TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
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DOI：
10.1242/jcs.143537
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发表时间：
2014-09
影响因子：
4
通讯作者：
P. Uchil;Tobias Pawliczek;T. D. Reynolds;Siyuan Ding;A. Hinz;James B. Munro;Fang Huang;R. W. Floyd;Haitao Yang;W. Hamilton;J. Bewersdorf;Y. Xiong;D. Calderwood;W. Mothes
中科院分区：
文献类型：
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作者：
P. Uchil;Tobias Pawliczek;T. D. Reynolds;Siyuan Ding;A. Hinz;James B. Munro;Fang Huang;R. W. Floyd;Haitao Yang;W. Hamilton;J. Bewersdorf;Y. Xiong;D. Calderwood;W. Mothes
摘要局灶性粘连是连接肌动蛋白细胞骨架和细胞外基质的大分子复合物。粘着斑的动态更新对细胞迁移至关重要。桩蛋白是一种多接头蛋白，在调节粘着斑动力学中起重要作用。在这里，我们确定TRIM15，三方基序蛋白家族的成员，作为一个paxillin相互作用的因素和局部粘连的一个组成部分。TRIM15通过其卷曲螺旋结构域与桩蛋白的LD 2基序之间的相互作用以肌球蛋白II独立的方式定位于局灶性接触。与其他粘着斑蛋白不同，TRIM15是一种稳定的粘着斑组分，由于其形成寡聚体的能力，其移动性受到限制。TRIM15耗尽的细胞显示受损的细胞迁移和降低的粘着斑分解率，除了扩大的粘着斑。因此，我们的研究证明了TRIM15作为粘着斑转换和细胞迁移的调节组分的细胞功能。
ABSTRACT Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multi-adaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15-depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.