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A multi-stage genome-wide association study of uterine fibroids in African Americans.
Hellwege JN, Jeff JM, Wise LA, Gallagher CS, Wellons M, Hartmann KE, Jones SF, Torstenson ES, Dickinson S, Ruiz-Narváez EA, Rohland N, Allen A, Reich D, Tandon A, Pasaniuc B, Mancuso N, Im HK, Hinds DA, Palmer JR, Rosenberg L, Denny JC, Roden DM, Stewart EA, Morton CC, Kenny EE, Edwards TL, Velez Edwards DR
(2017) Hum Genet 136: 1363-1373
MeSH Terms: Adult, African Americans, Alleles, Cell Adhesion Molecules, Female, Gene Expression Regulation, Neoplastic, Gene Frequency, Genetic Loci, Genome-Wide Association Study, Guanine Nucleotide Exchange Factors, Humans, Leiomyoma, Middle Aged, Neoplasm Proteins, Risk Factors, Uterine Neoplasms
Show Abstract · Added March 14, 2018
Uterine fibroids are benign tumors of the uterus affecting up to 77% of women by menopause. They are the leading indication for hysterectomy, and account for $34 billion annually in the United States. Race/ethnicity and age are the strongest known risk factors. African American (AA) women have higher prevalence, earlier onset, and larger and more numerous fibroids than European American women. We conducted a multi-stage genome-wide association study (GWAS) of fibroid risk among AA women followed by in silico genetically predicted gene expression profiling of top hits. In Stage 1, cases and controls were confirmed by pelvic imaging, genotyped and imputed to 1000 Genomes. Stage 2 used self-reported fibroid and GWAS data from 23andMe, Inc. and the Black Women's Health Study. Associations with fibroid risk were modeled using logistic regression adjusted for principal components, followed by meta-analysis of results. We observed a significant association among 3399 AA cases and 4764 AA controls at rs739187 (risk-allele frequency = 0.27) in CYTH4 (OR (95% confidence interval) = 1.23 (1.16-1.30), p value = 7.82 × 10). Evaluation of the genetic association results with MetaXcan identified lower predicted gene expression of CYTH4 in thyroid tissue as significantly associated with fibroid risk (p value = 5.86 × 10). In this first multi-stage GWAS for fibroids among AA women, we identified a novel risk locus for fibroids within CYTH4 that impacts gene expression in thyroid and has potential biological relevance for fibroids.
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4 Members
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16 MeSH Terms
The guanine nucleotide exchange factor (GEF) Asef2 promotes dendritic spine formation via Rac activation and spinophilin-dependent targeting.
Evans JC, Robinson CM, Shi M, Webb DJ
(2015) J Biol Chem 290: 10295-308
MeSH Terms: Actin Cytoskeleton, Amino Acid Sequence, Animals, Dendritic Spines, Embryo, Mammalian, Gene Expression Regulation, Developmental, Guanine Nucleotide Exchange Factors, Hippocampus, Microfilament Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurogenesis, Primary Cell Culture, Proto-Oncogene Proteins c-akt, RNA, Small Interfering, Rats, Receptors, N-Methyl-D-Aspartate, Signal Transduction, Synapses
Show Abstract · Added February 5, 2016
Dendritic spines are actin-rich protrusions that establish excitatory synaptic contacts with surrounding neurons. Reorganization of the actin cytoskeleton is critical for the development and plasticity of dendritic spines, which is the basis for learning and memory. Rho family GTPases are emerging as important modulators of spines and synapses, predominantly through their ability to regulate actin dynamics. Much less is known, however, about the function of guanine nucleotide exchange factors (GEFs), which activate these GTPases, in spine and synapse development. In this study we show that the Rho family GEF Asef2 is found at synaptic sites, where it promotes dendritic spine and synapse formation. Knockdown of endogenous Asef2 with shRNAs impairs spine and synapse formation, whereas exogenous expression of Asef2 causes an increase in spine and synapse density. This effect of Asef2 on spines and synapses is abrogated by expression of GEF activity-deficient Asef2 mutants or by knockdown of Rac, suggesting that Asef2-Rac signaling mediates spine development. Because Asef2 interacts with the F-actin-binding protein spinophilin, which localizes to spines, we investigated the role of spinophilin in Asef2-promoted spine formation. Spinophilin recruits Asef2 to spines, and knockdown of spinophilin hinders spine and synapse formation in Asef2-expressing neurons. Furthermore, inhibition of N-methyl-d-aspartate receptor (NMDA) activity blocks spinophilin-mediated localization of Asef2 to spines. These results collectively point to spinophilin-Asef2-Rac signaling as a novel mechanism for the development of dendritic spines and synapses.
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
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1 Members
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19 MeSH Terms
The Rho family GEF Asef2 regulates cell migration in three dimensional (3D) collagen matrices through myosin II.
Jean L, Yang L, Majumdar D, Gao Y, Shi M, Brewer BM, Li D, Webb DJ
(2014) Cell Adh Migr 8: 460-7
MeSH Terms: Cell Line, Cell Movement, Collagen, Guanine Nucleotide Exchange Factors, Heterocyclic Compounds, 4 or More Rings, Humans, Immunohistochemistry, Myosin Type II
Show Abstract · Added January 20, 2015
Cell migration is fundamental to a variety of physiological processes, including tissue development, homeostasis, and regeneration. Migration has been extensively studied with cells on 2-dimensional (2D) substrates, but much less is known about cell migration in 3D environments. Tissues and organs are 3D, which is the native environment of cells in vivo, pointing to a need to understand migration and the mechanisms that regulate it in 3D environments. To investigate cell migration in 3D environments, we developed microfluidic devices that afford a controlled, reproducible platform for generating 3D matrices. Using these devices, we show that the Rho family guanine nucleotide exchange factor (GEF) Asef2 inhibits cell migration in 3D type I collagen (collagen I) matrices. Treatment of cells with the myosin II (MyoII) inhibitor blebbistatin abolished the decrease in migration by Asef2. Moreover, Asef2 enhanced MyoII activity as shown by increased phosphorylation of serine 19 (S19). Furthermore, Asef2 increased activation of Rac, which is a Rho family small GTPase, in 3D collagen I matrices. Inhibition of Rac activity by treatment with the Rac-specific inhibitor NSC23766 abrogated the Asef2-promoted increase in S19 MyoII phosphorylation. Thus, our results indicate that Asef2 regulates cell migration in 3D collagen I matrices through a Rac-MyoII-dependent mechanism.
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8 MeSH Terms
The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast.
Ren L, Willet AH, Roberts-Galbraith RH, McDonald NA, Feoktistova A, Chen JS, Huang H, Guillen R, Boone C, Sidhu SS, Beckley JR, Gould KL
(2015) Mol Biol Cell 26: 256-69
MeSH Terms: Amino Acid Sequence, Cell Cycle Proteins, Cell Division, Cytokinesis, Cytoskeletal Proteins, GTP-Binding Proteins, Gene Regulatory Networks, Guanine Nucleotide Exchange Factors, Immunoblotting, Luminescent Proteins, Microscopy, Confocal, Molecular Sequence Data, Mutation, Protein Binding, Proteome, Proteomics, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Homology, Amino Acid, Time-Lapse Imaging, src Homology Domains
Show Abstract · Added January 20, 2015
Schizosaccharomyces pombe cdc15 homology (PCH) family members participate in numerous biological processes, including cytokinesis, typically by bridging the plasma membrane via their F-BAR domains to the actin cytoskeleton. Two SH3 domain-containing PCH family members, Cdc15 and Imp2, play critical roles in S. pombe cytokinesis. Although both proteins localize to the contractile ring, with Cdc15 preceding Imp2, only cdc15 is an essential gene. Despite these distinct roles, the SH3 domains of Cdc15 and Imp2 cooperate in the essential process of recruiting other proteins to stabilize the contractile ring. To better understand the connectivity of this SH3 domain-based protein network at the CR and its function, we used a biochemical approach coupled to proteomics to identify additional proteins (Rgf3, Art1, Spa2, and Pos1) that are integrated into this network. Cell biological and genetic analyses of these SH3 partners implicate them in a range of activities that ensure the fidelity of cell division, including promoting cell wall metabolism and influencing cell morphogenesis.
© 2015 Ren et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).
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21 MeSH Terms
P-REX1 creates a positive feedback loop to activate growth factor receptor, PI3K/AKT and MEK/ERK signaling in breast cancer.
Dillon LM, Bean JR, Yang W, Shee K, Symonds LK, Balko JM, McDonald WH, Liu S, Gonzalez-Angulo AM, Mills GB, Arteaga CL, Miller TW
(2015) Oncogene 34: 3968-76
MeSH Terms: Animals, Breast Neoplasms, Cell Survival, Feedback, Physiological, Female, Guanine Nucleotide Exchange Factors, Humans, MAP Kinase Signaling System, MCF-7 Cells, Mice, Inbred NOD, Mice, SCID, Mutation, Neoplasm Transplantation, Phosphatidylinositol 3-Kinases, Proto-Oncogene Proteins c-akt, Receptors, Growth Factor, rac GTP-Binding Proteins
Show Abstract · Added October 21, 2014
Phosphatidylinositol 3-kinase (PI3K) promotes cancer cell survival, migration, growth and proliferation by generating phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the inner leaflet of the plasma membrane. PIP3 recruits pleckstrin homology domain-containing proteins to the membrane to activate oncogenic signaling cascades. Anticancer therapeutics targeting the PI3K/AKT/mTOR (mammalian target of rapamycin) pathway are in clinical development. In a mass spectrometric screen to identify PIP3-regulated proteins in breast cancer cells, levels of the Rac activator PIP3-dependent Rac exchange factor-1 (P-REX1) increased in response to PI3K inhibition, and decreased upon loss of the PI3K antagonist phosphatase and tensin homolog (PTEN). P-REX1 mRNA and protein levels were positively correlated with ER expression, and inversely correlated with PI3K pathway activation in breast tumors as assessed by gene expression and phosphoproteomic analyses. P-REX1 increased activation of Rac1, PI3K/AKT and MEK/ERK signaling in a PTEN-independent manner, and promoted cell and tumor viability. Loss of P-REX1 or inhibition of Rac suppressed PI3K/AKT and MEK/ERK, and decreased viability. P-REX1 also promoted insulin-like growth factor-1 receptor activation, suggesting that P-REX1 provides positive feedback to activators upstream of PI3K. In support of a model where PIP3-driven P-REX1 promotes both PI3K/AKT and MEK/ERK signaling, high levels of P-REX1 mRNA (but not phospho-AKT or a transcriptomic signature of PI3K activation) were predictive of sensitivity to PI3K inhibitors among breast cancer cell lines. P-REX1 expression was highest in estrogen receptor-positive breast tumors compared with many other cancer subtypes, suggesting that neutralizing the P-REX1/Rac axis may provide a novel therapeutic approach to selectively abrogate oncogenic signaling in breast cancer cells.
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2 Members
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17 MeSH Terms
Spatial control of Cdc42 signalling by a GM130-RasGRF complex regulates polarity and tumorigenesis.
Baschieri F, Confalonieri S, Bertalot G, Di Fiore PP, Dietmaier W, Leist M, Crespo P, Macara IG, Farhan H
(2014) Nat Commun 5: 4839
MeSH Terms: Antigens, CD, Autoantigens, Cadherins, Carcinogenesis, Cell Line, Tumor, Cell Polarity, Gene Expression Regulation, Neoplastic, Gene Silencing, Humans, MAP Kinase Signaling System, MCF-7 Cells, Membrane Proteins, Mitogen-Activated Protein Kinase 3, Rho Guanine Nucleotide Exchange Factors, Signal Transduction, cdc42 GTP-Binding Protein, ras Guanine Nucleotide Exchange Factors, ras-GRF1
Show Abstract · Added April 10, 2018
The small GTPase Cdc42 is a key regulator of polarity, but little is known in mammals about its spatial regulation and the relevance of spatial Cdc42 pools for polarity. Here we report the identification of a GM130-RasGRF complex as a regulator of Cdc42 at the Golgi. Silencing GM130 results in RasGRF-dependent inhibition of the Golgi pool of Cdc42, but does not affect Cdc42 at the cell surface. Furthermore, active Cdc42 at the Golgi is important to sustain asymmetric front-rear Cdc42-GTP distribution in directionally migrating cells. Concurrent to Cdc42 inhibition, silencing GM130 also results in RasGRF-dependent Ras-ERK pathway activation. Moreover, depletion of GM130 is sufficient to induce E-cadherin downregulation, indicative of a loss in cell polarity and epithelial identity. Accordingly, GM130 expression is frequently lost in colorectal and breast cancer patients. These findings establish a previously unrecognized role for a GM130-RasGRF-Cdc42 connection in regulating polarity and tumorigenesis.
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1 Members
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18 MeSH Terms
Genome-wide association meta-analysis identifies novel variants associated with fasting plasma glucose in East Asians.
Hwang JY, Sim X, Wu Y, Liang J, Tabara Y, Hu C, Hara K, Tam CH, Cai Q, Zhao Q, Jee S, Takeuchi F, Go MJ, Ong RT, Ohkubo T, Kim YJ, Zhang R, Yamauchi T, So WY, Long J, Gu D, Lee NR, Kim S, Katsuya T, Oh JH, Liu J, Umemura S, Kim YJ, Jiang F, Maeda S, Chan JC, Lu W, Hixson JE, Adair LS, Jung KJ, Nabika T, Bae JB, Lee MH, Seielstad M, Young TL, Teo YY, Kita Y, Takashima N, Osawa H, Lee SH, Shin MH, Shin DH, Choi BY, Shi J, Gao YT, Xiang YB, Zheng W, Kato N, Yoon M, He J, Shu XO, Ma RC, Kadowaki T, Jia W, Miki T, Qi L, Tai ES, Mohlke KL, Han BG, Cho YS, Kim BJ
(2015) Diabetes 64: 291-8
MeSH Terms: Adult, Aged, Asian Continental Ancestry Group, Blood Glucose, Far East, Fasting, Female, Genetic Variation, Genome-Wide Association Study, Genotype, Guanine Nucleotide Exchange Factors, Humans, Male, Middle Aged, Phenotype, Protein-Serine-Threonine Kinases, Pyruvate Dehydrogenase (Acetyl-Transferring) Kinase, Receptor, IGF Type 1, Tumor Suppressor Proteins
Show Abstract · Added February 22, 2016
Fasting plasma glucose (FPG) has been recognized as an important indicator for the overall glycemic state preceding the onset of metabolic diseases. So far, most indentified genome-wide association loci for FPG were derived from populations with European ancestry, with a few exceptions. To extend a thorough catalog for FPG loci, we conducted meta-analyses of 13 genome-wide association studies in up to 24,740 nondiabetic subjects with East Asian ancestry. Follow-up replication analyses in up to an additional 21,345 participants identified three new FPG loci reaching genome-wide significance in or near PDK1-RAPGEF4, KANK1, and IGF1R. Our results could provide additional insight into the genetic variation implicated in fasting glucose regulation.
© 2015 by the American Diabetes Association. Readers may use this article as long as the work is properly cited, the use is educational and not for profit, and the work is not altered.
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2 Members
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19 MeSH Terms
Phosphorylation of serine 106 in Asef2 regulates cell migration and adhesion turnover.
Evans JC, Hines KM, Forsythe JG, Erdogan B, Shi M, Hill S, Rose KL, McLean JA, Webb DJ
(2014) J Proteome Res 13: 3303-13
MeSH Terms: Amino Acid Sequence, Cell Adhesion, Cell Line, Tumor, Cell Movement, Guanine Nucleotide Exchange Factors, HEK293 Cells, Humans, Molecular Sequence Data, Phosphorylation, Protein Processing, Post-Translational, Serine
Show Abstract · Added February 5, 2016
Asef2, a 652-amino acid protein, is a guanine nucleotide exchange factor (GEF) that regulates cell migration and other processes via activation of Rho family GTPases, including Rac. Binding of the tumor suppressor adenomatous polyposis coli (APC) to Asef2 is known to induce its GEF activity; however, little is currently known about other modes of Asef2 regulation. Here, we investigated the role of phosphorylation in regulating Asef2 activity and function. Using high-resolution mass spectrometry (MS) and tandem mass spectrometry (MS/MS), we obtained complete coverage of all phosphorylatable residues and identified six phosphorylation sites. One of these, serine 106 (S106), was particularly intriguing as a potential regulator of Asef2 activity because of its location within the APC-binding domain. Interestingly, mutation of this serine to alanine (S106A), a non-phosphorylatable analogue, greatly diminished the ability of Asef2 to activate Rac, while a phosphomimetic mutation (serine to aspartic acid, S106D) enhanced Rac activation. Furthermore, expression of these mutants in HT1080 cells demonstrated that phosphorylation of S106 is critical for Asef2-promoted migration and for cell-matrix adhesion assembly and disassembly (adhesion turnover), which is a process that facilitates efficient migration. Collectively, our results show that phosphorylation of S106 modulates Asef2 GEF activity and Asef2-mediated cell migration and adhesion turnover.
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2 Members
0 Resources
11 MeSH Terms
A genome-wide association study of anorexia nervosa.
Boraska V, Franklin CS, Floyd JA, Thornton LM, Huckins LM, Southam L, Rayner NW, Tachmazidou I, Klump KL, Treasure J, Lewis CM, Schmidt U, Tozzi F, Kiezebrink K, Hebebrand J, Gorwood P, Adan RA, Kas MJ, Favaro A, Santonastaso P, Fernández-Aranda F, Gratacos M, Rybakowski F, Dmitrzak-Weglarz M, Kaprio J, Keski-Rahkonen A, Raevuori A, Van Furth EF, Slof-Op 't Landt MC, Hudson JI, Reichborn-Kjennerud T, Knudsen GP, Monteleone P, Kaplan AS, Karwautz A, Hakonarson H, Berrettini WH, Guo Y, Li D, Schork NJ, Komaki G, Ando T, Inoko H, Esko T, Fischer K, Männik K, Metspalu A, Baker JH, Cone RD, Dackor J, DeSocio JE, Hilliard CE, O'Toole JK, Pantel J, Szatkiewicz JP, Taico C, Zerwas S, Trace SE, Davis OS, Helder S, Bühren K, Burghardt R, de Zwaan M, Egberts K, Ehrlich S, Herpertz-Dahlmann B, Herzog W, Imgart H, Scherag A, Scherag S, Zipfel S, Boni C, Ramoz N, Versini A, Brandys MK, Danner UN, de Kovel C, Hendriks J, Koeleman BP, Ophoff RA, Strengman E, van Elburg AA, Bruson A, Clementi M, Degortes D, Forzan M, Tenconi E, Docampo E, Escaramís G, Jiménez-Murcia S, Lissowska J, Rajewski A, Szeszenia-Dabrowska N, Slopien A, Hauser J, Karhunen L, Meulenbelt I, Slagboom PE, Tortorella A, Maj M, Dedoussis G, Dikeos D, Gonidakis F, Tziouvas K, Tsitsika A, Papezova H, Slachtova L, Martaskova D, Kennedy JL, Levitan RD, Yilmaz Z, Huemer J, Koubek D, Merl E, Wagner G, Lichtenstein P, Breen G, Cohen-Woods S, Farmer A, McGuffin P, Cichon S, Giegling I, Herms S, Rujescu D, Schreiber S, Wichmann HE, Dina C, Sladek R, Gambaro G, Soranzo N, Julia A, Marsal S, Rabionet R, Gaborieau V, Dick DM, Palotie A, Ripatti S, Widén E, Andreassen OA, Espeseth T, Lundervold A, Reinvang I, Steen VM, Le Hellard S, Mattingsdal M, Ntalla I, Bencko V, Foretova L, Janout V, Navratilova M, Gallinger S, Pinto D, Scherer SW, Aschauer H, Carlberg L, Schosser A, Alfredsson L, Ding B, Klareskog L, Padyukov L, Courtet P, Guillaume S, Jaussent I, Finan C, Kalsi G, Roberts M, Logan DW, Peltonen L, Ritchie GR, Barrett JC, Wellcome Trust Case Control Consortium 3, Estivill X, Hinney A, Sullivan PF, Collier DA, Zeggini E, Bulik CM
(2014) Mol Psychiatry 19: 1085-94
MeSH Terms: Anorexia Nervosa, Asian Continental Ancestry Group, Calcineurin, Carrier Proteins, Case-Control Studies, Cullin Proteins, European Continental Ancestry Group, Female, Genome-Wide Association Study, Guanine Nucleotide Exchange Factors, Humans, Japan, Male, Meta-Analysis as Topic, Nuclear Proteins, Polymorphism, Single Nucleotide
Show Abstract · Added May 27, 2014
Anorexia nervosa (AN) is a complex and heritable eating disorder characterized by dangerously low body weight. Neither candidate gene studies nor an initial genome-wide association study (GWAS) have yielded significant and replicated results. We performed a GWAS in 2907 cases with AN from 14 countries (15 sites) and 14 860 ancestrally matched controls as part of the Genetic Consortium for AN (GCAN) and the Wellcome Trust Case Control Consortium 3 (WTCCC3). Individual association analyses were conducted in each stratum and meta-analyzed across all 15 discovery data sets. Seventy-six (72 independent) single nucleotide polymorphisms were taken forward for in silico (two data sets) or de novo (13 data sets) replication genotyping in 2677 independent AN cases and 8629 European ancestry controls along with 458 AN cases and 421 controls from Japan. The final global meta-analysis across discovery and replication data sets comprised 5551 AN cases and 21 080 controls. AN subtype analyses (1606 AN restricting; 1445 AN binge-purge) were performed. No findings reached genome-wide significance. Two intronic variants were suggestively associated: rs9839776 (P=3.01 × 10(-7)) in SOX2OT and rs17030795 (P=5.84 × 10(-6)) in PPP3CA. Two additional signals were specific to Europeans: rs1523921 (P=5.76 × 10(-)(6)) between CUL3 and FAM124B and rs1886797 (P=8.05 × 10(-)(6)) near SPATA13. Comparing discovery with replication results, 76% of the effects were in the same direction, an observation highly unlikely to be due to chance (P=4 × 10(-6)), strongly suggesting that true findings exist but our sample, the largest yet reported, was underpowered for their detection. The accrual of large genotyped AN case-control samples should be an immediate priority for the field.
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1 Members
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16 MeSH Terms
Activation of Rac by Asef2 promotes myosin II-dependent contractility to inhibit cell migration on type I collagen.
Jean L, Majumdar D, Shi M, Hinkle LE, Diggins NL, Ao M, Broussard JA, Evans JC, Choma DP, Webb DJ
(2013) J Cell Sci 126: 5585-97
MeSH Terms: Cell Adhesion, Cell Line, Tumor, Cell Movement, Collagen Type I, Guanine Nucleotide Exchange Factors, Humans, Integrin beta1, Myosin Type II, cdc42 GTP-Binding Protein, rac GTP-Binding Proteins
Show Abstract · Added May 20, 2014
Non-muscle myosin II (MyoII) contractility is central to the regulation of numerous cellular processes, including migration. Rho is a well-characterized modulator of actomyosin contractility, but the function of other GTPases, such as Rac, in regulating contractility is currently not well understood. Here, we show that activation of Rac by the guanine nucleotide exchange factor Asef2 (also known as SPATA13) impairs migration on type I collagen through a MyoII-dependent mechanism that enhances contractility. Knockdown of endogenous Rac or treatment of cells with a Rac-specific inhibitor decreases the amount of active MyoII, as determined by serine 19 (S19) phosphorylation, and negates the Asef2-promoted increase in contractility. Moreover, treatment of cells with blebbistatin, which inhibits MyoII activity, abolishes the Asef2-mediated effect on migration. In addition, Asef2 slows the turnover of adhesions in protrusive regions of cells by promoting large mature adhesions, which has been linked to actomyosin contractility, with increased amounts of active β1 integrin. Hence, our data reveal a new role for Rac activation, promoted by Asef2, in modulating actomyosin contractility, which is important for regulating cell migration and adhesion dynamics.
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1 Members
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10 MeSH Terms