Bjerke MA , Dzamba BJ , Wang C , DeSimone DW .

R01 GM094793 NIGMS NIH HHS , R01 HD026402 NICHD NIH HHS , R21 HD071136 NICHD NIH HHS , GM094793 NIGMS NIH HHS , R01-HD26402 NICHD NIH HHS , R21-HD071136 NICHD NIH HHS , T32-GM08136 NIGMS NIH HHS , T32 GM008136 NIGMS NIH HHS

	Fig. 1. FAK knockdown inhibits gastrulation movements and axial elongation. (A) Representative Western blot of FAK expression levels in stage 11 embryos injected at one or two cell stage with Control or FAK morpholino (MO), β-actin was used as a loading control. (B) Quantification of FAK protein levels in stage 11 embryos, normalized to β-actin and shown relative to control embryos (N=10). Data are mean±SEM. (C–F) Time matched views of representative Control and FAK MO injected embryos. (C) Vegetal view at mid gastrula (stage 11.5, arrowheads indicate blastopore lip, red arrowhead=dorsal). (D) Dorso-anterior view at late neurula (stage 22, red dashed line marks open neural tube). (E) Dorso-lateral view at early tailbud (stage 25). (F) Lateral view at late tailbud (stage 32). Stages given for control embryos, a=anterior, p=posterior. (G) Representative images and quantification of gastrulation phenotype (blastopore closure) in stage 12 Control and FAK MO injected embryos compared with embryos co-injected with FAK MO and cFAK (N=7, Control MO n=371, FAK MO n=513, FAK MO+cFAK RNA n=327). Embryos were counted as having defects if their development was more than 1 h behind that of control embryos, if there was failure to form or close the blastopore, or if the embryos died during gastrulation. The example given for “FAK MO+cFAK” was counted as rescued (a mild phenotype and not included in count of embryos with defects). (H) Representative images and quantification of tailbud phenotype (axial elongation and formation of anterior structures) in stage 33 Control and FAK MO injected embryos compared with embryos co-injected with FAK MO and cFAK (N=4, Control MO n=225, FAK MO n=183, FAK MO+cFAK RNA n=217). Embryos were counted as having defects if they failed to form eye anlagen, had a distinctly shortened anterior–posterior axis or failed to close the neural tube. The example given for “FAK MO+cFAK” was counted as rescued (a mild phenotype and not included in count of embryos with defects). Data in G and H are mean±SEM. 25 ng MO injected per embryo. (I) Representative images from animal cap extension assay. Animal caps dissected from Control and FAK MO injected embryos with (+) and without (–) activin treatment (N=4, n=40/condition). (J) Representative images from Keller sandwich assay. Keller sandwiches made from Control and FAK MO injected embryos (N=3, n=15/condition). 20–25 ng MO and/or 200 pg RNA transcript injected per embryo.
	Fig. 2. FAK morphant mesendoderm cells migrate slowly and lack persistence. (A) Sagittal views of representative Control or FAK MO injected embryos from the same clutch that were fixed and bisected at time matched stages from early gastrulation (stage 10) through late gastrulation (stage 12). Arrowheads indicate position of the mesendoderm mantle, red arrowheads mark the first displacement between the mesendoderm and the blastocoel roof (bcr), red brackets mark the thickness of the marginal tissue, Bc=Brachet׳s cleft, d=dorsal, v=ventral. (B, C) Quantification of average velocity (B, displacement/time) and persistence (C, displacement/path length) of single mesendoderm cells on glass (N=3, Control MO n= 32, FAK MO n=65), cells in mesendoderm explants on glass (N=3, Control MO n=19, FAK MO n=23), and cells in mesendoderm explants on gels (N=3, Control MO n=22, FAK MO n=20). (D, E) Quantification of rescue of average velocity (D, displacement/time) and persistence (E, displacement/path length) of cells in mesendoderm explants on glass by co-injection of FAK MO with cFAK RNA (N=3, Control MO n=30, FAK MO n=32, FAK MO+cFAK RNA n=30). Data are mean ±SEM. ⁎p<0.05, ⁎⁎p<0.01, ⁎⁎⁎p<0.001. 20–25 ng MO and/or 200 pg RNA transcript injected per embryo.
	Fig. 3. FAK is essential for normal polarity of migrating mesendoderm. (A and B) Representative collapsed 5 µm z-stack images of live cells in control (A) and FAK morphant (B) mesendoderm explants expressing GAP-43-GFP to label membranes. Green arrowheads highlight protrusions in the expected direction of tissue movement and yellow arrowheads mark protrusions in any other direction. (C) Quantification of protrusions per cell in control and FAK morphant mesendoderm explants. Data are mean±SEM. (D) Quantification of protrusion angles of mesendoderm cells in explants from control (N=4, n=100) and FAK morphant (N=4, n=210) embryos, relative to cell centroids (center of rose diagram). 180° is defined as the predicted direction of normal tissue movement and marked in dark green. Mis-directed protrusions at 90° or 270° are marked in yellow and those at 0° are marked in red. Y axis for the rose diagrams represents percent of protrusions in each directional bin. Protrusions were quantified in both leading (row 1) and following (rows 2–4) cells. Significance was evaluated using circular statistical tests for randomness of distribution (Rayleigh׳s test, p(random)) and similarity of distribution (Mardia–Watson–Wheeler, p(same)). (E–G) Additional quantification of the data set shown in (D), indicating the percent of control or FAK morphant cells in mesendoderm explants with protrusions in the area defined in the cartoon beneath each graph, color coded to match graphs in (C). Data are mean±SEM. (E) Percent of cells with protrusions only within 45° of the direction of tissue migration. (F) Percent of cells with only protrusions deviating 75° or more from the direction of travel. (G) Percent of cells with at least one protrusion in the direction of travel and also one or more greater than 75° away from the expected direction of tissue migration. Scale bars=25 µm. 20–25 ng MO injected per embryo.
	Fig. 4. Actin organization is altered in FAK morphant cells. (A–E) Representative confocal images of live cells in mesendoderm explants expressing GFP–moesin to label the actin filament network. (A) Single plane confocal images of actin at the leading edges of cells in the first row (left) and following rows (right) of control mesendoderm explants. Green arrowheads indicate actin rich protrusions. (B) Single plane confocal images of actin on the leading edges of cells in the first row (left) and following rows (right) of FAK morphant mesendoderm explants. Yellow arrowheads indicate actin microspikes. (C) Collapsed 7.5 µm z-stack image of actin in a cell on the leading edge cell of a control explant. Greed arrowheads indicate cortical actin. (D) Collapsed 7.5 µm z-stack image of actin in a cell on the leading edge of a FAK morphant explant. Green arrowhead indicates cortical actin; yellow arrowheads indicate actin stress fibers. (E, F) Collapsed 5.5 µm z-stack images of cell–cell junctions in following rows of control (E) and FAK morphant (F) explants. Dashed lines mark the boundary between cells. (G) First frame from time-lapse confocal imaging of live cells in control mesendoderm explants (See Movie 1). Collapsed 5 µm z-stack image. Cells also labeled with fluorescently tagged dextran (blue) to show cell shape. (H) First frame from time-lapse confocal imaging of live cells in FAK morphant mesendoderm explants (See Movie 2). Collapsed 5 µm z-stack image. Cells also labeled with fluorescently tagged dextran (red) to show cell shape. Scale bars=10 µm (A, B, E) or 25 µm (C, D, G, H). 20–25 ng MO injected per embryo.
	Fig. 5. FAK is required for organization of the keratin filament network. (A–F) Representative collapsed 10 µm z-stack images of live cells in mesendoderm explants expressing GFP-XCK1 (8) to label the keratin filament network. (A, B) Keratin filaments in leading edge cells in control explants. Green arrowheads indicate basket like arrangement of filaments in the rear of each cell, green arrows indicatecabling across the leading edge cells. (C, D) Keratin filaments in leading edge cells in FAK morphant explants. Yellow arrowheads indicate mis-localized filaments, yellow arrows indicate loss of cabling, yellow dashed line in (D) denotes cell outline. (E, F) Keratin filaments in leading edge cells in explants co-injected with FAK MO and cFAK RNA, which is not targeted by the morpholino. Green arrowheads indicate basket-like arrangement of filaments, green arrows indicate cabling across leading edge cells. Scale bars=50 µm. 20–25 ng MO injected per embryo.
	Fig. 6. Spreading and cell traction are reduced in FAK morphant mesendoderm cells. (A) Representative image of control (blue) and FAK morphant (red) mesendoderm cells plated on Fn coated coverglass. Cells labeled with fluorescently tagged dextran to show cell shape and mark control vs. FAK morphant cells. (B) Quantification of percent of mesendoderm cells spread on Fn coated coverglass (N=3, Control MO n=88, FAK MO n=97). Data are mean±SEM. (C) Quantification of average force per cell exerted by mesendoderm cells on Fn coated micropost arrays (N=4, Control MO n=74, FAK MO n=56). (D) Quantification of circularity of cells from (C). (E) Examples of cells from (D) illustrating the circularity values indicated in top right corner of each panel. Cells labeled with fluorescently tagged dextran to show cell shape, microposts are shown in green. (F) Quantification of average stress applied by leading edge cells of mesendoderm explants to Fn coated polyacrylamide gels (N=3, n=6 explants/condition). Data in (C, D, F) are shown in box–whisker plots, bold line indicates mean, box delimits 25th–75th percentile and whiskers mark minimum and maximum values, statistical outliers are marked as dots. Scale bars=200 µm (A) or 50 µm (E). 25 ng MO injected per embryo.
	Fig. 7. Association of plakoglobin with C-cadherin is disrupted in early FAK morphant gastrulae. (A) Representative Western blot of plakoglobin or β-catenin immunoprecipitates from whole embryo lysates of control or FAK morphant embryos, probed with an antibody directed against C-cadherin. (B) Quantification of C-cadherin association with plakoglobin in early (stage 10) and late (stage 12) gastrulae injected with Control or FAK MOs. (C) Quantification of C-cadherin association with β-catenin in early (stage 10) and late (stage 12) gastrulae injected with Control or FAK MOs. Embryos from the same clutch were used for both plakoglobin and β-catenin co-immunoprecipitation at early and late stages of gastrulation (N=3). Blots were re-probed with antibodies directed against plakoglobin or β-catenin respectively and scans of these blots were used to normalize scans of C-cadherin blots, all values are shown relative to early control gastrulae. Data are mean±SEM. ⁎⁎p=0.003. 25 ng MO injected per embryo.
	Supplementary Fig. S1. FAK morpholino knocks down FAK protein expression and FAK protein expression is rescued by injection of cFAK RNA. (A) Quantification of expression of endogenous and exogenous (Xenopus FAK (xFAK), 200 pg injected transcript) FAK protein in stage 11 embryos, β-actin was used as a loading control (N=3). Data are mean±SEM. (B) Quantification of FAK expression at gastrula stage in FAK morphant embryos, compared with the amount present in control embryos from the same clutch at 1-cell, 8-cell, gastrula and neurula stages. FAK expression was normalized to β-actin and shown relative to expression in control embryos at gastrula stage (N=3). Data are mean±SEM. (C) Representative Western blot analysis of FAK protein expression in stage 11 embryos co-injected with 25 ng FAK MO and the chicken (Gallus gallus) ortholog of FAK (cFAK, 200 pg injected transcript), which is not targeted by FAK MO. Quantification is for blot shown. Expression levels were normalized to β-actin and calculated relative to uninjected controls. 20–25 ng MO injected per embryo.
	Supplementary Fig. S2. FAK morphants have defects in formation of anterior structures, notochord, gut and somites. (A–D׳) Representative images of collapsed 10 µm z-stacks through transverse sections of fixed tailbud stage embryos injected with Control or FAK MO and fluorescent dextrans to show cell shape (blue), yolk auto-fluorescence also captured for contrast (green). (A) Anterior section of control tailbud, arrows denote eye anlagen (e), diencephalon (d) and foregut (f). (B) Anterior section of FAK morphant tailbud. Arrows denote lack of clear eye anlagen (e) and poor organization of the neuro- and gastro-epithelia (d, e). (C, C׳) Mid-body (C) and posterior (C׳) sections of control tailbuds, arrows denote neural tube (nt), somites (s), notochord (n), midgut (m) and hindgut (h). (D, D׳) Mid-body (D) and posterior (D׳) sections of FAK morphant tailbuds, arrows denote cell-filled neural tube (nt), poorly defined somites (s), shortened and un-vacuolated notochord(n), and disorganization of the yolk rich endoderm cells fated to give rise to the gut (m, h). (E, F) Representative collapsed 10 µm z-stacks images of sagittal sections of control (E) and FAK morphant (F) tailbud stage embryos, co-injected with fluorescent dextrans to label cells and show structure of the somites. Anterior is at the top of both images. Scale bars =100 µm. 20 ng MO injected per embryo.
	Supplementary Fig. S3. Fn expression and matrix assembly are not affected by loss of FAK expression. (A, B) Examples of single-plane structured-illumination images of fixed animal caps from stage 11 control (A) or FAK morphant (B) embryos, stained for Fn. (C) Western blot analysis of Fn expression in control and FAK morphant embryos at stage 11, blot was also probed with antibodies against FAK and β-actin to control for FAK knockdown and gel loading respectively. (D, E) Western blot analysis of levels of phosphorylation of FAK on tyrosine 397 (D) (N=4) or tyrosine 861 (E) (N=3) in control and FAK morphant embryos at stage 11, β-actin was used as a loading control. The same lysates were also blotted for FAK to control for FAK expression levels; β-actin was used as a loading control. Scale bars =100 µm. 20–25 ng MO injected per embryo.
	Supplementary Fig. S4. Phosphorylation of myosin light chain (MLC) is not altered in FAK morphant embryos. (A) Representative image of Western blot of whole embryo lysates from control and FAK morphant embryos at stage 11 probed with an antibody against pMLC, β-actin was used as a loading control. (B) Quantification of pMLC levels in control and FAK morphant embryos (N=3). Data are mean±SEM. 25 ng MO injected per embryo.
	Supplementary Fig. S5. Knockdown of FAK does not significantly alter force per area but there is a significant correlation between decreased cell force and increased circularity. (A) Quantification of average force per micropost exerted by control and FAK morphant mesendoderm cells on Fn coated micropost arrays. Data are shown in box–whisker plots, bold line indicates mean, box delimits 25th–75th percentile and whiskers mark minimum and maximum values (N=4, Control MO n=74, FAK MO n=56). (B, C) Scatter plots of total cell force (y-axis, see Fig. 6C) and circularity (x-axis, see Fig. 6D) of mesendoderm cells isolated from control (B) and FAK morphant (C) embryos and plated on Fn coated micropost arrays. Correlation was analyzed using Kendall׳s tau test, the test statistic (τ) and p value are given. 25 ng MO injected per embryo.

Beningo, Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase. 2006, Pubmed

Beningo, Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase. 2006, Pubmed
Borghi, E-cadherin is under constitutive actomyosin-generated tension that is increased at cell-cell contacts upon externally applied stretch. 2012, Pubmed
Braga, The challenges of abundance: epithelial junctions and small GTPase signalling. 2005, Pubmed
Brieher, Regulation of C-cadherin function during activin induced morphogenesis of Xenopus animal caps. 1994, Pubmed , Xenbase
Burridge, Rho and Rac take center stage. 2004, Pubmed
Butler, Traction fields, moments, and strain energy that cells exert on their surroundings. 2002, Pubmed
Calalb, Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. 1995, Pubmed
Chang, FAK potentiates Rac1 activation and localization to matrix adhesion sites: a role for betaPIX. 2007, Pubmed
Chen, Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells. 2002, Pubmed
Clarke, Cytokeratin intermediate filament organisation and dynamics in the vegetal cortex of living Xenopus laevis oocytes and eggs. 2003, Pubmed , Xenbase
Crawford, Activity and distribution of paxillin, focal adhesion kinase, and cadherin indicate cooperative roles during zebrafish morphogenesis. 2003, Pubmed
Davidson, Patterning and tissue movements in a novel explant preparation of the marginal zone of Xenopus laevis. 2004, Pubmed , Xenbase
Davidson, Mesendoderm extension and mantle closure in Xenopus laevis gastrulation: combined roles for integrin alpha(5)beta(1), fibronectin, and tissue geometry. 2002, Pubmed , Xenbase
Davidson, Integrin alpha5beta1 and fibronectin regulate polarized cell protrusions required for Xenopus convergence and extension. 2006, Pubmed , Xenbase
Dimitriadis, Determination of elastic moduli of thin layers of soft material using the atomic force microscope. 2002, Pubmed
Doherty, Focal adhesion kinase is essential for cardiac looping and multichamber heart formation. 2010, Pubmed , Xenbase
Dumbauld, Contractility modulates cell adhesion strengthening through focal adhesion kinase and assembly of vinculin-containing focal adhesions. 2010, Pubmed
Dzamba, Cadherin adhesion, tissue tension, and noncanonical Wnt signaling regulate fibronectin matrix organization. 2009, Pubmed , Xenbase
Eyckmans, A hitchhiker's guide to mechanobiology. 2011, Pubmed
Fabry, Focal adhesion kinase stabilizes the cytoskeleton. 2011, Pubmed
Fonar, Focal adhesion kinase protein regulates Wnt3a gene expression to control cell fate specification in the developing neural plate. 2011, Pubmed , Xenbase
Furuta, Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. 1995, Pubmed
Georges-Labouesse, Mesodermal development in mouse embryos mutant for fibronectin. 1996, Pubmed
Grashoff, Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. 2010, Pubmed
Gu, Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. 1999, Pubmed
Hall, Rho GTPases and the actin cytoskeleton. 1998, Pubmed
Hanks, Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. 1992, Pubmed
Henry, Roles for zebrafish focal adhesion kinase in notochord and somite morphogenesis. 2001, Pubmed
Hens, Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis. 1995, Pubmed , Xenbase
Ilić, FAK promotes organization of fibronectin matrix and fibrillar adhesions. 2004, Pubmed
Ilić, Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. 1995, Pubmed
Johnson, Forced unfolding of proteins within cells. 2007, Pubmed
Jülich, Integrinalpha5 and delta/notch signaling have complementary spatiotemporal requirements during zebrafish somitogenesis. 2005, Pubmed
Keller, Developmental biology. Physical biology returns to morphogenesis. 2012, Pubmed
Keller, Shaping the vertebrate body plan by polarized embryonic cell movements. 2002, Pubmed
Keller, Regional expression, pattern and timing of convergence and extension during gastrulation of Xenopus laevis. 1988, Pubmed , Xenbase
Keller, Mechanisms of convergence and extension by cell intercalation. 2000, Pubmed
Kragtorp, Regulation of somitogenesis by Ena/VASP proteins and FAK during Xenopus development. 2006, Pubmed , Xenbase
Kölsch, Actin-dependent dynamics of keratin filament precursors. 2009, Pubmed
Lee, Disruption of gastrulation movements in Xenopus by a dominant-negative mutant for C-cadherin. 1995, Pubmed , Xenbase
Legant, Measurement of mechanical tractions exerted by cells in three-dimensional matrices. 2010, Pubmed
Lim, PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility. 2008, Pubmed
Lim, Knock-in mutation reveals an essential role for focal adhesion kinase activity in blood vessel morphogenesis and cell motility-polarity but not cell proliferation. 2010, Pubmed
Liu, Mechanical tugging force regulates the size of cell-cell junctions. 2010, Pubmed
Machacek, Coordination of Rho GTPase activities during cell protrusion. 2009, Pubmed
Marsden, Regulation of cell polarity, radial intercalation and epiboly in Xenopus: novel roles for integrin and fibronectin. 2001, Pubmed , Xenbase
Marsden, Integrin-ECM interactions regulate cadherin-dependent cell adhesion and are required for convergent extension in Xenopus. 2003, Pubmed , Xenbase
Michael, Focal adhesion kinase modulates cell adhesion strengthening via integrin activation. 2009, Pubmed
Mitra, Focal adhesion kinase: in command and control of cell motility. 2005, Pubmed
Myers, Focal adhesion kinase modulates Cdc42 activity downstream of positive and negative axon guidance cues. 2012, Pubmed , Xenbase
Ninomiya, Antero-posterior tissue polarity links mesoderm convergent extension to axial patterning. 2004, Pubmed , Xenbase
Nobes, Rho GTPases control polarity, protrusion, and adhesion during cell movement. 1999, Pubmed
Owen, Regulation of lamellipodial persistence, adhesion turnover, and motility in macrophages by focal adhesion kinase. 2007, Pubmed
Parsons, Focal adhesion kinase: the first ten years. 2003, Pubmed
Petridou, Activation of endogenous FAK via expression of its amino terminal domain in Xenopus embryos. 2012, Pubmed , Xenbase
Petridou, A dominant-negative provides new insights into FAK regulation and function in early embryonic morphogenesis. 2013, Pubmed , Xenbase
Playford, Focal adhesion kinase regulates cell-cell contact formation in epithelial cells via modulation of Rho. 2008, Pubmed
Rajagopalan, Direct comparison of the spread area, contractility, and migration of balb/c 3T3 fibroblasts adhered to fibronectin- and RGD-modified substrata. 2004, Pubmed
Ramos, Integrin-dependent adhesive activity is spatially controlled by inductive signals at gastrulation. 1996, Pubmed , Xenbase
Ren, Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. 2000, Pubmed
Rozario, The physical state of fibronectin matrix differentially regulates morphogenetic movements in vivo. 2009, Pubmed , Xenbase
Sawada, Force sensing by mechanical extension of the Src family kinase substrate p130Cas. 2006, Pubmed
Schaller, pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions. 1992, Pubmed
Schindelin, Fiji: an open-source platform for biological-image analysis. 2012, Pubmed
Schlaepfer, Control of motile and invasive cell phenotypes by focal adhesion kinase. 2004, Pubmed
Schlaepfer, Signaling through focal adhesion kinase. 1999, Pubmed
Schneider, Catenins in Xenopus embryogenesis and their relation to the cadherin-mediated cell-cell adhesion system. 1993, Pubmed , Xenbase
Schober, Focal adhesion kinase modulates tension signaling to control actin and focal adhesion dynamics. 2007, Pubmed
Schwartz, Cell adhesion receptors in mechanotransduction. 2008, Pubmed
Serrels, Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. 2007, Pubmed
Shook, Mechanisms, mechanics and function of epithelial-mesenchymal transitions in early development. 2003, Pubmed , Xenbase
Sieg, Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration. 1999, Pubmed
Stylianou, Imaging morphogenesis, in Xenopus with Quantum Dot nanocrystals. 2009, Pubmed , Xenbase
Tilghman, Focal adhesion kinase is required for the spatial organization of the leading edge in migrating cells. 2005, Pubmed
Tomar, A FAK-p120RasGAP-p190RhoGAP complex regulates polarity in migrating cells. 2009, Pubmed
Tseng, Spatial organization of the extracellular matrix regulates cell-cell junction positioning. 2012, Pubmed
Wang, Focal adhesion kinase is involved in mechanosensing during fibroblast migration. 2001, Pubmed
Wang, Transforming growth factor beta regulates cell-cell adhesion through extracellular matrix remodeling and activation of focal adhesion kinase in human colon carcinoma Moser cells. 2004, Pubmed
Weber, Integrins and cadherins join forces to form adhesive networks. 2011, Pubmed
Weber, A mechanoresponsive cadherin-keratin complex directs polarized protrusive behavior and collective cell migration. 2012, Pubmed , Xenbase
Winklbauer, Cell adhesion in amphibian gastrulation. 2009, Pubmed
Wozniak, Mechanotransduction in development: a growing role for contractility. 2009, Pubmed
Wöll, Dissection of keratin dynamics: different contributions of the actin and microtubule systems. 2005, Pubmed
Yamada, Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. 2007, Pubmed
Yang, Assaying stem cell mechanobiology on microfabricated elastomeric substrates with geometrically modulated rigidity. 2011, Pubmed
Yang, Embryonic mesodermal defects in alpha 5 integrin-deficient mice. 1993, Pubmed
Yonemura, alpha-Catenin as a tension transducer that induces adherens junction development. 2010, Pubmed