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NIP2/中心体蛋白(centrobin)的特性鉴定,Nek2的一种新型底物及其在微管稳定中的潜在作用

Characterization of NIP2/centrobin, a novel substrate of Nek2, and its potential role in microtubule stabilization.

作者信息

Jeong Yeontae, Lee Jungmin, Kim Kyeongmi, Yoo Jae Cheal, Rhee Kunsoo

机构信息

Department of Biological Sciences and Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea.

出版信息

J Cell Sci. 2007 Jun 15;120(Pt 12):2106-16. doi: 10.1242/jcs.03458. Epub 2007 May 29.

Abstract

Nek2 is a mitotic kinase whose activity varies during the cell cycle. It is well known that Nek2 is involved in centrosome splitting, and a number of studies have indicated that Nek2 is crucial for maintaining the integrity of centrosomal structure and microtubule nucleation activity. In the present study, we report that NIP2, previously identified as centrobin, is a novel substrate of Nek2. NIP2 was daughter-centriole-specific, but was also found in association with a stable microtubule network of cytoplasm. Ectopic NIP2 formed aggregates but was dissolved by Nek2 into small pieces and eventually associated with microtubules. Knockdown of NIP2 showed significant reduction of microtubule organizing activity, cell shrinkage, defects in spindle assembly and abnormal nuclear morphology. Based on our results, we propose that NIP2 has a role in stabilizing the microtubule structure. Phosphorylation may be crucial for mobilization of the protein to a new microtubule and stabilizing it.

摘要

Nek2是一种有丝分裂激酶,其活性在细胞周期中会发生变化。众所周知,Nek2参与中心体分裂,并且多项研究表明,Nek2对于维持中心体结构的完整性和微管成核活性至关重要。在本研究中,我们报告称,先前被鉴定为中心粒结合蛋白的NIP2是Nek2的一种新底物。NIP2是子代中心粒特异性的,但也发现它与细胞质中的稳定微管网络相关联。异位表达的NIP2形成聚集体,但被Nek2分解成小块并最终与微管相关联。敲低NIP2会导致微管组织活性显著降低、细胞收缩、纺锤体组装缺陷和异常的核形态。基于我们的研究结果,我们提出NIP2在稳定微管结构中发挥作用。磷酸化对于将该蛋白转运到新的微管并使其稳定可能至关重要。

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