Actin-Related Protein 3
Actin-Related Protein 2
Actin-Related Protein 2-3 Complex
Wiskott-Aldrich Syndrome Protein, Neuronal
Cell Surface Extensions
src Homology Domains
Lymphocyte migration through brain endothelial cell monolayers involves signaling through endothelial ICAM-1 via a rho-dependent pathway. (1/335)Lymphocyte extravasation into the brain is mediated largely by the Ig superfamily molecule ICAM-1. Several lines of evidence indicate that at the tight vascular barriers of the central nervous system (CNS), endothelial cell (EC) ICAM-1 not only acts as a docking molecule for circulating lymphocytes, but is also involved in transducing signals to the EC. In this paper, we examine the signaling pathways in brain EC following Ab ligation of endothelial ICAM-1, which mimics adhesion of lymphocytes to CNS endothelia. ICAM-1 cross-linking results in a reorganization of the endothelial actin cytoskeleton to form stress fibers and activation of the small guanosine triphosphate (GTP)-binding protein Rho. ICAM-1-stimulated tyrosine phosphorylation of the actin-associated molecule cortactin and ICAM-1-mediated, Ag/IL-2-stimulated T lymphocyte migration through EC monolayers were inhibited following pretreatment of EC with cytochalasin D. Pretreatment of EC with C3 transferase, a specific inhibitor of Rho proteins, significantly inhibited the transmonolayer migration of T lymphocytes, endothelial Rho-GTP loading, and endothelial actin reorganization, without affecting either lymphocyte adhesion to EC or cortactin phosphorylation. These data show that brain vascular EC are actively involved in facilitating T lymphocyte migration through the tight blood-brain barrier of the CNS and that this process involves ICAM-1-stimulated rearrangement of the endothelial actin cytoskeleton and functional EC Rho proteins. (+info)
Cell shrinkage regulates Src kinases and induces tyrosine phosphorylation of cortactin, independent of the osmotic regulation of Na+/H+ exchangers. (2/335)The signaling pathways by which cell volume regulates ion transporters, e.g. Na+/H+ exchangers (NHEs), and affects cytoskeletal organization are poorly understood. We have previously shown that shrinkage induces tyrosine phosphorylation in CHO cells, predominantly in an 85-kDa band. To identify volume-sensitive kinases and their substrates, we investigated the effect of hypertonicity on members of the Src kinase family. Hyperosmolarity stimulated Fyn and inhibited Src. Fyn activation was also observed in nystatin-permeabilized cells, where shrinkage cannot induce intracellular alkalinization. In contrast, osmotic inhibition of Src was prevented by permeabilization or by inhibiting NHE-1. PP1, a selective Src family inhibitor, strongly reduced the hypertonicity-induced tyrosine phosphorylation. We identified one of the major targets of the osmotic stress-elicited phosphorylation as cortactin, an 85-kDa actin-binding protein and well known Src family substrate. Cortactin phosphorylation was triggered by shrinkage and not by changes in osmolarity or pHi and was abrogated by PP1. Hyperosmotic cortactin phosphorylation was reduced in Fyn-deficient fibroblasts but remained intact in Src-deficient fibroblasts. To address the potential role of the Src family in the osmotic regulation of NHEs, we used PP1. The drug affected neither the hyperosmotic stimulation of NHE-1 nor the inhibition of NHE-3. Thus, members of the Src family are volume-sensitive enzymes that may participate in the shrinkage-related reorganization of the cytoskeleton but are probably not responsible for the osmotic regulation of NHE. (+info)
Regulation of endothelial cell myosin light chain kinase by Rho, cortactin, and p60(src). (3/335)Inflammatory diseases of the lung are characterized by increases in vascular permeability and enhanced leukocyte infiltration, reflecting compromise of the endothelial cell (EC) barrier. We examined potential molecular mechanisms that underlie these alterations and assessed the effects of diperoxovanadate (DPV), a potent tyrosine kinase activator and phosphatase inhibitor, on EC contractile events. Confocal immunofluorescent microscopy confirmed dramatic increases in stress-fiber formation and colocalization of EC myosin light chain (MLC) kinase (MLCK) with the actin cytoskeleton, findings consistent with activation of the endothelial contractile apparatus. DPV produced significant time-dependent increases in MLC phosphorylation that were significantly attenuated but not abolished by EC MLCK inhibition with KT-5926. Pretreatment with the Rho GTPase-inhibitory C3 exotoxin completely abolished DPV-induced MLC phosphorylation, consistent with Rho-mediated MLC phosphatase inhibition and novel regulation of EC MLCK activity. Immunoprecipitation of EC MLCK after DPV challenge revealed dramatic time-dependent tyrosine phosphorylation of the kinase in association with increased MLCK activity and a stable association of MLCK with the p85 actin-binding protein cortactin and p60(src). Translocation of immunoreactive cortactin from the cytosol to the cytoskeleton was noted after DPV in concert with cortactin tyrosine phosphorylation. These studies indicate that DPV activates the endothelial contractile apparatus in a Rho GTPase-dependent fashion and suggests that p60(src)-induced tyrosine phosphorylation of MLCK and cortactin may be important features of contractile complex assembly. (+info)
Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. (4/335)NMDA receptors are linked to intracellular cytoskeletal and signaling molecules via the PSD-95 protein complex. We report a novel family of postsynaptic density (PSD) proteins, termed Shank, that binds via its PDZ domain to the C terminus of PSD-95-associated protein GKAP. A ternary complex of Shank/GKAP/PSD-95 assembles in heterologous cells and can be coimmunoprecipitated from rat brain. Synaptic localization of Shank in neurons is inhibited by a GKAP splice variant that lacks the Shank-binding C terminus. In addition to its PDZ domain, Shank contains a proline-rich region that binds to cortactin and a SAM domain that mediates multimerization. Shank may function as a scaffold protein in the PSD, potentially cross-linking NMDA receptor/PSD-95 complexes and coupling them to regulators of the actin cytoskeleton. (+info)
Tyrosine phosphorylation of cortactin associated with Syk accompanies thromboxane analogue-induced platelet shape change. (5/335)Thromboxane A(2) (TxA(2)) is a potent vasoconstrictor and platelet agonist. Pharmacological studies have defined two classes of thromboxane receptors (TPs) in human platelets; sites that bind the agonist 1S-(1,2(5Z),3-(1E,3S),4)-7- 3-(3-hydroxy-4-(4'-iodophenoxy)-1-butenyl)-7-oxabicyclo-2.2. 1-heptan-2-yl-5-heptenoic acid (I-BOP) with high affinity support platelet shape change, whereas low affinity sites that bind irreversibly the antagonist GR 32191 transduce platelet aggregation. As the mechanisms of signal transduction involved in platelet aggregation begin to be elucidated, few results concern those involved in platelet shape change, which is independent of the engagement of GPIIb/IIIa. To elucidate the respective role of the two classes of pharmacological binding sites of TPs in shape change, platelets were incubated with I-BOP at low concentrations or stimulated by I-BOP at high concentrations after pretreatment with GR 32191 or activated with low concentrations of 8-epi-prostaglandin F(2)alpha. Under these three conditions, there is a rapid stimulation of protein tyrosine phosphorylation of the 80/85-kDa doublet identified as the cytoskeletal protein cortactin. Tyrosine phosphorylation of cortactin is kinetically correlated with the occurrence of shape change. These biochemical and morphological events are both inhibited by SQ 29548, a TP antagonist, indicating the specificity of the signal. Since tyrosine kinase Syk was activated early during platelet activation, we examined the possibility that cortactin is a potential substrate of Syk in TxA(2)-induced platelet shape change. p72 Syk phosphorylation and kinase activity took place during the period when platelets were changing shape upon low concentrations of I-BOP stimulation. Furthermore, cortactin was associated with Syk, and this association increases along with the level of phosphorylation. These data suggest a novel pathway for a G protein-coupled TxA(2) high affinity receptor to the protein-tyrosine kinase Syk, which is associated with cortactin in the very early steps of platelet activation. (+info)
An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation. (6/335)Invasive breast cancer cells have the ability to extend membrane protrusions, invadopodia, into the extracellular matrix (ECM). These structures are associated with sites of active matrix degradation. The amount of matrix degradation associated with the activity of these membrane protrusions has been shown to directly correlate with invasive potential. We demonstrate here that microinjection of polyclonal anti-cortactin antibodies blocks matrix degradation at invadopodia supporting the hypothesis that cortactin has a direct role in invasive behavior. MDA-MB-231, invasive breast cancer cells were sheared from the surface of a gelatin matrix to isolate invadopodia. Cortactin, paxillin and protein kinase C (PKC) mu, a serine kinase, were co-immunoprecipitated as a complex from invadopodia-enriched membranes. We confirmed the subcellular distribution of these proteins by immunolocalization and Western blotting. We also determined that, in contrast to its presence in invasive cells, this complex of proteins was not detected in lysates from non-invasive cells that do not form invadopodia. Taken together, these data suggest that the formation of this cortactin-containing complex correlates with cellular invasiveness. We hypothesize that this complex of molecules has a role in the formation and function of invadopodia during cellular invasion. (+info)
Signaling pathways and structural domains required for phosphorylation of EMS1/cortactin. (7/335)The structural characteristics of EMS1 (human cortactin) suggest that it may link signaling events to reorganization of the actin cytoskeleton. Interestingly, the EMS1 gene is commonly amplified and overexpressed in several human cancers, which may alter their invasive or metastatic properties. An 80 to 85-kDa mobility shift of EMS1 correlates with an alteration in subcellular distribution and is likely to represent an important regulatory event. In HEK 293 cells, epidermal growth factor treatment or cell detachment induced this shift, and this was blocked by the mitogen-activated protein/extracellular signal-regulated kinase kinase (MEK) inhibitor PD98059. Furthermore, expression of a constitutively active form of MEK induced the shift, indicating that MEK activation was both sufficient and necessary for this modification. The epidermal growth factor-induced shift correlated with increased phosphorylation on serine and threonine residues of the same tryptic phosphopeptides detected under basal conditions. Deletion of the helical-proline-rich region of the protein blocked the mobility shift and EMS1 phosphorylation. In vitro kinase assays demonstrated that the extracellular signal-regulated kinases represent candidate kinases for this region, although other MEK-regulated enzymes must also participate. These data identify MEK as an important intermediate involved in EMS1 phosphorylation and highlight the helical-proline-rich region as a key regulatory domain. (+info)
Synapse structure: glutamate receptors connected by the shanks. (8/335)A family of proteins has been identified whose members, the Shanks, physically link two major receptor complexes at excitatory synapses - NMDA receptors and metabotropic glutamate receptors. (+info)
Cortactin is a protein that plays a role in cell migration and adhesion. It is expressed in a variety of cell types, including fibroblasts, smooth muscle cells, and leukocytes. Cortactin is involved in the formation of actin-rich structures called podosomes, which are important for cell migration and invasion. It also plays a role in the regulation of actin polymerization and the assembly of focal adhesions, which are structures that connect cells to the extracellular matrix. Cortactin has been implicated in a number of diseases, including cancer, where it is often overexpressed and associated with increased cell migration and invasion.
Microfilament proteins are a type of cytoskeletal protein that make up the thinest filaments in the cytoskeleton of cells. They are composed of actin, a globular protein that polymerizes to form long, thin filaments. Microfilaments are involved in a variety of cellular processes, including cell shape maintenance, cell movement, and muscle contraction. They also play a role in the formation of cellular structures such as the contractile ring during cell division. In the medical field, microfilament proteins are important for understanding the function and behavior of cells, as well as for developing treatments for diseases that involve disruptions in the cytoskeleton.
Actin-Related Protein 3 (Arp3) is a protein that plays a crucial role in the formation and function of actin filaments, which are essential components of the cytoskeleton in cells. The cytoskeleton is a network of protein fibers that provides structural support and helps to maintain the shape of cells. Arp3 is a member of the actin-related protein (Arp) family, which is involved in the regulation of actin dynamics. Arp3 is a subunit of the Arp2/3 complex, which is responsible for the nucleation and branching of actin filaments. The Arp2/3 complex is activated by various signaling molecules, including the small GTPase protein Cdc42, and it promotes the formation of branched actin networks that are important for cell migration, endocytosis, and other cellular processes. Mutations in the ARPC3 gene, which encodes Arp3, have been associated with several human diseases, including hereditary motor and sensory neuropathy type IIIB (HMSN IIIB), which is a form of Charcot-Marie-Tooth disease. HMSN IIIB is a genetic disorder that affects the peripheral nervous system and is characterized by muscle weakness, sensory loss, and foot deformities.
Actin-Related Protein 2 (Arp2) is a protein that plays a crucial role in the assembly and disassembly of actin filaments, which are essential for cell movement, shape change, and intracellular transport. Arp2 is a subunit of the Arp2/3 complex, which is a multi-protein complex that nucleates the formation of new actin filaments from scratch. The Arp2/3 complex is activated by various signaling pathways and is involved in a wide range of cellular processes, including cell migration, endocytosis, and cytokinesis. Mutations in the Arp2/3 complex or its regulators have been implicated in various human diseases, including cancer, neurodegeneration, and immune disorders.
Actins are a family of globular, cytoskeletal proteins that are essential for the maintenance of cell shape and motility. They are found in all eukaryotic cells and are involved in a wide range of cellular processes, including cell division, muscle contraction, and intracellular transport. Actins are composed of two globular domains, the N-terminal and C-terminal domains, which are connected by a flexible linker region. They are capable of polymerizing into long, filamentous structures called actin filaments, which are the main component of the cytoskeleton. Actin filaments are dynamic structures that can be rapidly assembled and disassembled in response to changes in the cellular environment. They are involved in a variety of cellular processes, including the formation of cellular structures such as the cell membrane, the cytoplasmic cortex, and the contractile ring during cell division. In addition to their role in maintaining cell shape and motility, actins are also involved in a number of other cellular processes, including the regulation of cell signaling, the organization of the cytoplasm, and the movement of organelles within the cell.
Actin-Related Protein 2-3 Complex (Arp2/3 Complex) is a protein complex that plays a crucial role in the formation of actin filaments, which are essential for cell movement, division, and shape maintenance. The complex consists of seven subunits, including Arp2 and Arp3, which are encoded by the ARPC2 and ARPC3 genes, respectively. The Arp2/3 Complex is activated by various signaling pathways and binds to the sides of existing actin filaments, where it nucleates the assembly of new actin filaments. This process is known as branching, and it results in the formation of a network of actin filaments that can generate force and movement within the cell. Disruptions in the function of the Arp2/3 Complex have been implicated in various diseases, including cancer, neurodegenerative disorders, and immune system disorders. Therefore, understanding the regulation and function of the Arp2/3 Complex is important for developing new therapeutic strategies for these diseases.
Wiskott-Aldrich Syndrome Protein, Neuronal (WASP-Neuronal) is a protein that is involved in the regulation of the immune system and the development and maintenance of neurons in the brain. It is encoded by the WASP-Neuronal gene and is expressed primarily in neurons. Mutations in the WASP-Neuronal gene can lead to a rare genetic disorder called Wiskott-Aldrich syndrome (WAS), which is characterized by immune deficiency, eczema, and bleeding problems. WAS is caused by mutations in the WASP gene, which encodes the WASP protein. The WASP protein plays a critical role in the regulation of the immune system by controlling the movement of immune cells and the formation of immune cell structures called phagosomes. In addition to its role in the immune system, WASP-Neuronal is also involved in the development and maintenance of neurons in the brain. It is thought to play a role in the formation of synapses, which are the connections between neurons that allow them to communicate with each other. Mutations in the WASP-Neuronal gene can lead to neurological problems, including developmental delays, intellectual disability, and seizures. Overall, WASP-Neuronal is a protein that plays a critical role in the regulation of the immune system and the development and maintenance of neurons in the brain. Mutations in the WASP-Neuronal gene can lead to a range of health problems, including Wiskott-Aldrich syndrome and neurological disorders.
Cell surface extensions are structures that extend from the surface of a cell and are involved in various cellular functions. These extensions can be classified into two main types: primary and secondary. Primary cell surface extensions include hair-like structures called cilia and flagella. Cilia are short, hair-like structures that cover the surface of many cells, including those in the respiratory tract and the lining of the uterus. They are used to move mucus and other substances along the surface of the cell. Flagella, on the other hand, are longer and more whip-like structures that are used for movement. Secondary cell surface extensions include projections called microvilli and filopodia. Microvilli are small, finger-like projections that increase the surface area of cells and are involved in absorption and secretion. Filopodia are thin, thread-like projections that are involved in cell movement and communication. Cell surface extensions play important roles in many cellular processes, including cell movement, cell signaling, and nutrient absorption. They are also involved in the development and function of tissues and organs.
In the medical field, "src-family kinases" (SFKs) refer to a group of non-receptor tyrosine kinases that are involved in a variety of cellular processes, including cell growth, differentiation, migration, and survival. SFKs are activated by a variety of stimuli, including growth factors, cytokines, and hormones, and they play a critical role in regulating cell signaling pathways. SFKs are a subfamily of the larger tyrosine kinase family, which includes over 90 different kinases that are involved in a wide range of cellular processes. SFKs are characterized by their unique domain structure, which includes an N-terminal myristoylation site, a src homology 2 (SH2) domain, and a src homology 3 (SH3) domain. SFKs are involved in a variety of diseases, including cancer, cardiovascular disease, and inflammatory disorders. In cancer, SFKs are often overexpressed or activated, leading to uncontrolled cell growth and proliferation. In cardiovascular disease, SFKs are involved in the regulation of blood vessel function and the development of atherosclerosis. In inflammatory disorders, SFKs play a role in the activation of immune cells and the production of inflammatory mediators. Overall, SFKs are an important group of kinases that play a critical role in regulating cellular signaling pathways and are involved in a variety of diseases.
Dynamin II is a large GTPase protein that plays a crucial role in the process of endocytosis, which is the process by which cells internalize extracellular material. Dynamin II is responsible for the constriction and scission of the vesicle neck during endocytosis, which allows the vesicle to pinch off from the plasma membrane and form a new intracellular compartment. In addition to its role in endocytosis, dynamin II has also been implicated in a number of other cellular processes, including neurotransmitter release, vesicle trafficking, and intracellular signaling. Mutations in the gene encoding dynamin II have been associated with a number of human diseases, including Charcot-Marie-Tooth disease type 2D, hereditary spastic paraplegia, and some forms of cancer.
Tyrosine is an amino acid that is essential for the production of certain hormones, neurotransmitters, and other important molecules in the body. It is a non-essential amino acid, which means that it can be synthesized by the body from other amino acids or from dietary sources. In the medical field, tyrosine is often used as a dietary supplement to support the production of certain hormones and neurotransmitters, particularly dopamine and norepinephrine. These hormones play important roles in regulating mood, motivation, and other aspects of brain function. Tyrosine is also used in the treatment of certain medical conditions, such as phenylketonuria (PKU), a genetic disorder that affects the metabolism of phenylalanine, another amino acid. In PKU, tyrosine supplementation can help to prevent the buildup of toxic levels of phenylalanine in the body. In addition, tyrosine has been studied for its potential benefits in the treatment of other conditions, such as depression, anxiety, and fatigue. However, more research is needed to confirm these potential benefits and to determine the optimal dosage and duration of tyrosine supplementation.
The cytoskeleton is a complex network of protein filaments that extends throughout the cytoplasm of a cell. It plays a crucial role in maintaining the shape and structure of the cell, as well as facilitating various cellular processes such as cell division, movement, and intracellular transport. The cytoskeleton is composed of three main types of protein filaments: microfilaments, intermediate filaments, and microtubules. Microfilaments are the thinnest filaments and are involved in cell movement and muscle contraction. Intermediate filaments are slightly thicker than microfilaments and provide mechanical strength to the cell. Microtubules are the thickest filaments and serve as tracks for intracellular transport and as the structural framework for the cell. In addition to these three types of filaments, the cytoskeleton also includes various associated proteins and motor proteins that help to regulate and control the movement of the filaments. Overall, the cytoskeleton is a dynamic and essential component of the cell that plays a critical role in maintaining cellular structure and function.
The actin cytoskeleton is a complex network of protein filaments, including actin filaments, that extends throughout the cytoplasm of cells. It plays a crucial role in maintaining cell shape, facilitating cell movement, and enabling intracellular transport. The actin cytoskeleton is dynamic, constantly undergoing assembly and disassembly in response to changes in the cell's environment. It is composed of actin monomers, which polymerize to form filaments, and a variety of associated proteins that regulate filament assembly, stability, and function. Disruptions in the actin cytoskeleton can lead to a range of cellular abnormalities and diseases, including cancer, neurodegenerative disorders, and immune system dysfunction.
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- Phospho-Cortactin (Tyr421) Antibody detects endogenous levels of Cortactin only when phosphorylated at Tyrosine 421. (affbiotech.cn)
- CXCL12 induces tyrosine phosphorylation of cortactin, which plays a role in CXC chemokine receptor 4-mediated extracellular signal-regulated kinase activation and chemotaxis. (meharryresearch.org)
- Thus, our results indicate a novel role of H-Ras/ERK signaling and cortactin in the aggressive transformation of human mosethelial cells by SWCNT. (cdc.gov)
- Cortactin expression was shown to be controlled by the H-Ras/ERK signaling. (cdc.gov)
- Integrin alpha V and cortactin, but not epitheial-mesenchymal transition (EMT) transcriptional regulators, were up-regulated in the SWCNT-exposed cells, suggesting their role in the aggressive phenotype. (cdc.gov)
- 7. Cortactin Phosphorylation by Casein Kinase 2 Regulates Actin-Related Protein 2/3 Complex Activity, Invadopodia Function, and Tumor Cell Invasion. (nih.gov)
- Tyrosine phosphorylation of nmMLCK increased kinase activity, reversed nmMLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhanced binding to the critical actin-binding phosphotyrosine protein, cortactin. (johnshopkins.edu)
- Conversely, reduced c-Abl expression in EC (siRNA) markedly attenuated S1P-mediated cortical actin formation, reduced the EC modulus of elasticity (assessed by atomic force microscopy), reduced nmMLCK and cortactin tyrosine phosphorylation, and attenuated S1P-mediated barrier enhancement. (johnshopkins.edu)
- We built an invadopodia disassembly model where a signaling axis including TrioGEF Rac1 PAK1 and phosphorylation of cortactin causing invadopodia dissolution. (research-in-field.com)
- PAK within a GIT-PIX-PAK-Nck complicated located at focal adhesions settings adhesion-induced Rac1 activation and cell growing by regulating Rac1-β-Pix discussion [16 17 Furthermore PAK also modulates cytoskeleton dynamics and cell flexibility at the industry leading through phosphorylation of multiple substrates including myosin light-chain kinase (MLCK) paxillin filamin A cortactin the LIM-kinases (LIMKs) Arpc1b and stathmin . (biongenex.com)
- Actin cytoskeleton (green), the focal adhesion protein, paxillin (red), and the actin regulatory protein cortactin (blue) in a migrating fibroblast. (nih.gov)
- 2. Nanobodies targeting cortactin proline rich, helical and actin binding regions downregulate invadopodium formation and matrix degradation in SCC-61 cancer cells. (nih.gov)
- 9. Fascin actin bundling controls podosome turnover and disassembly while cortactin is involved in podosome assembly by its SH3 domain in THP-1 macrophages and dendritic cells. (nih.gov)
- These studies indicate an essential role for Abl kinase in vascular barrier regulation via posttranslational modification of nmMLCK and strongly support c-Abl-cortactin-nmMLCK interaction as a novel determinant of cortical actin-based cytoskeletal rearrangement critical to S1P-mediated EC barrier enhancement. (johnshopkins.edu)
- Shimamura S, Sasaki K and Tanaka M: The Src substrate SKAP2 regulates actin assembly by interacting with WAVE2 and cortactin proteins. (sasaki-institute.org)
- 19. Co-localization of cortactin and phosphotyrosine identifies active invadopodia in human breast cancer cells. (nih.gov)
- 15. Invadopodia proteins, cortactin, N-WASP and WIP differentially promote local invasiveness in ameloblastoma. (nih.gov)
- 6. Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation. (nih.gov)
- 8. Dissecting the functional domain requirements of cortactin in invadopodia formation. (nih.gov)
- 10. Cortactin and fascin-1 regulate extracellular vesicle release by controlling endosomal trafficking or invadopodia formation and function. (nih.gov)
- 11. An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion. (nih.gov)
- 16. The phosphatase Shp1 interacts with and dephosphorylates cortactin to inhibit invadopodia function. (nih.gov)
- 18. Cortactin function in invadopodia. (nih.gov)
- 20. Met receptor tyrosine kinase signals through a cortactin-Gab1 scaffold complex, to mediate invadopodia. (nih.gov)
- 12. Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. (nih.gov)
- Detection of Human Cortactin antibody by Western Blot. (labome.cn)
- Immunohistochemical analysis of paraffin-embedded Breast ca using Cortactin (PA5-27134) antibody at 1:250 dilution. (labome.cn)
- Western Blot analysis of Cortactin using anti-Cortactin Polyclonal Antibody (PA5-27134), in Hep G2 Cell Lysate (30 ug of cell lysate) and at a dilution of 1:1000. (labome.cn)
- Immunofluorescence analysis of methanol-fixed HeLa cells using Cortactin (PA5-29799) antibody at 1:200 dilution. (labome.cn)
- Immunohistochemical analysis of paraffin-embedded Cal27 xenograft using Cortactin (PA5-29799) antibody at 1:100 dilution. (labome.cn)
- Western Blot analysis of Cortactin using anti-Cortactin Polyclonal Antibody (PA5-29799), in H1299 Cell Lysate (30 ug of cell lysate) and at a dilution of 1:10000. (labome.cn)
- The membrane was incubated with rabbit anti-cortactin antigen affinity purified polyclonal antibody (Catalog # A01253-1) at 0.5 ug/mL overnight at 4 0 0 C, then washed with TBS-0.1%Tween 3 times with 5 minutes each and probed with a goat anti-rabbit IgG-HRP secondary antibody at a dilution of 1:10000 for 1.5 hour at RT. (labome.cn)
- 5. Phosphorylated cortactin recruits Vav2 guanine nucleotide exchange factor to activate Rac3 and promote invadopodial function in invasive breast cancer cells. (nih.gov)
- 3. Stratifying fascin and cortactin function in invadopodium formation using inhibitory nanobodies and targeted subcellular delocalization. (nih.gov)
- 2007). Src, cortactin and Arp2/3 complex are required for E-cadherin-mediated internalization of Listeria into cells . (up.pt)