EPLIN regulates actin dynamics by cross-linking and stabilizing filaments.
EPLIN regulates actin dynamics by cross-linking and stabilizing filaments.
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Eplin通过交联和稳定细丝来调节肌动蛋白动力学。
DOI：
10.1083/jcb.200212057
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发表时间：
2003-02-03
影响因子：
7.8
通讯作者：
Chang, David D
中科院分区：
文献类型：
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作者：
Maul, Raymond S;Song, Yuhong;Amann, Kurt J;Gerbin, Sachi C;Pollard, Thomas D;Chang, David D
肿瘤中丢失的上皮蛋白（EPLIN）是一种细胞凋亡相关蛋白，由在转化细胞中下调的基因编码。EPLIN增加肌动蛋白应力纤维的数量和大小，并抑制由Rac诱导的膜皱褶。EPLIN至少有两个肌动蛋白结合位点。纯化的重组EPLIN抑制肌动蛋白丝解聚并将丝交联成束。EPLIN不影响肌动蛋白在倒刺末端的自发聚合或伸长的动力学，但通过Arp 2/3复合物抑制肌动蛋白丝的分支成核。侧结合活性可以稳定纤维并解释Arp 2/3复合物介导的成核抑制。我们认为，EPLIN促进了稳定的肌动蛋白丝结构，如应力纤维的形成，而牺牲了更动态的肌动蛋白丝结构，如膜皱褶。EPLIN的表达减少可能有助于侵袭性肿瘤细胞的运动。
Epithelial protein lost in neoplasm (EPLIN) is a cytoskeleton-associated protein encoded by a gene that is down-regulated in transformed cells. EPLIN increases the number and size of actin stress fibers and inhibits membrane ruffling induced by Rac. EPLIN has at least two actin binding sites. Purified recombinant EPLIN inhibits actin filament depolymerization and cross-links filaments in bundles. EPLIN does not affect the kinetics of spontaneous actin polymerization or elongation at the barbed end, but inhibits branching nucleation of actin filaments by Arp2/3 complex. Side binding activity may stabilize filaments and account for the inhibition of nucleation mediated by Arp2/3 complex. We propose that EPLIN promotes the formation of stable actin filament structures such as stress fibers at the expense of more dynamic actin filament structures such as membrane ruffles. Reduced expression of EPLIN may contribute to the motility of invasive tumor cells.