biotechnology and Biological Sciences Research Council [BB/G012652/1, BB/H017828/1]
- Wellcome Trust [GR075373MA, WT078825AIA, 097820/Z/11/Z]
- FP7 EU Marie Curie postdoctoral intra-European fellowship [MDPTAR 272156]
- Netherlands Organization for Scientific Research [821.02.005]
- Biotechnology and Biological Sciences Research Council [BB/H017828/1, BB/G012652/1] Funding Source: researchfish
- BBSRC [BB/H017828/1, BB/G012652/1] Funding Source: UKRI
- Wellcome Trust [097820/Z/11/Z] Funding Source: Wellcome Trust
Microtubules and their associated proteins (MAPs) underpin the polarity of specialised cells. Adenomatous polyposis coli (APC) is one such MAP with a multifunctional agenda that requires precise intracellular localisations. Although APC has been found to associate with kinesin-2 subfamily members, the exact mechanism for the peripheral localization of APC remains unclear. Here we show that the heavy chain of kinesin-1 directly interacts with the APC C-terminus, contributing to the peripheral localisation of APC in fibroblasts. In rat hippocampal neurons the kinesin-1 binding domain of APC is required for its axon tip enrichment. Moreover, we demonstrate that APC requires interactions with both kinesin-2 and kinesin-1 for this localisation. Underlining the importance of the kinesin-1 association, neurons expressing APC lacking kinesin-1-binding domain have shorter axons. The identification of this novel kinesin-1-APC interaction highlights the complexity and significance of APC localisation in neurons.
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