Novel Mechanism for Negatively Regulating Rho-Kinase (ROCK) Signaling through Coronin1B Protein in Neuregulin 1 (NRG-1)-induced Tumor Cell Motility

Rana, Manish; Worthylake, Rebecca A.

doi:10.1074/jbc.m112.346114

Cited by 24 publications

(17 citation statements)

References 58 publications

(62 reference statements)

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“…Although ROCK-2 has been predicted to influence actin organization via cofilin (Shi et al. , 2013) or coronin1B (Rana and Worthylake, 2012) and tight junction assembly via cingulin (Terry et al. , 2011), we could not see any significant effect on actomyosin filament organization and tight junctions in cells depleted of ROCK2.…”

Section: Resultsmentioning

confidence: 99%

ROCK1 but not ROCK2 contributes to RhoA signaling and NMIIA-mediated contractility at the epithelial zonula adherens

Priya

Liang

Teo

et al. 2017

MBoC

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Section: Resultsmentioning

confidence: 99%

ROCK1 but not ROCK2 contributes to RhoA signaling and NMIIA-mediated contractility at the epithelial zonula adherens

Priya

Liang

Teo

et al. 2017

MBoC

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“…Direct regulation of MLC kinase by Coro1 proteins can be excluded, because the pharmacological inactivation of the kinase does not rescue normal Rac1-dependent cytoskeletal responses in CORO1 knockdown cells (Ojeda and Bustelo, unpublished). Due to this, Coro1 proteins may be involved in the negative control of Rock (37) or MLC phosphatase or MII enzyme activities. Alternatively, they could regulate more downstream regulatory steps, such as the destabilization of MII-based structures.…”

Section: Discussionmentioning

confidence: 99%

Coronin1 Proteins Dictate Rac1 Intracellular Dynamics and Cytoskeletal Output

Ojeda

Castro-Castro

Bustelo

2014

Molecular and Cellular Biology

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Rac1 regulates lamellipodium formation, myosin II-dependent contractility, and focal adhesions during cell migration. While the spatiotemporal assembly of those processes is well characterized, the signaling mechanisms involved remain obscure. We report here that the cytoskeleton-related Coronin1A and -1B proteins control a myosin II inactivation-dependent step that dictates the intracellular dynamics and cytoskeletal output of active Rac1. This step is signaling-branch specific, since it affects the functional competence of active Rac1 only when forming complexes with downstream ArhGEF7 and Pak proteins in actomyosin-rich structures. The pathway is used by default unless Rac1 is actively rerouted away from the structures by upstream activators and signals from other Rho GTPases. These results indicate that Coronin1 proteins are at the center of a regulatory hub that coordinates Rac1 activation, effector exchange, and the F-actin organization state during cell signaling. Targeting this route could be useful to hamper migration of cancer cells harboring oncogenic RAC1 mutations.

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“…Indeed, it has been noted that CORO1B is a negative regulator of ROCK signaling (Rana et al, 2012). Their results established that the breast tumor-promoting factor NRG-1 controlled the interaction between ROCK2 and CORO1B.…”

Section: Npm1mentioning

confidence: 95%

Profilin-1 Overexpression in MDA-MB-231 Breast Cancer Cells Is Associated with Alterations in Proteomics Biomarkers of Cell Proliferation, Survival, and Motility as Revealed by Global Proteomics Analyses

Coumans

Gau

Poljak

et al. 2014

OMICS: A Journal of Integrative Biology

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Despite early screening programs and new therapeutic strategies, metastatic breast cancer is still the leading cause of cancer death in women in industrialized countries and regions. There is a need for novel biomarkers of susceptibility, progression, and therapeutic response. Global analyses or systems science approaches with omics technologies offer concrete ways forward in biomarker discovery for breast cancer. Previous studies have shown that expression of profilin-1 (PFN1), a ubiquitously expressed actin-binding protein, is downregulated in invasive and metastatic breast cancer. It has also been reported that PFN1 overexpression can suppress tumorigenic ability and motility/invasiveness of breast cancer cells. To obtain insights into the underlying molecular mechanisms of how elevating PFN1 level induces these phenotypic changes in breast cancer cells, we investigated the alteration in global protein expression profiles of breast cancer cells upon stable overexpression of PFN1 by a combination of three different proteome analysis methods (2-DE, iTRAQ, label-free). Using MDA-MB-231 as a model breast cancer cell line, we provide evidence that PFN1 overexpression is associated with alterations in the expression of proteins that have been functionally linked to cell proliferation (FKPB1A, HDGF, MIF, PRDX1, TXNRD1, LGALS1, STMN1, LASP1, S100A11, S100A6), survival (HSPE1, HSPB1, HSPD1, HSPA5 and PPIA, YWHAZ, CFL1, NME1) and motility (CFL1, CORO1B, PFN2, PLS3, FLNA, FLNB, NME2, ARHGDIB). In view of the pleotropic effects of PFN1 overexpression in breast cancer cells as suggested by these new findings, we propose that PFN1-induced phenotypic changes in cancer cells involve multiple mechanisms. Our data reported here might also offer innovative strategies for identification and validation of novel therapeutic targets and companion diagnostics for persons with, or susceptibility to, breast cancer.

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Novel Mechanism for Negatively Regulating Rho-Kinase (ROCK) Signaling through Coronin1B Protein in Neuregulin 1 (NRG-1)-induced Tumor Cell Motility

Cited by 24 publications

References 58 publications

ROCK1 but not ROCK2 contributes to RhoA signaling and NMIIA-mediated contractility at the epithelial zonula adherens

ROCK1 but not ROCK2 contributes to RhoA signaling and NMIIA-mediated contractility at the epithelial zonula adherens

Coronin1 Proteins Dictate Rac1 Intracellular Dynamics and Cytoskeletal Output

Profilin-1 Overexpression in MDA-MB-231 Breast Cancer Cells Is Associated with Alterations in Proteomics Biomarkers of Cell Proliferation, Survival, and Motility as Revealed by Global Proteomics Analyses

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