scholarly journals Src SH2 Arginine 175 Is Required for Cell Motility: Specific Focal Adhesion Kinase Targeting and Focal Adhesion Assembly Function

2006 ◽  
Vol 26 (12) ◽  
pp. 4399-4409 ◽  
Author(s):  
Myeong Gu Yeo ◽  
Michael A. Partridge ◽  
Ellen J. Ezratty ◽  
Qiong Shen ◽  
Gregg G. Gundersen ◽  
...  
Keyword(s):  
Cell Motility ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Src Kinase ◽  
Focal Adhesions ◽  
Sh2 Domain ◽  
Wild Type ◽  
Binding Function ◽  
Generation Capacity ◽  
Substrate Phosphorylation

ABSTRACT Src kinase is a crucial mediator of adhesion-related signaling and motility. Src binds to focal adhesion kinase (FAK) through its SH2 domain and subsequently activates it for phosphorylation of downstream substrates. In addition to this binding function, data suggested that the SH2 domain might also perform an important role in targeting Src to focal adhesions (FAs) to enable further substrate phosphorylations. To examine this, we engineered an R175L mutation in cSrc to prevent the interaction with FAK pY397. This constitutively open Src kinase mediated up-regulated substrate phosphorylation in SYF cells but was unable to promote malignant transformation. Significantly, SrcR175L cells also had a profound motility defect and an impaired FA generation capacity. Importantly, we were able to recapitulate wild-type motile behavior and FA formation by directing the kinase to FAs, clearly implicating the SH2 domain in recruitment to FAK and indicating that this targeting capacity, and not simply Src-FAK scaffolding, was critical for normal Src function.

scholarly journals Η έκφραση της Focal Adhesion Kinase, Src kinase και Paxillin σε κυτταρολογικό υλικό ασθενών με νευρoβλάστωμα

2015 ◽  
Author(s):  
Παναγιώτης Κρατημένος
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Src Kinase ◽  
Focal Adhesions ◽  
Needle Aspiration ◽  
Aspiration Cytology ◽  
Fine Needle ◽  
Kaplan Meier ◽  
Sds Page ◽  
Needle Aspiration Cytology

Γενικά: Το νευροβλαστωμα αποτελεί εμβρυϊκής προέλευσης όγκο προερχόμενο από κύτταρα νευρικής ακρολοφίας (συμπαθητικά γάγγλια, μυελώδης μοίρα των επινεφριδίων). Είναι ο πιο συχνός εξωκρανιακός όγκος στα παιδιά και αποτελεί το 7-10% των παιδικών κακοηθειών. Γνωρίζουμε πως, σε ασθενείς σταδίου IV, η πενταετής επιβίωση είναι συνήθως μικρότερη του 40%. Έως τώρα γνωρίζουμε πως η έκφραση του γονιδίου N-Myc αποτελεί σημαντικό αρνητικό προγνωστικό παράγοντα σε ασθενείς με νευροβλάστωμα. Γνωρίζουμε επίσης από προηγούμενες μελέτες πως ορισμένα κακοήθη νεοπλάσματα ενηλίκων εμφανίζουν αυξημένη έκφραση των πρωτεϊνών Focal Adhesion Kinase, Src και Paxillin και πως η έκφρασή τους συσχετίζεται με τη σταδιοποίηση των όγκων και την επιβίωση των ασθενών. Οι πρωτεϊνες FAK-Src-Paxillin βρίσκονται στην υπομεμβρανική περιοχή των Focal Adhesions (FΑs). H δομή των FAs αλλάζει συνεχώς καθώς το σήμα μεταδίδεται από τον πυρήνα στην πλασματική μεμβράνη μέσω του κυτταροπλάσματοςΈτσι ξεκινάει η κυτταρική κινητικότητα και η μετάστασηΣκοπός: Θελήσαμε να να διερευνήσουμε αν το σύμπλοκο FAK-Src-Paxillin, εκτός από τα κακοήθη νεοπλάσματα ενηλίκων, εκφράζεται και στο νευροβλάστωμα. Ο σκοπός της παρούσας μελέτης είναι ο προσδιορισμός της έκφρασης της FAK-Src-Paxillin α.Σε κυτταρικές σειρές ανθρωπίνου νευροβλαστώματος και β.σε κλινικό υλικό παιδιών με νευροβλάστωμα διερευνώντας πιθανή συσχέτιση της έκφρασής τoυς με την κλινική έκβαση των παιδιών.Υπόθεση: Η έκφραση του συμπλόκου FAK-Src-PΑΧ είναι αυξημένη σε κυτταρικές σειρές και κλινικό υλικό ασθενών με νευροβλάστωμα και συσχετίζεται με την πρόγνωσή τους.Υλικό και Μέθοδοι: Αρχικά, για τη μελέτη των κυτταρικών σειρών, τα κύτταρα των σειρών Κ562, ΝΙΗ/3T3, CCF-STTG1, SKNSH, IMR-32 και U-87-MG καλλιεργήθηκαν σε τριβλία κυτταροκαλλιέργειας. Έγινε ανάλυση της έκφρασης Src, FAK και Paxillin σε 10% SDS-PAGE Western-blot, immunoblot με τη χρήση ειδικών αντισωμάτων. (Stark 1979). Εξετάστηκε η έκφραση της καθε πρωτεϊνης με βάση την ένταση χρώσης ημιποσοτικά. Στη συνέχεια, για τη μελέτη του κλινικού υλικού, εξετάστηκαν 23 παιδιά με σταδίου IV νευροβλάστωμα από το Institut Curie, Παρίσι. Έγινε ανάλυση στις Κλινικές Πληροφορίες των ασθενών και εξετάστηκε με ανοσοϊστοχημεία κλινικό υλικό το οποίο προήλθε μετά από βιοψία με λεπτή βελόνη (FNA), μονιμοποίηση και διατήρηση του υλικού με μορφή cell block (Orell and Sterrett's Fine Needle Aspiration Cytology, Philadelphia 2005). Πραγματοποιήθηκε στατιστική ανάλυση στα αποτελέσματα της έκφρασης των ενζύμων στις κυτταρικές σειρές καθώς και στα αποτελέσματα ανοσοϊστοχημείας στα cell blocks από τις βιοψίες των ασθενών με Χ2. Η συσχέτιση της έκφρασης των ενζύμων με την επιβίωση των ασθενών πραγματοποιήθηκε με τις καμπύλες Kaplan Meier. Αποτελέσματα: Στις κυτταρικές σειρές νευροβλαστώματος παρατηρήθηκε αυξημένη έκφραση των πρωτεϊνών FAK, Src και Paxillin σε σύγκριση με την έκφραση της πρωτεϊνης μάρτυρα b-actin. Σε ότι αφορά το κλινικό δείγμα, η μέση ηλικία των ασθενών ήταν 3 ± 1.3 έτη (SD 0.2 με 5.5 έτη) . Οι ασθενείς χωρίστηκαν σε 8 άρρενα και 15 θήλεα άτομα. Όλοι οι ασθενείς ήταν σταδίου IV. Το γονίδιο N-myc ήταν υπερεκφρασμένο σε 9 ασθενείς. Η παρακολούθησή τους έγινε από 12 έως και 120 μήνες μετά τη διάγνωση (μέσος όρος 50 μήνες). Η έκφραση της FAK ήταν αυξημένη σε 14/23 ασθενείς (59%). Η Src kinase εμφάνισε αυξημένη έκφραση σε 8/23 ασθενείς (32%) και η Paxillin εμφάνισε αυξημένη έκφραση σε 9/23 ασθενείς (33%). Με βάση τα παρόντα στοιχεία, η μεμονωμένη έκφραση της FAK και της Src kinase φαίνεται πως δε συσχετίζεται σημαντικά με την επιβίωση των ασθενών. Η έκφραση της Paxillin, αντίθετα, δείχνει να συσχετίζεται σημαντικά με την κλινική έκβαση των ασθενών όταν το τελικό γεγονός ήταν η μη επιβίωση ή η επιβίωση με παρουσία νόσου είτε υποτροπής. Ταυτόχρονη έκφραση FAK-Src-Paxillin συσχετίζεται με πιο δυσμενή πρόγνωση παιδιών με νευροβλάστωμα σε σύγκριση με παιδιά που δεν εμφάνισαν έκφραση και των τριων πρωτεϊνών. Η ταυτόχρονη έκφραση του συμπλόκου FAK-Src-Paxillin σε συνδυασμό με την υπερέκφραση του γονιδίου N-Myc συσχετίστηκε με ακόμη πιο δυσμενή πρόγνωση. Συμπέρασμα: Η έκφραση του συμπλόκου FAK-Src-PΑΧ είναι αυξημένη σε κυτταρικές σειρές ανθρωπίνου νευροβλαστώματος. Η έκφραση του συμπλόκου FAK-Src-Paxillin είναι αυξημένη σε κλινικό υλικό ασθενών με νευροβλάστωμα και ίσως συνδέεται με δυσμενή έκβαση της κλινικής τους πορείας. Θεωρούμε πως το επόμενο βήμα είναι ίσως η στόχευση του συμπλόκου FAK-Src-Paxillin με ειδικούς αναστολείς μικρού μοριακού βάρους κάτι που ίσως οδηγήσει σε καλύτερη πρόγνωση των παιδιών με νευροβλάστωμα

scholarly journals Arrestins regulate cell spreading and motility via focal adhesion dynamics

2015 ◽  
Vol 26 (4) ◽  
pp. 622-635 ◽  
Author(s):  
Whitney M. Cleghorn ◽  
Kevin M. Branch ◽  
Seunghyi Kook ◽  
Christopher Arnette ◽  
Nada Bulus ◽  
...  
Keyword(s):  
Cell Motility ◽  
Focal Adhesion ◽  
Cell Attachment ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
Wild Type

Focal adhesions (FAs) play a key role in cell attachment, and their timely disassembly is required for cell motility. Both microtubule-dependent targeting and recruitment of clathrin are critical for FA disassembly. Here we identify nonvisual arrestins as molecular links between microtubules and clathrin. Cells lacking both nonvisual arrestins showed excessive spreading on fibronectin and poly-d-lysine, increased adhesion, and reduced motility. The absence of arrestins greatly increases the size and lifespan of FAs, indicating that arrestins are necessary for rapid FA turnover. In nocodazole washout assays, FAs in arrestin-deficient cells were unresponsive to disassociation or regrowth of microtubules, suggesting that arrestins are necessary for microtubule targeting–dependent FA disassembly. Clathrin exhibited decreased dynamics near FA in arrestin-deficient cells. In contrast to wild-type arrestins, mutants deficient in clathrin binding did not rescue the phenotype. Collectively the data indicate that arrestins are key regulators of FA disassembly linking microtubules and clathrin.

scholarly journals Focal Adhesion Targeting: The Critical Determinant of FAK Regulation and Substrate Phosphorylation

1999 ◽  
Vol 10 (8) ◽  
pp. 2507-2518 ◽  
Author(s):  
Yu Shen ◽  
Michael D. Schaller
Keyword(s):  
Cell Adhesion ◽  
Subcellular Localization ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Focal Adhesions ◽  
Wild Type ◽  
Critical Determinant ◽  
Single Region ◽  
Dependent Cell ◽  
Substrate Phosphorylation

The focal adhesion kinase (FAK) is discretely localized to focal adhesions via its C-terminal focal adhesion–targeting (FAT) sequence. FAK is regulated by integrin-dependent cell adhesion and can regulate tyrosine phosphorylation of downstream substrates, like paxillin. By the use of a mutational strategy, the regions of FAK that are required for cell adhesion–dependent regulation and for inducing tyrosine phosphorylation of paxillin were determined. The results show that the FAT sequence was the single region of FAK that was required for each function. Furthermore, the FAT sequence of FAK was replaced with a focal adhesion–targeting sequence from vinculin, and the resulting chimera exhibited cell adhesion–dependent tyrosine phosphorylation and could induce paxillin phosphorylation like wild-type FAK. These results suggest that subcellular localization is the major determinant of FAK function.

scholarly journals The Cytoplasmic Tyrosines of Integrin Subunit β1 Are Involved in Focal Adhesion Kinase Activation

2000 ◽  
Vol 20 (15) ◽  
pp. 5758-5765 ◽  
Author(s):  
Krister Wennerberg ◽  
Annika Armulik ◽  
Takao Sakai ◽  
Marjam Karlsson ◽  
Reinhard Fässler ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Phosphorylation Site ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
Integrin Subunit ◽  
Wild Type ◽  
Directed Cell Migration ◽  
Dependent Cell

ABSTRACT We have previously shown that mutation of the two tyrosines in the cytoplasmic domain of integrin subunit β1 (Y783 and Y795) to phenylalanines markedly reduces the capability of β1A integrins to mediate directed cell migration. In this study, β1-dependent cell spreading was found to be delayed in GD25 cells expressing β1AY783/795F compared to that in wild-type GD25-β1A. Focal adhesion kinase (FAK) tyrosine phosphorylation and activation were severely impaired in response to β1-dependent adhesion in GD25-β1AY783/795F cells compared to that in wild-type GD25-β1A or mutants in which only a single tyrosine was altered (β1AY783F or β1AY795F). Phosphorylation site-specific antibodies selective for FAK phosphotyrosine 397 indicated that the defect in FAK phosphorylation via β1AY783/795F lies at the level of the initial autophosphorylation step. Indeed, β1A-dependent tyrosine phosphorylation of tensin and paxillin was lost in the β1AY783/795F cells, consistent with the impairment in FAK activation. In contrast, p130CAS overall tyrosine phosphorylation was unaffected by the β1 mutations. Despite the defect in β1-mediated FAK activation, FAK was still localized to focal adhesions. Taken together, the phenotype of the GD25-β1AY783/795F cells resembles, but is distinct from, the phenotype observed in FAK-null cells. These observations argue that tyrosines 783 and 795 within the cytoplasmic tail of integrin subunit β1A are critical mediators of FAK activation and cell spreading in GD25 cells.

scholarly journals The Association of ASAP1, an ADP Ribosylation Factor-GTPase Activating Protein, with Focal Adhesion Kinase Contributes to the Process of Focal Adhesion Assembly

2002 ◽  
Vol 13 (6) ◽  
pp. 2147-2156 ◽  
Author(s):  
Yunhao Liu ◽  
Joost C. Loijens ◽  
Karen H. Martin ◽  
Andrei V. Karginov ◽  
J. Thomas Parsons
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
Ph Domain ◽  
Wild Type ◽  
Gtpase Activating Protein ◽  
Adp Ribosylation ◽  
Transient Overexpression ◽  
Adp Ribosylation Factor

ASAP1 (ADP ribosylation factor [ARF]- GTPase-activating protein [GAP] containing SH3, ANK repeats, and PH domain) is a phospholipid-dependent ARF-GAP that binds to and is phosphorylated by pp60Src. Using affinity chromatography and yeast two-hybrid interaction screens, we identified ASAP1 as a major binding partner of protein tyrosine kinase focal adhesion kinase (FAK). GlutathioneS-transferase pull-down and coimmunoprecipitation assays showed the binding of ASAP1 to FAK is mediated by an interaction between the C-terminal SH3 domain of ASAP1 with the second proline-rich motif in the C-terminal region of FAK. Transient overexpression of wild-type ASAP1 significantly retarded the spreading of REF52 cells plated on fibronectin. In contrast, overexpression of a truncated variant of ASAP1 that failed to bind FAK or a catalytically inactive variant of ASAP1 lacking GAP activity resulted in a less pronounced inhibition of cell spreading. Transient overexpression of wild-type ASAP1 prevented the efficient organization of paxillin and FAK in focal adhesions during cell spreading, while failing to significantly alter vinculin localization and organization. We conclude from these studies that modulation of ARF activity by ASAP1 is important for the regulation of focal adhesion assembly and/or organization by influencing the mechanisms responsible for the recruitment and organization of selected focal adhesion proteins such as paxillin and FAK.

EGF receptor regulation of cell motility: EGF induces disassembly of focal adhesions independently of the motility-associated PLCgamma signaling pathway

1998 ◽  
Vol 111 (5) ◽  
pp. 615-624 ◽  
Author(s):  
H. Xie ◽  
M.A. Pallero ◽  
K. Gupta ◽  
P. Chang ◽  
M.F. Ware ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Motility ◽  
Map Kinase ◽  
Signaling Pathway ◽  
Focal Adhesion ◽  
Kinase Activity ◽  
Egf Receptor ◽  
Focal Adhesions ◽  
Short Term ◽  
Egfr Kinase

A current model of growth factor-induced cell motility invokes integration of diverse biophysical processes required for cell motility, including dynamic formation and disruption of cell/substratum attachments along with extension of membrane protrusions. To define how these biophysical events are actuated by biochemical signaling pathways, we investigate here whether epidermal growth factor (EGF) induces disruption of focal adhesions in fibroblasts. We find that EGF treatment of NR6 fibroblasts presenting full-length WT EGF receptors (EGFR) reduces the fraction of cells presenting focal adhesions from approximately 60% to approximately 30% within 10 minutes. The dose dependency of focal adhesion disassembly mirrors that for EGF-enhanced cell motility, being noted at 0.1 nM EGF. EGFR kinase activity is required as cells expressing two kinase-defective EGFR constructs retain their focal adhesions in the presence of EGF. The short-term (30 minutes) disassembly of focal adhesions is reflected in decreased adhesiveness of EGF-treated cells to substratum. We further examine here known motility-associated pathways to determine whether these contribute to EGF-induced effects. We have previously demonstrated that phospholipase C(gamma) (PLCgamma) activation and mobilization of gelsolin from a plasma membrane-bound state are required for EGFR-mediated cell motility. In contrast, we find here that short-term focal adhesion disassembly is induced by a signaling-restricted truncated EGFR (c'973) which fails to activate PLCgamma or mobilize gelsolin. The PLC inhibitor U73122 has no effect on this process, nor is the actin severing capacity of gelsolin required as EGF treatment reduces focal adhesions in gelsolin-devoid fibroblasts, further supporting the contention that focal adhesion disassembly is signaled by a pathway distinct from that involving PLCgamma. Because both WT and c'973 EGFR activate the erk MAP kinase pathway, we additionally explore here this signaling pathway, not previously associated with growth factor-induced cell motility. Levels of the MEK inhibitor PD98059 that block EGF-induced mitogenesis and MAP kinase phosphorylation also abrogate EGF-induced focal adhesion disassembly and cell motility. In summary, we characterize for the first time the ability of EGFR kinase activity to directly stimulate focal adhesion disassembly and cell/substratum detachment, in relation to its ability to stimulate migration. Furthermore, we propose a model of EGF-induced motogenic cell responses in which the PLCgamma pathway stimulating cell motility is distinct from the MAP kinase-dependent signaling pathway leading to disassembly and reorganization of cell-substratum adhesion.

scholarly journals Campylobacter jejuni Triggers Signaling through Host Cell Focal Adhesions To Inhibit Cell Motility

mBio ◽  
2021 ◽  
Author(s):  
Courtney M. Klappenbach ◽  
Nicholas M. Negretti ◽  
Jesse Aaron ◽  
Teng-Leong Chew ◽  
Michael E. Konkel
Keyword(s):  
Epithelial Cells ◽  
Cell Motility ◽  
Host Cell ◽  
Campylobacter Jejuni ◽  
Focal Adhesion ◽  
Foodborne Pathogen ◽  
Focal Adhesions ◽  
Structure And Function ◽  
Content Type ◽  
And Function

Campylobacter jejuni is a major foodborne pathogen that causes severe gastritis. We investigated the dynamics of focal adhesion structure and function in C. jejuni -infected epithelial cells.

scholarly journals Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins.

1997 ◽  
Vol 17 (3) ◽  
pp. 1702-1713 ◽  
Author(s):  
D D Schlaepfer ◽  
M A Broome ◽  
T Hunter
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Intracellular Signaling ◽  
Protein Tyrosine Kinase ◽  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Sh2 Domain ◽  
Mitogen Activated Protein Kinase

The focal adhesion kinase (FAK), a protein-tyrosine kinase (PTK), associates with integrin receptors and is activated by cell binding to extracellular matrix proteins, such as fibronectin (FN). FAK autophosphorylation at Tyr-397 promotes Src homology 2 (SH2) domain binding of Src family PTKs, and c-Src phosphorylation of FAK at Tyr-925 creates an SH2 binding site for the Grb2 SH2-SH3 adaptor protein. FN-stimulated Grb2 binding to FAK may facilitate intracellular signaling to targets such as ERK2-mitogen-activated protein kinase. We examined FN-stimulated signaling to ERK2 and found that ERK2 activation was reduced 10-fold in Src- fibroblasts, compared to that of Src- fibroblasts stably reexpressing wild-type c-Src. FN-stimulated FAK phosphotyrosine (P.Tyr) and Grb2 binding to FAK were reduced, whereas the tyrosine phosphorylation of another signaling protein, p130cas, was not detected in the Src- cells. Stable expression of residues 1 to 298 of Src (Src 1-298, which encompass the SH3 and SH2 domains of c-Src) in the Src- cells blocked Grb2 binding to FAK; but surprisingly, Src 1-298 expression also resulted in elevated p130cas P.Tyr levels and a two- to threefold increase in FN-stimulated ERK2 activity compared to levels in Src- cells. Src 1-298 bound to both FAK and p130cas and promoted FAK association with p130cas in vivo. FAK was observed to phosphorylate p130cas in vitro and could thus phosphorylate p130cas upon FN stimulation of the Src 1-298-expressing cells. FAK-induced phosphorylation of p130cas in the Src 1-298 cells promoted the SH2 domain-dependent binding of the Nck adaptor protein to p130cas, which may facilitate signaling to ERK2. These results show that there are additional FN-stimulated pathways to ERK2 that do not involve Grb2 binding to FAK.

scholarly journals Cardiac fibroblasts require focal adhesion kinase for normal proliferation and migration

2009 ◽  
Vol 296 (3) ◽  
pp. H627-H638 ◽  
Author(s):  
Ana Maria Manso ◽  
Seok-Min Kang ◽  
Sergey V. Plotnikov ◽  
Ingo Thievessen ◽  
Jaewon Oh ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Adult Mouse ◽  
Cardiac Fibroblasts ◽  
Focal Adhesions ◽  
Protein Levels ◽  
Tyrosine Kinase 2 ◽  
A Cell ◽  
And Migration ◽  
Proliferation And Migration

Migration and proliferation of cardiac fibroblasts (CFs) play an important role in the myocardial remodeling process. While many factors have been identified that regulate CF growth and migration, less is known about the signaling mechanisms involved in these processes. Here, we utilized Cre-LoxP technology to obtain focal adhesion kinase (FAK)-deficient adult mouse CFs and studied how FAK functioned in modulating cell adhesion, proliferation, and migration of these cells. Treatment of FAKflox/flox CFs with Ad/Cre virus caused over 70% reduction of FAK protein levels within a cell population. FAK-deficient CFs showed no changes in focal adhesions, cell morphology, or protein expression levels of vinculin, talin, or paxillin; proline-rich tyrosine kinase 2 (Pyk2) expression and activity were increased. Knockdown of FAK protein in CFs increased PDGF-BB-induced proliferation, while it reduced PDGF-BB-induced migration. Adhesion to fibronectin was not altered. To distinguish between the function of FAK and Pyk2, FAK function was inhibited via adenoviral-mediated overexpression of the natural FAK inhibitor FAK-related nonkinase (FRNK). Ad/FRNK had no effect on Pyk2 expression, inhibited the PDGF-BB-induced migration, but did not change the PDGF-BB-induced proliferation. FAK deficiency had only modest effects on increasing PDGF-BB activation of p38 and JNK MAPKs, with no alteration in the ERK response vs. control cells. These results demonstrate that FAK is required for the PDGF-BB-induced migratory response of adult mouse CFs and suggest that FAK could play an essential role in the wound-healing response that occurs in numerous cardiac pathologies.

scholarly journals Contractility modulates cell adhesion strengthening through focal adhesion kinase and assembly of vinculin-containing focal adhesions

2010 ◽  
pp. n/a-n/a ◽  
Author(s):  
David W. Dumbauld ◽  
Heungsoo Shin ◽  
Nathan D. Gallant ◽  
Kristin E. Michael ◽  
Harish Radhakrishna ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Focal Adhesions
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