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DEPDC1B 协调有丝分裂过程中的去黏附事件和细胞周期进程。

DEPDC1B coordinates de-adhesion events and cell-cycle progression at mitosis.

机构信息

Istituto Europeo di Oncologia (IEO), 20141 Milan, Italy; Fondazione IFOM-Istituto FIRC di Oncologia Molecolare, 20139 Milan, Italy; Center for Genomic Science of IIT@SEMM, Istituto Italiano di Tecnologia (IIT), 20139 Milan, Italy.

Istituto Europeo di Oncologia (IEO), 20141 Milan, Italy.

出版信息

Dev Cell. 2014 Nov 24;31(4):420-33. doi: 10.1016/j.devcel.2014.09.009.

DOI:10.1016/j.devcel.2014.09.009
PMID:25458010
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4250264/
Abstract

Cells entering mitosis become rounded, lose attachment to the substrate, and increase their cortical rigidity. Pivotal to these events is the dismantling of focal adhesions (FAs). How mitotic reshaping is linked to commitment to divide is unclear. Here, we show that DEPDC1B, a protein that accumulates in G2, coordinates de-adhesion events and cell-cycle progression at mitosis. DEPDC1B functions as an inhibitor of a RhoA-based signaling complex, which assembles on the FA-associated protein tyrosine phosphatase, receptor type, F (PTPRF) and mediates the integrity of FAs. By competing with RhoA for the interaction with PTPRF, DEPDC1B promotes the dismantling of FAs, which is necessary for the morphological changes preceding mitosis. The circuitry is relevant in whole organisms, as shown by the control exerted by the DEPDC1B/RhoA/PTPRF axis on mitotic dynamics during zebrafish development. Our results uncover an adhesion-dependent signaling mechanism that coordinates adhesion events with the control of cell-cycle progression.

摘要

进入有丝分裂的细胞会变成圆形，失去与基质的附着，并增加皮质刚性。这些事件的关键是焦点粘连（FA）的解体。有丝分裂重塑如何与分裂的承诺联系在一起尚不清楚。在这里，我们表明，在 G2 中积累的蛋白 DEPDC1B 协调有丝分裂过程中的脱附事件和细胞周期进程。DEPDC1B 作为基于 RhoA 的信号复合物的抑制剂起作用，该复合物组装在 FA 相关的蛋白酪氨酸磷酸酶受体型 F（PTPRF）上，并介导 FA 的完整性。通过与 RhoA 竞争与 PTPRF 的相互作用，DEPDC1B 促进 FA 的解体，这对于有丝分裂前的形态变化是必要的。该电路在整个生物体中都是相关的，正如 DEPDC1B/RhoA/PTPRF 轴在斑马鱼发育过程中对有丝分裂动力学的控制所表明的那样。我们的结果揭示了一种依赖于粘附的信号机制，该机制协调粘附事件与细胞周期进程的控制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/acca39d449bb/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/b4cc390de0fb/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/2725a7b5f326/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/af4af8f6cc93/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/026dfb0998c5/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/933dbf247316/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/cc1d4507ecd9/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/a832ad445bf3/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/acca39d449bb/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/b4cc390de0fb/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/2725a7b5f326/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/af4af8f6cc93/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/026dfb0998c5/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/933dbf247316/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/cc1d4507ecd9/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/a832ad445bf3/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0f2c/4250264/acca39d449bb/gr7.jpg

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