A novel role for IQGAP1 protein in cell motility through cell retraction.
A novel role for IQGAP1 protein in cell motility through cell retraction.
复制标题
IQGAP1蛋白在细胞缩回中的新作用。
DOI：
10.1016/j.bbrc.2014.04.038
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发表时间：
2014-05-23
影响因子：
3.1
通讯作者：
Schober, Joseph M.
中科院分区：
文献类型：
--
作者：
Foroutannejad, Sahar;Rohner, Nathan;Reimer, Michael;Kwon, Guim;Schober, Joseph M.
IQGAP 1已成为细胞迁移、粘附连接维持、微生物发病机制和细胞内运输过程中细胞骨架动力学调节的关键组分。已知IQGAP 1定位于多种细胞类型中板状伪足的突出边缘，并与肌动蛋白动力学的调节因子相互作用。在这里，我们提供的证据表明IQGAP 1通过细胞边缘收缩在细胞运动中的新作用。在检查的一些细胞系中，IQGAP 1与WAVE定位明显分离，表明IQGAP 1可能定位于收缩边缘。B16 F10小鼠黑色素瘤细胞表现出最有限的分离，其中GFP-IQGAP 1的出现与细胞边缘收缩速度和mCherry-Arp 3的消失相关。这些结果表明，在某些细胞类型中，IQGAP 1可能起促进细胞收缩而不是板状伪足边缘突出的作用。此外，我们研究了IQGAP 1与粘附位点标记物、肌球蛋白IIA、钙调蛋白和IQGAP 2的共定位。在富含IQGAP 1的区域，黏着斑蛋白、桩蛋白和磷酸化酪氨酸的免疫荧光染色减少，表明粘附部位解体。有趣的是，钙调蛋白，而不是肌球蛋白IIA或IQGAP 2，与IQGAP 1共同定位在细胞收缩区域。总体而言，这些结果表明IQGAP 1（与IQGAP 2不同）在细胞迁移中的新作用，其通过上调收缩性和下调粘附位点（可能通过钙调蛋白相互作用）。
IQGAP1 has emerged as a key component in the regulation of cytoskeleton dynamics during cell migration, maintenance of adherens junctions, microbial pathogenesis and intracellular trafficking. IQGAP1 is known to localize to the protruding edge of lamellipodia in a variety of cell types and interact with regulators of actin dynamics. Here, we provide evidence suggesting a novel role of IQGAP1 in cell motility through cell edge retraction. In some of the cell lines examined, IQGAP1 was markedly separated from WAVE localization suggesting IQGAP1 may localize to retracting edges. B16F10 mouse melanoma cells exhibited the most restricted separation in which the appearance of GFP-IQGAP1 correlated with cell edge retraction velocity and the disappearance of mCherry-Arp3. These results demonstrate that in some cell types IQGAP1 may function to promote cell retraction not lamellipodium edge protrusion. In addition, we examined co-localization of IQGAP1 with adhesion site markers, myosin IIA, calmodulin and IQGAP2. In areas rich in IQGAP1 there was decreased immunofluorescence staining of vinculin, paxillin and phosphorylated-tyrosine indicating adhesion site disassembly. Interestingly, calmodulin, but not myosin IIA or IQGAP2, co-localized with IQGAP1 in areas of cell retraction. Overall these results suggest a new role of IQGAP1, distinct form IQGAP2, in cell migration through up regulation of contractility and downregulation of adhesion sites potentially through calmodulin interaction.
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