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Validated All-in-One™ qPCR Primer for PTK2(NM_153831.4) Search again
Product ID:
HQP159643
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
FADK, FADK 1, FAK, FAK1, FRNK, PPP1R71, p125FAK, pp125FAK
Gene Description:
protein tyrosine kinase 2
Target Gene Accession:
NM_153831.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. At least four transcript variants encoding four different isoforms have been found for this gene, but the full-length natures of only two of them have been determined.
Gene References into function
- Tyrosine phosphorylation of FAK regulates localization and downstream signaling with profound effects on cell movement.
- Regulation of G protein-linked guanine nucleotide exchange factors for Rho, PDZ-RhoGEF, and LARG by tyrosine phosphorylation: evidence of a role for focal adhesion kinase
- FAK regulates the activity of Akt/protein kinase B and GSK-3beta and the association of GSK-3beta with FAK to influence insulin-stimulated glycogen synthesis in hepatocytes.
- proliferative effect of fibronectin in combination with T cell lymphokines on psoriatic uninvolved basal keratinocyte progenitors may be due to abnormal in vivo integrin-driven focal adhesion kinase activity and downstream signaling.
- Laminin-10/11 and fibronectin differentially prevent apoptosis induced by serum removal via phosphatidylinositol 3-kinase/Akt- and MEK1/ERK-dependent pathways (Laminin 10; separate entry for Laminin 11).
- comparison with FAK2 of the mechanism of tyrosine phosphorylation upon vWF interaction with glycoprotein Ib-IX-V complex
- Nck-2 interacts with focal adhesion kinase (FAK), a cytoplasmic protein tyrosine kinase critically involved in the cellular control of motility
- beta1 integrin regulates fibroblast viability through a PI3K/Akt/protein kinase B signaling pathway in response to a matrix-derived mechanical stimulus
- Primary arrest of circulating platelets on collagen involves phosphorylation of Syk, cortactin and focal adhesion kinase
- This study reports two crystal structures of the focal adhesion targeting domain of focal adhesion kinase.
- IGF-I protects the cells from apoptosis by blocking the activation of caspases, which may be responsible for the loss of FAK and Akt.
- REVIEW: The focal adhesion kinase--a regulator of cell migration and invasion
- Mutated focal adhesion kinase induces apoptosis in a human glioma cell line
- The association of focal adhesion kinase with Wiskott-Aldrich syndrome protein is associated with cell migration in stromal cell-derived factor-1alpha-stimulated Jurkat cells
- The results of this study indicate that dual inhibition of focal adhesion kinase (FAK) and epidermal growth factor receptor (EGFR) signaling pathways can cooperatively enhance apoptosis in breast cancers.
- Cerivastatin-induced inhibition of glioblastoma cell migration was associated with the down-regulation of tyrosine phosphorylation of FAK. FAK phosphorylation correlated well with tumor cell invasiveness.
- Expression of focal adhesion kinase and alpha5 and beta1 integrins in carcinomas and its clinical significance.
- results indicated that the mitochondrial pathway is required for ionizing radiation-induced apoptosis, and focal adhesion kinase overexpression blocks this pathway, rendering antiapoptotic states.
- Functional involvement of src and focal adhesion kinase in a CD99 splice variant-induced motility of human breast cancer cells
- Engagement of CD44 either by its natural ligand hyaluronan or a specific antibody on a cell line induced tyrosine phosphorylation and activation of focal adhesion kinase.
- An altered relationship of FAK and Pyk2 was observed for different tumors and could also be important for osteosarcoma development
- Results reveal a novel mechanism of FAK phosphorylation by signalling cascades involving a member of the LDL receptor family.
- FAK NH(2)-terminal domain fragments have roles independent of Y397, kinase, and FAT domains
- R-Ras promotes focal adhesion formation by signaling to FAK and p130(Cas) through a novel mechanism that differs from but synergizes with the alpha2beta1 integrin.
- TGF-beta1 up-regulates expression of integrins and fibronectin, an effect that is associated with autophosphorylation/activation of FAK.
- Shear-induced platelet aggregation induced by 2B-rVWF binding to platelet GPIb produced pp125FAK at shear rate 4000 s-1 but not at 200 s-1
- caspase-3-mediated proteolysis of FAK, an anti-apoptotic protein, is regulated by hsp72
- FAK and Pyk2 function as important signaling effectors in gliomas and indicate that their differential regulation may be determining factors in the temporal development of proliferative or migrational phenotypes.
- This review of recent studeis provides considerable insight into the functional roles and signaling mechanisms of FAK as a positive regulator of both cell motility and cell survival.
- Augmented activation of FAK is an immediate signaling event required for the trans-regulation of integrin alpha L beta 2 by alpha 4 beta 1 in Jurkat T cells.
- Decidual beta1 integrin and FAK participate in this final step of implantation.
- FAK activity is regulated by low molecular weight phosphotyrosine phosphatase in human cells
- FAK is activated by VEGF in human brain microvascular endothelial cells
- Inhibition of FAK by antisense oligonucleotideds enhances the sensitivity of breast cancer cells to campothecin.
- CIB regulates platelet spreading through the regulation of FAK activation.
- FAK has a role in the pathology of human cancer [review]
- TIMP-1 activates cell survival signaling pathways involving focal adhesion kinase, phosphatidylinositol 3-kinase, and ERKs in human breast epithelial cells
- both c-Src/PI3K and c-Src/Fak/Erk1/2 pathways are involved in the up-regulation of c-myc and cyclin d1 expression mediated by prolactin
- FAK and Src are important survival factors, playing a role in protecting colon cancer cell lines from Adenovirus-containing FAK-CD (Ad-FAK-CD)-induced apoptosis
- beta1 integrin/FAK-mediated signaling on osteoblasts could be involved in ICAM-1- and RANKL-dependent osteoclast maturation
- FAK has a role in binding of soluble and surface-bound ligand to integrin alphaIIbbeta3
- All ESFT cell lines expressed five- to twenty-eight-fold-increased values of FAK, . These results raise the possibility that the overexpression of c-myc and FAK are involved in the poor prognosis of ESFT.
- PTK2 and EIF3S3, which, respectively, encode focal adhesion kinase and the p40 subunit of the eukaryotic initiation factor 3, were probable targets within the amplification at 8q23-q24 and may be involved in progression of HCC.
- pp125FAK interacts with the large conductance calcium-activated hSlo potassium channel in human osteoblasts: potential role in mechanotransduction
- focal adhesion kinase and src are stimulated by G alpha q and platelet activating factor receptor in vascular endothelium
- The above results indicate that PKB-Ser-473 and FAK-Tyr phosphorylation stimulated by TGF-beta1 are both dependent on cell adhesion.
- the proteolytic degradation of FAK is temporally distinct from its tyrosine dephosphorylation, occurring when apoptotic pathways are already initiated and during a generalized destruction of signaling proteins
- Extracellular pressure may increase integrin affinity and promote colon cancer adhesion via actin dependent inside-out focal adhesion kinase and Src signals. This mechanotransduced pathway may regulate metastasizing tumor cell adhesion.
- FAK could play an important role in hepatocellular carcinoma progression
- Calcium rises locally trigger focal adhesion disassembly and enhance residency of focal adhesion kinase at focal adhesions
- RhoA/Rho-kinase pathway followed by tyrosine phosphorylation of FAK and paxillin leads to ATP release and actin reorganization in vascular endothelium
- Cloning and characterization of the promoter region of human focal adhesion kinase gene and analysis of nuclear factor kappa B and p53 binding sites
- Results demonstrate FHL2 expression in human ovarian cancer cells, suggesting an important functional role of pp125FAK and FHL2 complex in gynecologic malignancies.
- FAK has a role functioning upstream of PI3K/Akt, in transducing a beta(1) integrin viability signal in collagen matrices
- Activation of rho had no effect on phosphorylation of FAK.
- Activation of FAK and ERK1/2 by MCSP appear to involve independent mechanisms.
- FAK and Akt are activated in the attached fibroblast-populated collagen matrix whereas the p53 level is relatively low; matrix detachment downregulates FAK and Akt activity and induces p53.
- focal adhesion kinase phosphorylation is mediated by VEGFR2 and regulated by heat shock protein 90 and Src kinase activities
- Data show that squamous cell carcinoma cells escape suspension-induced, p53-mediated anoikis by forming multicellular aggregates that use fibronectin survival signals mediated by integrin alpha(v) and focal adhesion kinase.
- The introduction of FAK siRNA in HL-60/FAK cells sensitized them against TRAIL-induced apoptosis, confirming that overexpressed FAK downregulates procaspase-8 expression, which subsequently inhibits downstream apoptosis pathway in the HL-60/FAK cells.
- Overexpression and Phosphorylation of focal adhesion kinase is associated with ovarian carcinoma
- The level of FAK tyrosine phosphorylation appeared to be inversely correlated with the level of the PTEN protein in human; the defect of PTEN in tumor cells could alter the phosphorylation of FAK
- overexpression of FAK promoted exit from G(1) in glioblastoma cells, enhanced expression of cyclins D1 and E while reducing expression of p27(Kip1) and p21(Waf1), and enhanced the kinase activity of the cyclin D1-cyclin-dependent kinase-4 (cdk4) complex
- the first FAK subdomain of the FERM domain of focal adhesion kinase has a role in its normal regulation and function in the cell
- the derepression of Rb-E2F-regulated genes leads to apoptosis through inactivation of focal adhesion kinase and activation of caspase-8
- Angiotensin II mediates an increase in FAK and paxillin phosphorylation and induces human umbilical vein endothelial cells migration through signal transduction pathways
- RET signals through focal adhesion kinase in medullary thyroid cancer cells.
- identified PTK2 SNPs that displayed strong signals in joint analysis of linkage and association (unadjusted P<10(-7)) with SLE
- appears to be involved in early events of integrin-mediated adhesion of circulating carcinoma cells under fluid flow in vitro and in vivo
- FAK siRNA-treated cells displayed a decrease in migration when serum or EGF (epidermal growth factor) were used as chemo-attractants; results demonstrated that inhibition of FAK protein leads to alterations in cell growth and migration.
- FAK protein overexpression coincides with Her-2/neu overexpression and may mediate HER2 signaling via Src, resulting in PI3K/Akt activation
- apoptotic is propagated by decreased phosphorylation of focal adhesion kinase (FAK), which is linked to increased phosphorylation of c-Jun N-terminal kinase (JNK) and to decreased levels of p53
- integrin alpha(v) inhibition abrogates FAK phosphorylation at focal adhesion sites and diminishes MMP-2 secretion leading to reduced migration and invasion of human coronary artery smooth muscle cells
- FAK can suppress p53-mediated apoptosis and inhibit transcriptional activity of p53
- In the prostate carcinoma PC-3 cell model, the action of the gastrin releasing peptide (GRP) analog, bombesin (BN), on the activation of focal adhesion kinase (FAK) and invasiveness suggests that this kinase might favor metastasis
- results indicate an additional mechanism for regulation of FAK activity during cell spreading and migration, involving Ser-722 phosphorylation modulated through the competing actions of GSK3beta and PP1
- SOCS-3 negatively regulates cell growth and cell motility by inhibiting Janus kinase (JAK)/STAT and FAK signalings in hepatocellular carcinoma cells
- We propose a model in which removal of FERM-mediated auto-inhibition is important to increase FAK catalytic activity but the translocation and clustering of this enzyme at the focal adhesions is required for maximal phosphorylation at Tyr-397.
- A regulatory mechanism of cell invasion was suggested whereby FAK promotes cell-surface presentation of MT1-MMP by inhibiting endophilin A2-dependent endocytosis
- Data show that alpha(v)beta3/Tat interaction triggers the activation of NF-kappaB in endothelial cells in a focal adhesion kinase-, RhoA- and pp60src-dependent manner, and this activation is required for motogenic activity of Tat in endothelial cells.
- Upregulation of focal adhesion kinase is associated with breast cancer
- JSAP1.FAK complex functions cooperatively as a scaffold for the JNK signaling pathway and regulator of cell migration on FN
- Data show that phosphorylation of focal adhesion kinase (FAK) at Tyr-397 is a key determinant of how FAK controls focal adhesion turnover.
- results suggest the possibility that therapeutic resistance to all-trans retinoic acid may be related to FAK overexpression
- phosphorylation of pp125(FAK) is a late, integrin-dependent event, results suggest that platelet activation and aggregation occur in vivo in these patients
- In vivo loss of FAK does not affect migration/proliferation of basal keratinocytes in the same way as it affects multipotent stem cells of the skin.
- FAK may act in glioblastoma as a downstream target of growth factor signaling, with integrins enhancing the impact of such signaling in the tumor microenvironment
- FAK regulates integrin-dependent MMP-2 and MMP-9 expression and release by T lymphoid cells through src kinase
- Data suggest that focal adhesion kinase plays a significant role in signaling pathways of a hepatocyte growth factor-responsive cell line derived from cholangiocarcinoma.
- FAK-induced down-modulation of RhoA activity via p190RhoGAP is a crucial step in signaling endothelial barrier restoration after increased endothelial permeability
- Inhibition of FAK by SHP-2 plays a crucial role in the morphogenetic activity of Helicobacter pylori CagA.
- Data suggest a model in which netrin stimulates UNC5 tyrosine phosphorylation and signaling in a manner dependent on the co-receptor DCC, through the recruitment of Src and FAK kinases.
- While in CXCR2-expressing cells FAK phosphorylation was adhesion-dependent and was stimulated by fibronectin, in CXCR1-expressing cells FAK phosphorylation was adhesion-independent.
- These studies also raise the possibility that fully active forms of c-Src and Fak in breast tumors.
- These data suggest that FAK might differently regulate apoptosis and focal adhesion formation through site-specific, Src-dependent tyrosine phosphorylation in senescent cells.
- Weak expression of FAK in invasive cervical cancer is a strong independent predictor of poor patient outcome.
- These data demonstrate a critical role for FAK in the regulation of cyclin-dependent kinase inhibitors (CDKIs) through two independent mechanisms: Skp2 dependent and Skp2 independent.
- FAK is up-regulated in NSCLC, and it may have a role in lung cancer progression
- FAK protein abundance appears regulated at the mRNA level during gut epithelial cell motility.
- The technique of RNA silencing [small interfering RNA] confirmed the role of FAK in invasive prostatic cancer.
- Gastrin-releasing peptide upregulates ICAM-1 via FAK promotes tumor cell motility and attachment to the extracellular matrix.
- Enhanced expression of FAK and phospho-FAK were observed in colon cancer tissues.
- CAGE promotes motility of cancer cells through activation of focal adhesion kinase (FAK.
- FAK signaling pathways provide a link between activation of ERK1/2 by extracellular matrix proteins and mesenchymal stem cell differentiation into osteoblasts
- Src and Rac1 have roles in focal adhesion kinase and ERK mitogenic signaling in epithelial cells
- Our results indicate that increased FAK phosphorylation at Ser-843 represses FAK phosphorylation at Tyr-397, thus suggesting a mechanism of cross-talk between these phosphorylation sites that could regulate FAK-mediated cell shape and migration.
- TGF-beta1 co-ordinately and independently activates the FAK and AKT protein kinase pathways to confer an anoikis-resistant phenotype to myofibroblasts.
- Downregulation of either FAK or ILK expression inhibited SPARC-mediated AKT phosphorylation, and targeting both FAK and ILK attenuated AKT activation more potently than targeting either FAK or ILK alone
- Src and focal adhesion kinase mediate cyclic mechanical strain-induced extracellular regulated kinase phosphorylation and proliferation of pulmonary epithelial cells.
- Study found that either carbachol or EGF promoted a striking ERK-dependent phosphorylation of FAK at Ser-910, but these agonists caused only slight stimulation of FAK at Tyr-397 in T84 cells.
- results delineate a novel force-activated inside-out Src/PI3K/FAK/Akt pathway by which cancer cells regulate their own adhesion.
- N-MYC induces FAK expression.
- Ephrin-A1 serves as a critical negative regulator in the tumorigenesis of gliomas by down-regulating EphA2 and FAK.
- role FAK plays in promoting cell invasion through the activation of distinct signaling pathways induced by EGF with protein MMP-9 transcription and secretion in follicular thyroid carcinoma cells
- Fak/Src signaling to the PI3-K/Akt-1 and MEK/Erk pathways undergoes a differentiation state-specific uncoupling in enterocytes.
- These results suggest that engagement of beta1 integrins on systemic lupus erythematosus T cells could induce FAK-mediated signaling and subsequent CD40L expression and proliferation.
- In kidney disease, increased parathyroid hyperplasia cell growth driven by enhanced EGFR could be further aggravated through elevations in integrin beta1 and FAK expression.
- The expression of phosphorylated FAK was documented in all 28 cytokeratin-positive breast cancer samples.
- Decreased acetylglucosaminyltransferase activity due to smaall interferingRNA expression in human breast carcinoma cells resulted in attenuation of the dephosphorylation of FAK induced by epidermal growth factor.
- c-Abl activation by insulin, via a modification of FAK response, may play an important role in directing mitogenic versus metabolic insulin receptor signaling.
- STAP-2 associates with FAK and enhances its degradation, proteasome inhibitors block FAK degradation, and STAP-2 recruits an endogenous E3 ubiquitin ligase, Cbl, to FAK.
- Catalytic activity is required for integrin alpha5beta1-stimulated Src (Proto-Oncogene Proteins pp60(c-src)) activation.
- These findings provide evidence that mutations in fibronectin, induce anoikis in human squamous cell carcinoma cells by modulating integrin alpha v-mediated phosphorylation of FAK and ERK.
- Not cell detachment, but the proteolytic cleavage (or inhibition) of FAK is a key modulator as well as a promising indicator of apoptosis in epithelial cells under oxidative stress.
- FAK causes defects in spreading, reinforcement of integrin-cytoskeleton linkages and migration and at the same time could ameliorate the adhesion of metastatic cells to suboptimal surfaces.
- provide direct evidence of conformational regulation of FAK in living cells and novel insight into the mechanism regulating FAK conformation
- The results presented here indicate that actin reorganization through FAK/PI3-K/Rac-1 activation operates in various human cancer cell systems supporting a functional role for FAK/PI-3K/Rac1/actin signaling in controlling cell motility.
- Increased focal Adhesion Kinase due to mutations of p53 is associated with breast and colon cancers
- MAP-kinase activity necessary for TGFbeta1-stimulated mesangial cell type I collagen expression requires adhesion-dependent phosphorylation of FAK tyrosine 397.
- Col-IV regulates the secretion of MMP-9 via a Src and FAK dependent pathway in MCF-7 cells
- These findings suggest that modified signaling mechanisms regulate cancer cell migration through an endothelial monolayer versus those involved in cell migration on or through ECM.
- Focal adhesion kinase as well as p130Cas and paxillin should be a crucial molecule undergoing stronger tyrosine phosphorylation in GD3-expressing melanoma cells.
- Structural basis for the interaction between FAK and CD4 is reported.
- indicate the involvement of FAK-dependent activation of extracellular signal-regulated kinase in Toll like receptor-mediated eosinophil stimulation
- Tac-beta1 inhibits cell spreading, at least in part, by preventing the phosphorylation of FAK at Tyr-397
- In human cells, FAK knockdown raised p53-p21 levels & slowed cell proliferation but did not cause apoptosis. Nuclear FAK plays a scaffolding role in facilitating cell survival through enhanced p53 degradation under stress.
- Concordant overexpression of p-FAK and p-ERK1/2 in extramammary Paget's disease (EMPD) is associated with the grade of malignancy of EMPD.
- identified the binding site of the p53 and FAK interaction and demonstrated that mutating this site and targeting the site with peptides affects p53 functioning and viability in the cells.
- PTPD1 is a component of a multivalent scaffold complex nucleated by FAK at specific intracellular sites
- These results strongly support that Elk-1 protein is a novel binding-protein partner for FAK, a finding that significantly broadens the potential functioning of FAK and Elk-1.
- HEPL maintains Cas family function in localization to focal adhesions, as well as regulation of FAK activity, focal adhesion integrity, and cell spreading.
- simultaneous inhibition of both Focal adhesion kinase and the insulin-like growth factor-I receptor represents a potential novel therapeutic approach in human pancreatic adenocarcinoma
- FAK expression is necessary for efficient phosphorylation of T-cell differentiation protein MAL following stimulation with bacterial lipopolysaccharide and protein I/II.
- Data show that NG2 and integrin alpha4 oppositely regulate anoikis in fibroblasts, and that NG2 and integrin alpha4 regulate FAK phosphorylation by PKCalpha-dependent and -independent pathways, respectively.
- Anoikis causes a down-activation of Fak, Src, Akt-1 and Erk1/2, a loss of Fak-Src association, and a sustained/enhanced activation of p38b, which is required as apoptosis/anoikis driver
- focal adhesion kinase mediates caveolin-1 up-regulation during epithelial to mesenchymal transition
- these data reported here support the conclusion that FAK enhances invasion of HNSCC by promoting both increased cell motility and MMP-2 production
- FAK induces KLF8 expression in human ovarian cancer cells by activating the PI3K-Akt signaling pathway, leading to the activation of KLF8 promoter by Sp1
- c-FLIPL promotes the motility of HeLa cells by activating FAK and ERK, and increasing MMP-9 expression.
- Data show that genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation.
- Focal adhesion kinase is phosphorylated in response to interferon-gamma-inducible GTPase expression.
- review of kinase-independent interaction of FAK with p53with focus on FAK and p53 signaling, which link signal transduction pathways
- FAK is expressed by advanced-stage neuroblastoma
- FAK has two nuclear export signal sequences, but only one of the signal sequences demonstrates full biological nuclear export activity.
- focal adhesion kinase controls the balance of adhesion types in cells, and that this is one of the determinants of whether a cancer cell can make stable matrix-degrading invadopodia.
- SRC-3/AIB1 is required for focal adhesion turnover and focal adhesion kinase activation.
- analysis of PAFR activation and pleiotropic effects on tyrosine phospho-EGFR/Src/FAK/paxillin in ovarian cancer
- Focal adhesion kinase (FAK)-related non-kinase inhibits myofibroblast differentiation through differential MAPK activation in a FAK-dependent manner.
- These data indicate that FAK is functioning in cell migration, but fibril-forming collagen-induced FAK degradation is necessary for endothelial tube formation.
- Results suggest that HAb18G/CD147 enhances the invasion and metastatic potentials of human hepatoma cells via integrin alpha3beta1-mediated FAK-paxillin and FAKPI3K-Ca(2+) signal pathways.
- These data support the cooperative function of Pyk2 and FAK in breast cancer progression and suggest that dual inhibition of FAK and Pyk2 is an efficient therapeutic approach for targeting invasive breast cancer.
- The interplay between FAK and ERK in androgen-independent prostate cancer cells (PC3 and DU145 cells), was investigated.
- Following down-regulation of MR-1, the phosphorylations of MLC2, focal adhesion kinase (FAK), and Akt were dramatically decreased
- FAK is essentially required in chondrocyte communication with type II collagen by regulating type II collagen expression and cell proliferation.
- FAK, mTOR and IGF-IR are inhibited by TAE226 in esophageal cancer cells
- The lysyl oxidase pro-peptide attenuates fibronectin-mediated activation of focal adhesion kinase and p130Cas in breast cancer cells.
- analysis of FAK expression regulation and therapeutic potential [review]
- PGE2 greatly induced hepatocellular carcinoma cell adhesion, migration, and invasion by activating FAK/paxillin/Erk pathway.
- Results describe a a novel mechanism by which vitronectin receptors and focal adhesion kinase could promote cancer metastasis via ERK5 activation.
- Bis-phosphorylated FAK is a useful biomarker of Src kinase inhibition in vivo.
- FAK supports Ras- and PI3K-dependent mammary tumor initiation, maintenance, and progression to metastasis.