Transducer of Cdc42-dependent Actin Assembly Promotes Epidermal Growth Factor-induced Cell Motility and Invasiveness

Hu, Jinghui; Mukhopadhyay, Alka; Craig, Andrew W.B.

doi:10.1074/jbc.m110.157974

Cited by 40 publications

(41 citation statements)

References 61 publications

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“…Interestingly, membrane ruffling was also inhibited (supplementary material Fig. S2A,B), indicating that FBP17 and CIP4 are also implicated in this process as reported for Toca-1 (Hu et al, 2011a). Notably, the aberrant podosomes and robust membrane ruffling induced by PSTPIP2 knockdown were significantly suppressed by the depletion of Toca proteins ( Fig.…”

Section: Pstpip2 Knockdown Induces Aberrant Podosome Formation With Dmentioning

confidence: 61%

“…Podosomal actin structures are formed by the WASP/N-WASP-activated Arp2/3 complex at the plasma membrane (Albiges-Rizo et al, 2009;Murphy and Courtneidge, 2011). Recently, Toca proteins have been identified as key players in podosome/invadopodia formation (Chander et al, 2012;Hu et al, 2011a;Hu et al, 2011b;Linder et al, 2000;Pichot et al, 2010;Tsuboi et al, 2009), through their self-assembling property for the activation of WASP-mediated actin polymerization. However, it is unclear how the level of Toca protein assembly is determined for proper formation and dynamic turnover of podosomes.…”

Section: Introductionmentioning

confidence: 99%

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Antagonistic regulation of F-BAR protein assemblies controls actin polymerization during podosome formation

Tsujita

Kondo

Kurisu

et al. 2013

Journal of Cell Science

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Summary FBP17, an F-BAR domain protein, has emerged as a crucial factor linking the plasma membrane to WASP-mediated actin polymerization. Although it is well established that FBP17 has a powerful self-polymerizing ability that promotes actin nucleation on membranes in vitro, knowledge of inhibitory factors that counteract this activity in vivo is limited. Here, we demonstrate that the assembly of FBP17 on the plasma membranes is antagonized by PSTPIP2, another F-BAR protein implicated in auto-inflammatory disorder. Knockdown of PSTPIP2 in macrophage promotes the assembly of FBP17 as well as subsequent actin nucleation at podosomes, resulting in an enhancement of matrix degradation. This phenotype is rescued by expression of PSTPIP2 in a manner dependent on its F-BAR domain. Time-lapse total internal reflection fluorescence (TIRF) microscopy observations reveal that the self-assembly of FBP17 at the podosomal membrane initiates actin polymerization, whereas the clustering of PSTPIP2 has an opposite effect. Biochemical analysis and live-cell imaging show that PSTPIP2 inhibits actin polymerization by competing with FBP17 for assembly at artificial as well as the plasma membrane. Interestingly, the assembly of FBP17 is dependent on WASP, and its dissociation by WASP inhibition strongly induces a self-organization of PSTPIP2 at podosomes. Thus, our data uncover a previously unappreciated antagonism between different F-BAR domain assemblies that determines the threshold of actin polymerization for the formation of functional podosomes and may explain how the absence of PSTPIP2 causes auto-inflammatory disorder.

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Section: Pstpip2 Knockdown Induces Aberrant Podosome Formation With Dmentioning

confidence: 61%

Section: Introductionmentioning

confidence: 99%

Antagonistic regulation of F-BAR protein assemblies controls actin polymerization during podosome formation

Tsujita

Kondo

Kurisu

et al. 2013

Journal of Cell Science

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“…In the case of the F-BAR adaptor Pacsin-2, it was shown to localize to the base of microspikes via its F-BAR domain (Shimada et al, 2010). Similar localization of Toca-1 to the base of filopodia has also been reported recently (Bu et al, 2009;Hu et al, 2010). Future studies will be required to fully understand the potential roles of F-BAR proteins in invadopodia formation or dynamics.…”

Section: Discussionmentioning

confidence: 98%

Cdc42-interacting protein 4 is a Src substrate that regulates invadopodia and invasiveness of breast tumors by promoting MT1-MMP endocytosis

Mukhopadhyay

Truesdell

et al. 2011

Journal of Cell Science

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SummaryInvadopodia are actin-rich membrane protrusions that promote extracellular matrix degradation and invasiveness of tumor cells. Src protein-tyrosine kinase is a potent inducer of invadopodia and tumor metastases. Cdc42-interacting protein 4 (CIP4) adaptor protein interacts with actin regulatory proteins and regulates endocytosis. Here, we show that CIP4 is a Src substrate that localizes to invadopodia in MDA-MB-231 breast tumor cells expressing activated Src (MDA-SrcYF). To probe the function of CIP4 in invadopodia, we established stable CIP4 knockdown in MDA-SrcYF cell lines by RNA interference. Compared with control cells, CIP4 knockdown cells degrade more extracellular matrix (ECM), have increased numbers of mature invadopodia and are more invasive through matrigel. Similar results are observed with knockdown of CIP4 in EGF-treated MDA-MB-231 cells. This inhibitory role of CIP4 is explained by our finding that CIP4 limits surface expression of transmembrane type I matrix metalloprotease (MT1-MMP), by promoting MT1-MMP internalization. Ectopic expression of CIP4 reduces ECM digestion by MDA-SrcYF cells, and this activity is enhanced by mutation of the major Src phosphorylation site in CIP4 (Y471). Overall, our results identify CIP4 as a suppressor of Srcinduced invadopodia and invasion in breast tumor cells by promoting endocytosis of MT1-MMP.

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“…4, fourth row, left) are also enriched in samples from BL-ZO-1-compared with ZO-1-BLexpressing cells. TOCA-1 binds to and remodels lipid bilayers and localizes to cell junctions in Caenorhabditis elegans (38) and to some extent in A431 cells (39).…”

Section: Specific Proteins Are Differentially Tagged In Cells Expressmentioning

confidence: 99%

The N and C Termini of ZO-1 Are Surrounded by Distinct Proteins and Functional Protein Networks

Itallie

Aponte

Tietgens

et al. 2013

Journal of Biological Chemistry

109

118

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Background: Biotin ligase tagging with ZO-1 was applied to identify a more complete tight junction proteome. Results: Identical but also different proteins and functional networks were identified near the N and C ends of ZO-1. Conclusion:The ends of ZO-1 are embedded in different functional subcompartments of the tight junction. Significance: Biotin tagging with ZO-1 expands the tight junction proteome and defines subcompartments of the junction.

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Transducer of Cdc42-dependent Actin Assembly Promotes Epidermal Growth Factor-induced Cell Motility and Invasiveness

Cited by 40 publications

References 61 publications

Antagonistic regulation of F-BAR protein assemblies controls actin polymerization during podosome formation

Antagonistic regulation of F-BAR protein assemblies controls actin polymerization during podosome formation

Cdc42-interacting protein 4 is a Src substrate that regulates invadopodia and invasiveness of breast tumors by promoting MT1-MMP endocytosis

The N and C Termini of ZO-1 Are Surrounded by Distinct Proteins and Functional Protein Networks

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