• In recent years, the search for intracellular signaling integrator downstream of receptor tyrosine kinases provided valuable novel substrates. (springer.com)
  • Ang II-induced cellular events have been implicated, in part, in the activation of mitogen-activated protein (MAP) kinases. (aspetjournals.org)
  • Through its interaction with Vav2, AFAP1L1 regulates Rac activity and downstream control of PAK1/2/3 (p21-activated kinases) phosphorylation of myosin light chain (MLC) kinase and MLC2. (nature.com)
  • Intracellular signaling pathways that involve protein tyrosine kinases (PTKs) are critical for the control of most cellular processes. (chemdiv.com)
  • Both domains were initially identified as modules that recognize phosphorylated tyrosines in receptor tyrosine kinases and other signaling proteins. (chemdiv.com)
  • Accumulating proof shows that Syk can work as a tumor suppressor unlike various other tyrosine kinases that generally promote growth-stimulating activity resulting in tumorigenicity (15). (careersfromscience.org)
  • Activated receptor tyrosine kinases bind the Shc adaptor protein through its N-terminal phosphotyrosine-binding (PTB) and C-terminal Src homology 2 (SH2) domains. (elsevierpure.com)
  • How receptor tyrosine kinases activate Ras. (wikidata.org)
  • Canonically, the binding of ligands to their cognate receptors leads to the recruitment and phosphorylation of tyrosine kinases, which in turn recruit and phosphorylate STAT3 at Tyr705 (4). (abwizbio.com)
  • The present invention provides inhibitors of protein kinases comprising a molecule having at least a first moiety competent for penetration of the molecule into cells, and a second moiety for having a protein kinase inhibiting effect within the cells. (justia.com)
  • The present invention relates to cell permeable, stable conjugates comprising a cell-permeability enhancement moiety and a peptide or peptidomimetic, as selective inhibitors of protein kinases, to pharmaceutical compositions containing them, as well as to processes for the preparation and use of such complex molecules. (justia.com)
  • Protein kinases are involved in signal transduction pathways linking growth factors, hormones and other cell regulation molecules to cell growth, survival and metabolism under both normal and pathological conditions. (justia.com)
  • The superfamily of protein kinases includes protein kinase A and protein kinase C, as well as the more recently discovered protein kinase B (PKB). (justia.com)
  • Since PKB activation is PI′-3-kinase dependent, the persistent activation of certain protein tyrosine kinases, such as IGF−1 receptor, EGF receptor, PDGF receptor, pp60c-Src, and the like, leads to the persistent activation of PKB which is indeed encountered in many tumors. (justia.com)
  • The role of protein tyrosine kinases (PTKs) has been widely studied but less is known on the protein tyrosine phosphatases (PTPs) responsible for immunoregulation [ 3 ]. (biomedcentral.com)
  • The SH3 proteins interact with adaptor proteins and tyrosine kinases. (ufoscience.org)
  • Interacting with tyrosine kinases, SH3 proteins usually bind far away from the active site. (ufoscience.org)
  • What is the role for SH2 domains in signaling via receptor tyrosine kinases? (ufoscience.org)
  • SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. (ufoscience.org)
  • Like the other Vav proteins, Vav3 is phosphorylated (activated) following ligand binding to a variety of receptor tyrosine kinases (TKs), including EGF receptor, PDGF receptor, insulin receptor, and insulin-like growth factor I receptor. (cytoskeleton.com)
  • The Crk family of adaptor proteins (Crk I, Crk II and CrkL) are Src Homology 2 (SH2) and Src Homology 3 (SH3) domain-containing proteins that form protein complexes important for transmiting signals downstream of tyrosine kinases. (ecmbio.com)
  • The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). (umbc.edu)
  • Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. (umbc.edu)
  • Of all these proteins, mostly SH2 domain-containing protein-tyrosine phosphatase interacts with the PECAM-1 cytoplasmic domain. (wikipedia.org)
  • SHP-1 is a Src homology 2 (SH2) domain-containing tyrosine phosphatase that plays an essential role in negative regulation of immune cell activity. (reading.ac.uk)
  • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. (embl.de)
  • PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. (diabetesjournals.org)
  • PTEN (MMAC1/TEP1) is a dual-specificity protein phosphatase involved in signal transduction and tumor suppression ( 9 , 10 ). (diabetesjournals.org)
  • PTPH1 is a protein tyrosine phosphatase expressed in T cells but its effect on immune response is still controversial. (biomedcentral.com)
  • SRC homology 2 (SH2)-containing tyrosine phosphatase-2 (SHP-2) has a controversial effect on lymphocyte signaling. (biomedcentral.com)
  • Another negative regulator of hematopoietic cell development and function is SHP-1 (SRC homology 2 (SH2)-containing tyrosine phosphatase 1), that is mainly expressed in hematopoietic and lymphoid cells [ 8 ]. (biomedcentral.com)
  • CagA can specifically bind to the SH2 domain of Src homology 2 (SH2)-containing protein tyrosine phosphatase (SHP-2), which induces spatial configuration change of SHP-2 and activates it [ 40 ]. (biomedcentral.com)
  • Pure T-cell deficiencies are caused by defects in either a CD3 subunit (such as CD3 δ, CD3 ζ, CD3 ε ) or in CD45 tyrosine phosphatase, key proteins involved in pre-TCR and/or TCR signaling at the positive selection stage. (medscape.com)
  • AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes. (nature.com)
  • A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. (wikidata.org)
  • GRB2 (growth factor receptor-bound protein 2), an adaptor protein involved in signal transduction, contains a central SH2 domain flanked by two SH3 domains. (rndsystems.com)
  • The adaptor protein APS is a substrate of the insulin receptor and couples receptor activation with phosphorylation of Cbl to facilitate glucose uptake. (rcsb.org)
  • SHP-2 can hamper the TRIF (TIR-domain-containing adapter-inducing interferon-β) adaptor protein-dependent TLR4 and TLR3 signal transduction with a consequent block of the pro-inflammatory cytokine production [ 7 ]. (biomedcentral.com)
  • AND-34/BCAR3 (Breast Cancer Anti-Estrogen Resistance 3) associates with the focal adhesion adaptor protein, p130CAS/BCAR1. (molvis.org)
  • Receptor dimerization and autophosphorylation attracts proteins containing Src homology 2 (SH2) or phosphotyrosine binding (PTB) domains including adaptor proteins like FRS2 and GRB2. (springer.com)
  • SH2 (Src homology region 2) and PTB (phosphotyrosine-binding) domains are small protein modules that mediate protein-protein interactions involved in many signal transduction pathways. (chemdiv.com)
  • Adam Kashishian (Fred Hutchinson Cancer Research Center, Seattle): "The question of the specificity of Src homology 2 (SH2) domain/phosphotyrosine interactions has been an important one since the ability of the SH2 domains to bind phosphotyrosine- containing peptides was first shown. (the-scientist.com)
  • There is a great interest in studying phosphotyrosine dependent protein-protein interactions in tyrosine kinase pathways that play a critical role in many aspects of cellular function. (biomedcentral.com)
  • tensin4 TNS4) was defined as a faraway person in the tensin focal adhesion family members (Lo and Lo 2002 It really is a much smaller sized proteins compared to various other tensins in support of stocks the SH2 (Src homology 2) and PTB (phosphotyrosine binding) domains bought at the C-terminal ends of most various other tensins (Lo 2004 (body 1). (researchensemble.com)
  • 2007 The SH2 domain of cten interacts with phosphotyrosine-containing protein. (researchensemble.com)
  • SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. (ufoscience.org)
  • The ↑[Ca 2+ ] i activates a signaling cascade that involves, sequentially, calcium-calmodulin, nitric oxide synthase, guanylyl cyclase, and protein kinase G. This signal transduction pathway enables Cl − to pass through vesicular channels and act as a counterion for the transport of H + , so that the vesicles of secretogogue-stimulated cells become acidic. (jneurosci.org)
  • AFAP1L1 intersects several invadopodia pathway components through its multiple domains and motifs, including the following (i) pleckstrin homology domains that bind phospholipids generated at the plasma membrane by phosphoinositide 3-kinase, (ii) a direct filamentous-actin binding domain and (iii) phospho-tyrosine motifs (pY136 and pY566) that specifically bind Vav2 and Nck2 SH2 domains, respectively. (nature.com)
  • PIP3 binds to the pleckstrin homology (PH) domains of PKB, recruits it to the membrane where it is phosphorylated and converted to its activated form. (justia.com)
  • Vav3 contains a calponin homology (CH) domain, an acidic domain (AC), the Dbl homology (DH) and pleckstrin homology (PH) domains which are common to all Rho GEFs, an atypical cysteine-rich zinc finger (C1) domain, a proline rich domain, a Src homology-2 (SH2) domain, and two Src homology-3 (SH3) domains flanking the single SH2 region. (cytoskeleton.com)
  • Protein kinase Calpha therefore critically and negatively regulates SHP-1 function, forming part of a mechanism to retain SHP-1 in a basal active state through interaction with its SH2 domains, and phosphorylating its C-terminal Ser(591) upon cellular activation leading to inhibition of SHP-1 activity and an increase in the tyrosine phosphorylation status of its substrates. (reading.ac.uk)
  • Binding of insulin to its receptor activates the insulin receptor tyrosine kinase, resulting in autophosphorylation and phosphorylation of several substrates, including insulin receptor substrate (IRS)-1 through -4. (diabetesjournals.org)
  • EC 3.1.3.48 ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. (embl.de)
  • After binding, Shc is phosphorylated within the central collagen-homology (CH) linker region on Tyr-317, a residue remote to both the PTB and SH2 domains. (elsevierpure.com)
  • Inhibition is removed by tyrosine kinase (TK)-mediated phosphorylation of the conserved Tyr174 residue (on Vav3, Tyr173 corresponds to Vav1 Tyr174 based on Vav1 amino acid numbering) in the AC helix. (cytoskeleton.com)
  • The GDNF family ligands (GFLs) function through a glycosyl-phosphatidylinositol-(GPI) anchored coreceptor, GDNF family receptor alpha (GFRα), and rearranged during transfection (RET), a well-known receptor tyrosine kinase involved in kidney development, spermatogonial stem cell maintenance, and the development and maintenance of the sympathetic, parasympathetic, and enteric nervous systems [ 1 , 2 ]. (medsci.org)
  • Activation of human platelets by cross-linking of the platelet low-affinity IgG receptor, the Fcγ receptor IIA (Fcγ-RIIA), or by collagen is associated with rapid phosphorylation on tyrosine of the non-receptor tyrosine kinase syk. (elsevierpure.com)
  • Parafollicular (PF) cells secrete 5-HT in response to stimulation of a G-protein-coupled Ca 2+ receptor (CaR) by increased extracellular Ca 2+ (↑[Ca 2+ ] e ). (jneurosci.org)
  • Spry1, Spry2, and Spry4 but not Spry3 are induced transcriptionally and limit the duration and intensity mainly of ERK phosphorylation in response to growth factor (GF) stimulation (with the exception of EGF signaling). (springer.com)
  • Upon leptin stimulation the phosphorylation of STAT3 is one of the key events in JAK2-STAT3 pathway, followed by the dimerization and nuclear translocation of this molecule. (biomedcentral.com)
  • In addition, B-cell and/or T-cell receptor stimulation also results in phosphorylation of Vav3. (cytoskeleton.com)
  • EGF stimulation induces phosphorylation of Tyr-251, which increases binding of Crk to the SH2 domain of Abl, and promotes transactivation of Abl. (ecmbio.com)
  • PECAM-1 is a cell-cell adhesion protein which interacts with other PECAM-1 molecules through homophilic interactions or with non-PECAM-1 molecules through heterophilic interactions. (wikipedia.org)
  • Then these proteins can initiate signalling pathways. (wikipedia.org)
  • Among them are the Sprouty proteins which mainly act as inhibitors of growth factor-dependent neuronal and glial signaling pathways. (springer.com)
  • The functions of SH2 and PTB domains include targeting of their host proteins to different cellular compartments, assembly of key components of signaling pathways in response to extracellular signals, and the control of autoinhibition, activation and dimerization of their host proteins. (chemdiv.com)
  • The SH2 domains bind phosphorylated immunoreceptor tyrosine-based activation motifs (ITAMs) and therefore couple turned on immunoreceptors to multiple downstream signaling pathways. (careersfromscience.org)
  • Tyrosine phosphorylation of GRB2 SH3 domains reduces binding to Sos and negatively regulates downstream signaling pathways including Ras, JNK and MAPK. (rndsystems.com)
  • Benefits Diverse categories of pathways are activated in uFB and PD We carried out GSEA of gene transcription and protein expression information obtained in human HCC cell lines cultured in uFB and PD. (sykinhibitors.com)
  • However, close examination showed the results of protein data inclusion were rather opposite within the uFB and PD groups In uFB, the total quantity of pathways was decreased, whilst new pathways such as RIG I like receptor signaling were activated. (sykinhibitors.com)
  • What pathways are this gene/protein implicaed in? (cancerindex.org)
  • Nearly 60% of genetic alterations have been found in AML patients involve in signaling pathways including signaling of tyrosine kinase receptor FLT3. (lu.se)
  • They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). (umbc.edu)
  • Phosphorylation of syk increases its autophosphorylation activity measured in a kinase assay performed on syk immunoprecipitates. (elsevierpure.com)
  • The SH2 (Src Homology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. (ufoscience.org)
  • Phosphorylation is still observed, albeit sometimes reduced, in the presence of a combination of a protein kinase C inhibitor, Ro 31-8220, and the intracellular calcium chelator, BAPTA-AM, demonstrating independence from phosphoinositide-specific phospholipase C (PLC) activity. (elsevierpure.com)
  • What are physical characteristics found in all tyrosine kinase receptors? (flashcardmachine.com)
  • Upon activation of either PAR1 or PAR4 thrombin receptors, the association between the three proteins was retained, and Vav1 became phosphorylated on tyrosine and SHP-1 became phosphorylated on Ser(591). (reading.ac.uk)
  • Dramatic changes in domain coupling and structural rigidity, induced by Tyr-317 phosphorylation, may alter Shc function, bringing about marked differences in the association of unphosphorylated and phosphorylated Shc with its numerous partners, including activated membrane receptors. (elsevierpure.com)
  • Different growth factor receptors were known to bind different constellations of SH2 domain-containing proteins. (the-scientist.com)
  • Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. (embl-heidelberg.de)
  • The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. (cancerindex.org)
  • PTPH1 overexpression in Jurkat T cells reduces indirectly the TCR-induced serine phosphorylation of Mek, Erk, Jnk and AP-1 leading to a decreased IL-2 gene activation [ 13 ]. (biomedcentral.com)
  • Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. (embl.de)
  • The target specificity of individual SH2 domains is based on the recognition of the three amino acids carboxyl terminal to the phospho-tyrosine within the target molecule. (ufoscience.org)
  • Subsequent studies have shown that, while binding of SH2 domains to their target proteins is strictly regulated by tyrosine phosphorylation, most PTB domains actually bind to their (nonphosphorylated) targets constitutively. (chemdiv.com)
  • The SH3 domain of Src-family PTKs, which regulate many cellular functions, such as cell proliferation and differentiation, survival, migration and cytoskeletal modifications, is mainly involved in substrate recognition and downregulation of the kinase activity. (ufoscience.org)
  • In human platelets, SHP-1 was found to constitutively associate with its substrate Vav1 and, through its SH2 domains, with protein kinase Calpha. (reading.ac.uk)
  • Shc phosphorylation plays a pivotal role in the initiation of mitogenic signaling through the Ras/Raf/MEK/ERK pathway, but it is unclear if Tyr-317 phosphorylation affects Shc-receptor interactions through the PTB and SH2 domains. (elsevierpure.com)
  • As we mapped and mutated phosphorylation sites in the platelet-derived growth factor (PDGF) receptor, we found a dramatic difference in interactions of three tyrosines in the `kinase-insert' region. (the-scientist.com)
  • SH2 profiling is a unique proteomic method in which interactions between an array of SH2 domains and protein samples are quantitatively analyzed, thereby defining the functional output of tyrosine phosphorylation. (biomedcentral.com)
  • Furthermore, the deleterious aftereffect of missense mutations can occur not merely from immediate disruption of CAPN3 function(s), but additionally from disruption from the protein's structural integrity, that could affect its intra or intermolecular protein lead and interactions to decreased stability or altered localization. (exposed-skin-care.net)
  • Upon phosphorylation, STAT3 proteins dimerize and translocate to the nucleus where they bind to promoter elements of target genes and modulate their transcription (4). (abwizbio.com)
  • The dowstrean targets include cell cycle regulatory genes such as fos , cyclin D , c-Myc , pim1 and anti-apoptotic genes such as B-cell CLL/Lymphoma-2 ( Bcl-2 ), Bcl-xL , survivin and X-linked inhibitor of apoptosis protein ( XIAP ) (6). (abwizbio.com)
  • As opposed to other styles of muscles dystrophy, where mutations take place in genes encoding structural protein, calpainopathy was the initial reported kind of dystrophy predetermined by mutations within a gene encoding a proteolytic enzyme. (exposed-skin-care.net)
  • This domain occurred 332 times on human genes ( 753 proteins). (umbc.edu)
  • The cytotoxin-associated gene A ( cagA ) is one of the most important virulence genes of H. pylori , which is located at the end of cag pathogenicity island ( cag PAI) and encodes the 120-145 kDa CagA protein [ 7 ]. (biomedcentral.com)
  • Was this a function of differences in receptor primary sequence, their locations in the cell, or, possibly, the specificity of the protein kinase domain of the receptor? (the-scientist.com)
  • Ang II caused a rapid tyrosine phosphorylation of Src homology and collagen (Shc), which was inhibited by quercetin. (aspetjournals.org)
  • Fcγ-RIIA also undergoes phosphorylation in syk immunoprecipitates from platelets activated by cross-linking of Fcγ-RIIA but not by collagen, suggesting that it associates with the kinase. (elsevierpure.com)
  • Consistent with this, tyrosine-phosphorylated Fcγ-RIIA is precipitated by a glutathione S-transferase (GST) fusion protein containing the tandem src homology (SH2) domains of syk from Fcγ-RIIA-but not collagen-activated cells. (elsevierpure.com)
  • Two uncharacterized tyrosine-phosphorylated proteins of 40 and 65 kDa are uniquely precipitated by a GST fusion protein containing the tandem syk-SH2 domains in collagen-stimulated platelets. (elsevierpure.com)
  • Our study revealed that the ZNF500 mRNA and protein levels were higher in breast cancer tissues than those in their normal counterparts. (bvsalud.org)
  • The structure of this protein was determined by molecular cloning in 1990, when it was found out that PECAM-1 has N-terminal domain with 574 amino acids, transmembrane domain with 19 amino acids and C-terminal cytoplasmic domain with 118 amino acids. (wikipedia.org)
  • After the tyrosine is phosphorylated, PECAM-1 recruits Src homology 2 domain-containing signalling proteins. (wikipedia.org)
  • This entry represents the PTPase domain found in several tyrosine-specific protein phosphatases (PTPases). (embl.de)
  • Taxonomic distribution of proteins containing PTPc domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with PTPc domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing PTPc domain in the selected taxonomic class. (embl.de)
  • This domain is also known as the breakpoint cluster region-homology (BH) domain. (embl-heidelberg.de)
  • Taxonomic distribution of proteins containing RhoGAP domain. (embl-heidelberg.de)
  • The complete taxonomic breakdown of all proteins with RhoGAP domain is also avaliable . (embl-heidelberg.de)
  • This gene is highly expressed in fetal brain and encodes a protein of relative molecular mass 91K, named oligophrenin-1, which contains a domain typical of a Rho-GTPase-activating protein (rhoGAP). (embl-heidelberg.de)
  • lymphocyte cytosolic protein 2 (SH2 domain. (wikigenes.org)
  • The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. (cancerindex.org)
  • Which of the following is specifically bound by Src homology 2 domain? (ufoscience.org)
  • All NSP proteins contain an NH 2 -terminal SH2 (Src homology domain 2) domain, a central proline/serine-rich domain, and a COOH-terminal domain with modest homology to Ras subfamily GDP-exchange factors (GEFs). (molvis.org)
  • Crk II Tyr-221 (CrkL Tyr-207) phosphorylation is a negative regulatory site, while Crk Tyr-251 phosphorylation in the SH3 domain is a positive regulatory site. (ecmbio.com)
  • Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1. (umbc.edu)
  • The obvious benefit of this method is that the low sample requirement allows detection of SH2 binding in samples which are difficult to analyze using traditional protein interaction assays. (biomedcentral.com)
  • Adaptor proteins contain a series of protein-binding sites that link respective interaction partners to each other and facilitate the generation of larger signaling complexes (1). (ufoscience.org)
  • The complex molecules are preferably peptide conjugates having improved cell-permeability, serum stability and kinase selectivity compared to known protein kinase inhibitors. (justia.com)
  • Pharmaceutical compositions that include these protein kinase inhibitors, and methods of using such compositions for treatment of cancers and other diseases associated with protein kinase activity are also disclosed. (justia.com)
  • Since the protein lacks enzymatic activities, it will be difficult to develop chemical compounds capable to directly and specifically modulate Sprouty functions. (springer.com)
  • Mutation of either Tyr740 or 751 strongly reduced binding of an SH2 protein. (the-scientist.com)
  • Our results highlight a SNT-207858 new part for Syk tyrosine kinase in regulating cellular senescence and determine Syk-mediated senescence like a novel tumor suppressor pathway whose inactivation may contribute to melanoma tumorigenicity. (careersfromscience.org)
  • SH2 domains of cten and various other tensins bind towards the SIY442DNV site on DLC1 (Deleted in Liver organ Cancer tumor 1) and phosphorylation from the tyrosine is not needed (Liao et al. (researchensemble.com)
  • Systemic administration of PTEN ASO once a week in mice suppressed PTEN mRNA and protein expression in liver and fat by up to 90 and 75%, respectively, and normalized blood glucose concentrations in db / db and ob / ob mice. (diabetesjournals.org)
  • Thus, the expression of inactive PI3K mutants or chemical agents, such as wortmannin and LY294002 that interfere with PI3K activity, inhibit Akt phosphorylation, glucose uptake, and glycogen and lipid synthesis in vitro ( 7 , 8 ). (diabetesjournals.org)
  • We have identified a novel pathway that directs Lyn/Src family tyrosine kinase signals to the invadopodia to regulate sarcoma cell invasion via the molecule AFAP-1-like-1 (AFAP1L1), a new member of the AFAP (actin filament-associated protein) family. (nature.com)
  • These data define a novel pathway that directs Lyn/Src family tyrosine kinase signals to sarcoma cell invadopodia through specific recruitment of Vav2 and Nck2 to phosphorylated AFAP1L1, to control cell migration and invasion. (nature.com)
  • A. Kashishian, A. Kazlauskas, J.A. Cooper, "Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo," The EMBO Journal, 11[4]:1373-82, 1992. (the-scientist.com)
  • GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. (embl-heidelberg.de)
  • The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins. (embl-heidelberg.de)
  • By enhancing their GTPase activity, GAP proteins inactivate small Rho and Ras proteins, so inactivation of rhoGAP proteins might cause constitutive activation of their GTPase targets. (embl-heidelberg.de)
  • In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity. (embl-heidelberg.de)
  • To investigate the structural impact of Shc phosphorylation, molecular dynamics simulations were carried out using special-purpose Molecular Dynamics Machine-Grape computers. (elsevierpure.com)
  • Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. (embl-heidelberg.de)
  • We previously established SH2 profiling, a phosphoproteomic approach based on membrane binding assays that utilizes purified Src Homology 2 (SH2) domains as a molecular tool to profile the global tyrosine phosphorylation state of cells. (biomedcentral.com)
  • These molecular properties of PKB and its central role in tumorigenesis, implies that this protein kinase may be an attractive target for novel anti-cancer agents. (justia.com)
  • All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW. (ecmbio.com)
  • The antibody detects a 40 kDa* protein corresponding to the molecular mass of Crk II on SDS-PAGE immunoblots of human K562 cells stimulated with pervanadate. (phosphosolutions.com)
  • This review comprehends literatures on leptin and leptin resistance and especially discusses what STAT3 phosphorylation would contribute to central leptin resistance. (biomedcentral.com)
  • Ser727 phosphorylation can also stimulate mitochondrial STAT3, where it may trigger oxidative phosphorylation (9), confer stress protection by reducing reactive oxygen species (ROS) accumulation and apoptosis (10,11) and support Ras-induced malignant transformation (12). (abwizbio.com)
  • PI3K is composed of two subunits: the p85 regulatory subunit, containing two Src homology-2 domains, and the p110 catalytic subunit ( 2 - 4 ). (diabetesjournals.org)
  • Antibodies targeting CD markers or other extracellular proteins may be added prior to fixation if the epitope is disrupted by formaldehyde and/or methanol. (cellsignal.com)
  • Phosphorylation of SHP-1 was mediated by protein kinase C and negatively regulated the activity of SHP-1 as demonstrated by a decrease in the in vitro ability of SHP-1 to dephosphorylate Vav1 on tyrosine. (reading.ac.uk)
  • Src homology 2 (SH2) domains are evolutionary conserved small protein modules that bind specifically to tyrosine-phosphorylated peptides. (ufoscience.org)
  • The encoded protein is a member of the immunoglobulin superfamily and is likely involved in leukocyte transmigration, angiogenesis, and integrin activation. (wikipedia.org)
  • Furthermore, LY294002, a PI3-K inhibitor and a quercetin derivative, inhibited Ang II-induced JNK activation as well as Akt phosphorylation. (aspetjournals.org)
  • Western blot assays indicated that the proliferation of SK-Hep1 and HepG2 cells was inhibited by anti-FGF2 ds-Diabody through inhibiting the phosphorylation activation of AKT and MAPK. (bvsalud.org)
  • In addition ot Tyr705 phosphorylation, Ser727 is required for maximal activation although Tyr705 phopsohrylation plays a key activating role (7,8). (abwizbio.com)
  • Calpain 3 provides 54 and 51% series homology towards the 80 kDa subunits of - and m-calpains, respectively, and stocks similar properties with one of these ubiquitously portrayed calpains such as for example Ca2+- reliant activation and maximal activity at natural pH (1). (exposed-skin-care.net)
  • Platelet endothelial cell adhesion molecule (PECAM-1) also known as cluster of differentiation 31 (CD31) is a protein that in humans is encoded by the PECAM1 gene found on chromosome17q23.3. (wikipedia.org)
  • What does this gene/protein do? (cancerindex.org)
  • We describe here a new model for regulation of SHP-1 involving phosphorylation of its C-terminal Ser(591) by associated protein kinase Calpha. (reading.ac.uk)