GIPC1 Interacts with MyoGEF and Promotes MDA-MB-231 Breast Cancer Cell Invasion

Wu, Di; Haruta, Akiko; Wei, Qize

doi:10.1074/jbc.m110.107649

Cited by 18 publications

(21 citation statements)

References 58 publications

(58 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To test this possibility, we examined whether exogenous expression of a carboxyl-terminal fragment lacking the carboxyl-terminal PDZ-binding motif (MyoGEF-501-780-⌬SEV) interfered with actin filament formation. We have found previously that MyoGEF polypeptides that lack the carboxyl-terminal three residues (SEV) do not bind to GIPC1 (46). As shown in Fig.…”

Section: Resultsmentioning

confidence: 78%

“…Our previous findings have shown that the carboxyl-terminal end of MyoGEF contains a PDZ-binding motif that can interact with the PDZ domain-containing protein GIPC1 (46). Therefore, it is possible that exogenous expression of MyoGEF-501-790, which contains the carboxyl-terminal PDZ-binding motif, could interfere with actin organization by disrupting the GIPC1-MyoGEF interaction.…”

Section: Resultsmentioning

confidence: 99%

“…Our findings demonstrate that exogenous expression of the MyoGEF carboxylterminal region interferes with MyoGEF functions, leading to cytokinesis defects and decreasing breast cancer cell invasion. It has been shown that the carboxyl-terminal region of MyoGEF can interact with centrosome/spindle-associated protein (CSPP), ezrin, and GIPC1 (46,47,58). Aurora B and Plk1 can phosphorylate the carboxyl-terminal region of MyoGEF (31,32).…”

Section: Discussionmentioning

confidence: 99%

“…We have found previously that the PH domain of MyoGEF can interact with nonmuscle myosin II (15,24). The PDZ domain of GIPC1 can bind to the carboxyl-terminal PDZ-binding motif of MyoGEF, and the GIPC1-MyoGEF interaction is implicated in promoting breast cancer cell invasion (46). The ezrin-radixinmoesin proteins can link the plasma membrane to actin filaments and play a critical role in organizing the cell cortex and promoting breast tumor metastasis (73,74).…”

Section: Discussionmentioning

confidence: 99%

“…We have reported previously that MyoGEF plays an important role in the regulation of cytokinesis and breast cancer cell invasion (15,24,31,32,46,47). MyoGEF is highly expressed in invasive breast cancer cells and tissues (15).…”

Section: We Have Reported Previously That Nonmuscle Myosin Ii-interacmentioning

confidence: 99%

See 4 more Smart Citations

Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Jiao

et al. 2014

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: MyoGEF is implicated in regulating cytokinesis and breast cancer cell invasion. Results: Binding of the MyoGEF carboxyl-terminal region to its DH domain suppresses breast cancer cell invasion and interferes with cytokinesis. Conclusion: Intramolecular interactions of MyoGEF act as an autoinhibitory mechanism to regulate MyoGEF functions. Significance: Autoinhibitory intramolecular interactions of MyoGEF serve as a control point to regulate cytokinesis and breast cancer cell invasion.

show abstract

Section: Resultsmentioning

confidence: 78%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: We Have Reported Previously That Nonmuscle Myosin Ii-interacmentioning

confidence: 99%

See 3 more Smart Citations

Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Jiao

et al. 2014

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

G protein‐coupled receptors participate in cytokinesis

et al. 2012

View full text Add to dashboard Cite

Cytokinesis, the last step during cell division, is a highly coordinated process that involves the relay of signals from both the outside and inside of the cell. We have a basic understanding of how cells regulate internal events, but how cells respond to extracellular cues is less explored. In a systematic RNAi screen of G-protein-coupled receptors (GPCRs) and their effectors, we found that some GPCRs are involved in cytokinesis. RNAi knockdown of these GPCRs caused increased binucleated cell formation, and live cell imaging showed that most formed midbodies but failed at the abscission stage. OR2A4 localized to cytokinetic structures in cells and its knockdown caused cytokinesis failure at an earlier stage, likely due to effects on the actin cytoskeleton. Identifying the downstream components that transmit GPCR signals during cytokinesis will be the next step and we show that GIPC1, an adaptor protein for GPCRs, may play a part. RNAi knockdown of GIPC1 significantly increased binucleated cell formation. Understanding the molecular details of GPCRs and their interaction proteins in cytokinesis regulation will give us important clues about GPCRs signaling as well as how cells communicate with their environment during division.

show abstract

Genome‐wide association study of INDELs identified four novel susceptibility loci associated with lung cancer risk

Dai

Huang

Amos³

et al. 2019

Intl Journal of Cancer

View full text Add to dashboard Cite

Genome‐wide association studies (GWAS) have identified 45 susceptibility loci associated with lung cancer. Only less than SNPs, small insertions and deletions (INDELs) are the second most abundant genetic polymorphisms in the human genome. INDELs are highly associated with multiple human diseases, including lung cancer. However, limited studies with large‐scale samples have been available to systematically evaluate the effects of INDELs on lung cancer risk. Here, we performed a large‐scale meta‐analysis to evaluate INDELs and their risk for lung cancer in 23,202 cases and 19,048 controls. Functional annotations were performed to further explore the potential function of lung cancer risk INDELs. Conditional analysis was used to clarify the relationship between INDELs and SNPs. Four new risk loci were identified in genome‐wide INDEL analysis (1p13.2: rs5777156, Insertion, OR = 0.92, p = 9.10 × 10−8; 4q28.2: rs58404727, Deletion, OR = 1.19, p = 5.25 × 10−7; 12p13.31: rs71450133, Deletion, OR = 1.09, p = 8.83 × 10−7; and 14q22.3: rs34057993, Deletion, OR = 0.90, p = 7.64 × 10−8). The eQTL analysis and functional annotation suggested that INDELs might affect lung cancer susceptibility by regulating the expression of target genes. After conducting conditional analysis on potential causal SNPs, the INDELs in the new loci were still nominally significant. Our findings indicate that INDELs could be potentially functional genetic variants for lung cancer risk. Further functional experiments are needed to better understand INDEL mechanisms in carcinogenesis.

show abstract

GIPC1 Interacts with MyoGEF and Promotes MDA-MB-231 Breast Cancer Cell Invasion

Cited by 18 publications

References 58 publications

Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

G protein‐coupled receptors participate in cytokinesis

Genome‐wide association study of INDELs identified four novel susceptibility loci associated with lung cancer risk

Contact Info

Product

Resources

About