EVI5 is a novel centrosomal protein that binds to α- and γ-tubulin
EVI5 is a novel centrosomal protein that binds to α- and γ-tubulin
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DOI：
10.1016/j.ygeno.2005.06.002
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发表时间：
2005-11-01
期刊：
影响因子：
4.4
通讯作者：
Cowell, JK
中科院分区：
文献类型：
--
作者：
Faitar, SL;Dabbeekeh, JTS;Cowell, JK
人EV 15蛋白携带指示Rab GT3活化蛋白（GAP）活性的TBC结构域和C-末端区域中的广泛卷曲螺旋基序。EV 15在成人、胎儿和癌症组织中普遍表达，并因多聚腺苷酸化信号的差异使用而以两种mRNA形式存在。蛋白质印迹分析表明，不同分子量的蛋白质种类可能是由翻译后修饰产生的。FPLC分析表明，EV 15蛋白可以形成二聚体和共聚焦显微镜表明，EV 15，除了在细胞核中的弥漫性定位，也优先定位于间期细胞的中心粒周围材料。免疫沉淀和GST下拉实验表明，EV 15存在于与α和γ微管蛋白的复合物中。两种相互作用都定位于EV 15蛋白的N-末端部分。因此，EV 15是一种新的中心体蛋白，具有复杂的表达模式和亚细胞定位，可能参与中心体的稳定性和动力学。(c)2005年爱思唯尔公司All rights reserved.
The human EV15 protein carries a TBC domain indicative of Rab GTPase activating protein (GAP) activity, and an extensive coiled-coil motif in the C-terminal region. EV15 is ubiquitously expressed in adult, fetal, and cancer tissues and exists as two mRNA species resulting from differential use of polyadenylation signals. Western blot analysis suggests that different molecular weight protein species are probably generated by posttranslational modification. FPLC analysis demonstrates that EV15 protein can form dimers and confocal microscopy indicates that EV15, in addition to a diffuse localization in the nucleus, also preferentially localizes to the pericentriolar material in interphase cells. Immunoprecipitation and GST pull-down experiments demonstrate that EV15 exists in complexes with both alpha- and gamma-tubulin. Both interactions are localized to the N-terminal part of the EV15 protein. Thus, EV15 is a novel centrosomal protein with a complex expression pattern and subcellular localization, possibly involved in centrosome stability and dynamics. (c) 2005 Elsevier Inc. All rights reserved.