Centrosome separation driven by actin-microfilaments during mitosis is mediated by centrosome-associated tyrosine-phosphorylated cortactin

Wang, Wenqi; Chen, Luyun; Ding, Yubo; Jin, Jing; Liao, Kan

doi:10.1242/jcs.018176

Cited by 63 publications

(46 citation statements)

References 32 publications

(70 reference statements)

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“…In FaDu cells serum starvation alone led to only partial synchrony, and therefore cells were synchronized in G 1 phase by a combination of serum starvation and hydroxyurea treatment ( Fig. 1c) (53). Upon release from this G 1 block into medium containing serum but lacking hydroxyurea, bromodeoxyuridine (BrdU) incorporation was used to quantify the percentage of cells that had entered S phase after 6 h (Fig.…”

Section: Resultsmentioning

confidence: 99%

Cortactin Modulates RhoA Activation and Expression of Cip/Kip Cyclin-Dependent Kinase Inhibitors To Promote Cell Cycle Progression in 11q13-Amplified Head and Neck Squamous Cell Carcinoma Cells

Croucher

Rickwood

Tactacan

et al. 2010

Molecular and Cellular Biology

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The cortactin oncoprotein is frequently overexpressed in head and neck squamous cell carcinoma (HNSCC), often due to amplification of the encoding gene (CTTN). While cortactin overexpression enhances invasive potential, recent research indicates that it also promotes cell proliferation, but how cortactin regulates the cell cycle machinery is unclear. In this article we report that stable short hairpin RNA-mediated cortactin knockdown in the 11q13-amplified cell line Cortactin is an F-actin binding protein involved in a variety of cellular processes, including endocytosis, vesicle trafficking, and the formation of cellular protrusions such as lamellipodia (14). In order to mediate these functions, cortactin interacts with a variety of proteins depending on the cell type and subcellular compartment, and this is achieved via distinct binding domains located within the cortactin molecule. The N terminus of cortactin harbors an acidic region that represents the interaction site for the actin-polymerizing Arp2/Arp3 complex, and this is followed by a repeat region containing the F-actin binding site. A Src homology 3 (SH3) domain located at the C terminus of cortactin recruits diverse proteins, including components of the endocytosis machinery (e.g., CD2AP and dynamin) and regulators of Rho family GTPases (e.g., BPGAP1 and Fgd1) and actin polymerization (e.g., N-WASP), while an adjacent proline-rich region contains phosphorylation sites for Src family kinases (14).The cortactin gene (CTTN) is located at chromosome band 11q13, a region that is commonly amplified in many human malignancies, particularly breast, ovarian, and bladder cancers and head and neck squamous cell carcinoma (HNSCC) (43).Several genes lie within this chromosomal region and are overexpressed upon its amplification. However, of these genes, the amplification of cyclin D1 (CCND1) and CTTN is most frequently associated with poor clinical outcomes such as decreased patient survival and increased metastasis (34,43). Chromosomal mapping of the 11q13 locus has revealed four distinct regions that can be individually or coordinately amplified (12,20,34). Within this locus, CCND1 and CTTN are located on different amplicons, and independent amplification of these genes has been demonstrated (34). In HNSCC, a tumor type in which 11q13 amplification occurs at the relatively high frequency of ϳ30% (43), CTTN amplification has been identified as an independent predictor of reduced disease-specific survival while CCND1 amplification is not prognostic in this tumor type (16,18,38,39). This strongly suggests that cortactin overexpression can act independently to promote tumor progression in cases of HNSCC.Due to the ability of cortactin to promote actin polymerization, many previous studies on cancer cells have focused on the role of cortactin in promoting cell motility and invasion (35,40,54), effects mediated by increased lamellipodial persistence (5), invadopodia formation (4), and protease secretion (10, 11). In agreement with this, cortactin overexpression has b...

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Section: Resultsmentioning

confidence: 99%

Cortactin Modulates RhoA Activation and Expression of Cip/Kip Cyclin-Dependent Kinase Inhibitors To Promote Cell Cycle Progression in 11q13-Amplified Head and Neck Squamous Cell Carcinoma Cells

Croucher

Rickwood

Tactacan

et al. 2010

Molecular and Cellular Biology

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“…Immunofluorescent Staining-Immunofluorescent staining was performed as described previously (50). Briefly, cells cultured on coverslips were fixed with 4% paraformaldehyde for 10 min at room temperature and then cells were extracted with 0.5% Triton X-100 solution for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Defining the Protein–Protein Interaction Network of the Human Hippo Pathway

Wang

Huang

et al. 2014

Molecular & Cellular Proteomics

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124

120

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The Hippo pathway, which is conserved from Drosophila to mammals, has been recognized as a tumor suppressor signaling pathway governing cell proliferation and apoptosis, two key events involved in organ size control and tumorigenesis. Although several upstream regulators, the conserved kinase cascade and key downstream effectors including nuclear transcriptional factors have been defined, the global organization of this signaling pathway is not been fully understood. Thus, we conducted a proteomic analysis of human Hippo pathway, which revealed the involvement of an extensive protein-protein interaction network in this pathway. The mass spectrometry data were deposited to ProteomeXchange with identifier PXD000415. Our data suggest that 550 interactions within 343 unique protein components constitute the central protein-protein interaction landscape of human Hippo pathway. Our study provides a glimpse into the global organization of Hippo pathway, reveals previously unknown interactions within this pathway, and uncovers new potential components involved in the regulation of this pathway. Understanding these interactions will help us further dissect the Hippo signaling-pathway and extend our knowledge of organ size control. Molecular &

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“…Immunofluorescent staining was performed as described previously (Wang et al 2008). Briefly, cells cultured on coverslips were fixed by 4% paraformaldehyde for 10 min at room temperature and then extracted with 0.5% Triton X-100 solution for 5 min.…”

Section: Immunofluorescent Stainingmentioning

confidence: 99%

PTPN14 is required for the density-dependent control of YAP1

et al. 2012

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Through an shRNA-mediated loss-of-function screen, we identified PTPN14 as a potential tumor suppressor. PTPN14 interacts with yes-associated protein 1 (YAP1), a member of the hippo signaling pathway. We showed that PTPN14 promotes the nucleus-to-cytoplasm translocation of YAP1 during contact inhibition and thus inhibits YAP1 transactivation activity. Interestingly, PTPN14 protein stability was positively controlled by cell density. We identified the CRL2 LRR1 (cullin2 RING ubiquitin ligase complex/leucine-rich repeat protein 1) complex as the E3 ligase that targets PTPN14 for degradation at low cell density. Collectively, these data suggest that PTPN14 acts to suppress cell proliferation by promoting cell density-dependent cytoplasmic translocation of YAP1.

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Centrosome separation driven by actin-microfilaments during mitosis is mediated by centrosome-associated tyrosine-phosphorylated cortactin

Cited by 63 publications

References 32 publications

Cortactin Modulates RhoA Activation and Expression of Cip/Kip Cyclin-Dependent Kinase Inhibitors To Promote Cell Cycle Progression in 11q13-Amplified Head and Neck Squamous Cell Carcinoma Cells

Cortactin Modulates RhoA Activation and Expression of Cip/Kip Cyclin-Dependent Kinase Inhibitors To Promote Cell Cycle Progression in 11q13-Amplified Head and Neck Squamous Cell Carcinoma Cells

Defining the Protein–Protein Interaction Network of the Human Hippo Pathway

PTPN14 is required for the density-dependent control of YAP1

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