• p130Cas/BCAR1 is a member of the Cas family (Crk-associated substrate) of adaptor proteins which is characterized by the presence of multiple conserved motifs for protein-protein interactions, and by extensive tyrosine and serine phosphorylations. (wikipedia.org)
  • These Cas proteins have a high structural homology, characterized by the presence of multiple protein interaction domains and phosphorylation motifs through which Cas family members can recruit effector proteins. (wikipedia.org)
  • A large scale purification of Ptdlns 3-kinase was developed to allow gel purification and peptide sequence analysis of both the 85 kDa and 110 kDa proteins. (ucl.ac.uk)
  • Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform. (embl.de)
  • A multiple alignment of representative PX domain sequences from eukaryotic proteins [ ( PUBMED:9687503 ) ], shows relatively little sequence conservation, although their structure appears to be highly conserved. (embl.de)
  • There are 32485 PX domains in 32392 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing PX domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with PX domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing PX domain in the selected taxonomic class. (embl.de)
  • The yeast PX domain-only proteins Grd19p (YOR357C) and Ypt35p (YHR105W), as well as the isolated PX domains from Mvp1p (YMR004W), Snx42p/Cvt20p/Atg20p (YDL113C), Vam7p (YGL212W), and Vps17p (YOR132W), yielded a total of 40 reproducible two-hybrid interactions. (embl.de)
  • Thirty-five interactions were found for the full-length proteins of Bem1p (YBR200W), Snx42p, Snx4p/Cvt13p (YJL036W), Vam7p, Vps5p (YOR069W), and Vps17p, but these appear not to require the PX domain, because these interactions could not be reproduced with PX-only baits. (embl.de)
  • Their selectivity with STAT-3 and other STAT family proteins still needs further exploration. (biomedcentral.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 SH3 domain is a 60 amino acids segment shared by diverse structural and signaling proteins [ 6 ]. (oncotarget.com)
  • Here, we show that insulin-induced activation of ERKs was enhanced by stable overexpression of growth factor receptor-bound protein 2 (GRB2) but not by overexpression of GRB2 proteins with point mutations in the Src homology 2 and 3 domains. (nih.gov)
  • 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)
  • The ECM proteins bind to the extracellular domains of integrin heterodimers, whereas the actin stress fibers link to integrin cytoplasmic tails via large molecular complexes. (rupress.org)
  • 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)
  • There are 47093 RhoGAP domains in 46979 proteins in SMART's nrdb database. (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)
  • Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins. (embl-heidelberg.de)
  • Outcomes Inhibitions of PDGF receptor kinase, the docking proteins element Src-family kinases, as well as the success component PI3K all eradicated PDGF-stimulated ROS creation and corroborated using the suppressed cell development. (thetechnoant.info)
  • Among the goals for ROS in vivo may be the reversible oxidation of phosphatases, which as well as proteins tyrosine kinases are in charge of maintaining a standard proteins tyrosine phosphorylation-dephosphorylation homeostasis in cell signaling in vivo [5,14]. (thetechnoant.info)
  • Included in these are Src family members kinases, phosphatidylinositol-3-kinase (PI3K), phospholipase C (PLC) and little GTP-binding proteins Ras [34-36]. (thetechnoant.info)
  • The SH2 domain binds to phosphotyrosine residues in RTKs such as PDGF and EGF, non-RTKs such as Bcr/Abl and FAK, and docking proteins such as FRS-2 and Gab1. (rndsystems.com)
  • There are 37989 PTPc domains in 29134 proteins in SMART's nrdb database. (embl.de)
  • 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)
  • non-etheless there are many exceptions like the SH2 domains of SLAM-associated proteins (aka SAP SH2D1A) and cten where the binding needs Temocapril the tyrosine but irrespective of its phosphorylation position. (researchensemble.com)
  • CAPN3 provides some exclusive domains including its NH2-terminal domains I which has 20C30 additional proteins not within - and m-calpains and two exclusive insertion sequences' of 62 and 77 proteins on the COOH-terminal parts of domains II (known as Is normally1) and domains III (known as IS2). (exposed-skin-care.net)
  • 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)
  • This domain occurred 332 times on human genes ( 753 proteins). (umbc.edu)
  • Among the regulators of p130Cas/BCAR1 tyrosine phosphorylation, receptor tyrosine kinases (RTKs) and integrins play a prominent role. (wikipedia.org)
  • The substrate domain consists of 15 repeats of the YxxP consensus phosphorylation motif for Src family kinases (SFKs). (wikipedia.org)
  • Binding of IL-10 to the extracellular domain of IL-10R1 activates phosphorylation of the receptor-associated Janus tyrosine kinases, JAK1 and Tyk2. (nih.gov)
  • These kinases then phosphorylate specific tyrosine residues (Y446 and Y496) on the intracellular domain of the IL-10R1 chain. (nih.gov)
  • This study gives insight into the interactions between PDGFRβ and Abl2 in the context of Abl2 regulation, and also provide a framework to better understand how growth factor receptors can engage with and regulate Abl family kinases through multistep phosphorylation events. (yale.edu)
  • 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)
  • 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)
  • signaling in the zoom lens epithelial cells, where concerted efforts from the upstream the different parts of PDGF receptor kinase, Src-family kinases, PI3K, Rac, and Ras protein are needed. (thetechnoant.info)
  • Each isoform serves via two receptor tyrosine kinases of PDGFR and PDGFR inducing dimerization of receptors and autophosphorylation of distinct tyrosines in the intracellular domains from the receptor. (thetechnoant.info)
  • 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)
  • In addition, B-cell and/or T-cell receptor stimulation also results in phosphorylation of Vav3. (cytoskeleton.com)
  • The SH3-SH2-SH3 C-terminal domains bind directly with the auto-phosphorylated cytoplasmic tails of the receptor TKs while the B- and T-cell receptors activate cytosolic TKs. (cytoskeleton.com)
  • Recombinant expressed p85 α and p85β associate with and are phosphorylated by both platelet-derived growth factor receptor and Polyoma middle T antigen;pp60c-src complexes in vitro. (ucl.ac.uk)
  • c-Src (cellular Src), encoded by Src gene, is a non-receptor tyrosine kinase first isolated as the normal cellular homolog to the potent avian sarcoma viral transforming oncogene v-Src [ 4 ]. (intechopen.com)
  • 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)
  • 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)
  • STAT3 binds to these sites via its SH2 (Src homology 2) domain, and is, in turn, tyrosine-phosphorylated by the receptor-associated JAKs. (nih.gov)
  • MB&B professors Dr. Karen Anderson and Dr. Anthony Koleske published a paper this month in the Journal of Biological Chemistry called 'Platelet-derived growth factor receptor beta activates Abl2 via direct binding and phosphorylation. (yale.edu)
  • us pharmacological inhibitors such as Picroto in GABAA receptor antagonist, Pertussis to in Gi protein coupled receptor pathway inhibitor, Herbimycin A tyrosine kinase inhibitor, Chelerythrine chloride protein kinase C inhibitor, not Wortmannin A phosphoinositide 3 kinase inhibitor, H 89 cAMP dependent protein kinase A inhibitor for 1 hr at 37 C with 5% CO2 in humidified air prior to the addition of human SIZP. (vegfr-3inhibitor.com)
  • Hepatocyte growth factor (HGF) is produced by stromal and mesenchymal cells, and it stimulates epithelial cell proliferation, motility, morphogenesis and angiogenesis in various organs via tyrosine phosphorylation of its cognate receptor, Met. (spandidos-publications.com)
  • Coexpression with Src-homology 2B1 (SH2B1), like coexpression with GH-bound GH receptor, partially restores the activity of all three JAK2 mutants. (biobender.com)
  • Coexpression with Src-homology 2 (SH2)B1, like coexpression with GH-bound GH receptor, also partially restored their kinase activity. (biobender.com)
  • Based on these results and the crystal structure of the JAK2 kinase domain name, we hypothesize that small changes in the conformation of the regions of JAK2 surrounding Tyr 868, 966, and 972 due, for example, to phosphorylation, binding to a ligand-bound cytokine receptor, and/or binding to SH2B1, may be essential for JAK2 to presume a maximally active conformation. (biobender.com)
  • 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)
  • Structurally, all known receptor PTPases, are made up of a variable length extracellular domain, followed by a transmembrane region and a C-terminal catalytic cytoplasmic domain. (embl.de)
  • Some of the receptor PTPases contain fibronectin type III (FN-III) repeats, immunoglobulin-like domains, MAM domains or carbonic anhydrase-like domains in their extracellular region. (embl.de)
  • 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)
  • IRS then binds to the regulatory subunit of PI3K through its Src homology domains, and this interaction activates the catalytic unit. (diabetesjournals.org)
  • the preferred GFRα coreceptor for GDNF is GFRα1, although GDNF also weakly binds to GFRα2 and GFRα3 [ 3 ]. (medsci.org)
  • We report that cten binds to another tumor suppressor, deleted in liver cancer 1 (DLC-1), and the SH2 domain of cten is responsible for the interaction. (rupress.org)
  • 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)
  • The remaining carboxy-terminal sequence contains a bipartite Src-binding domain (residues 681-713) able to bind both the SH2 and SH3 domains of Src. (wikipedia.org)
  • c-Src tyrosine kinase plays an important role in signal transduction pathways, where its activity is regulated by phosphorylation of the two tyrosine residues. (intechopen.com)
  • To investigate the conformational change of c-Src tyrosine kinase, we applied network analysis to time series of correlation among residues. (intechopen.com)
  • With centrality measures such as betweenness centrality, degree centrality, and closeness centrality, we observed a few important residues that significantly contribute to the conformational change of c-Src tyrosine kinase for the different time steps. (intechopen.com)
  • The PX domain is approximately 120 residues long [ ( PUBMED:11373621 ) ], and folds into a three-stranded beta-sheet followed by three -helices and a proline-rich region that immediately preceeds a membrane-interaction loop and spans approximately eight hydrophobic and polar residues. (embl.de)
  • Once phosphorylated, these tyrosine residues (and their flanking peptide sequences) serve as temporary docking sites for the latent transcription factor, STAT3 (signal transducer and activator of transcription-3). (nih.gov)
  • PKB activation involves phosphorylation of two amino acid residues, Ser473 and Thr308. (justia.com)
  • Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. (embl.de)
  • It had been soon found that many PTB domains bind to tyrosine residues irrespective of their phosphorylation position. (researchensemble.com)
  • 2003 As opposed to PTB domains SH2 domains recognize an important phosphotyrosine and adjacent C-terminal residues. (researchensemble.com)
  • PF cells were found to express regulatory (p85) and catalytic (p110α and p110β) subunits of phosphatidylinositol 3′-kinase (PI3′-kinase). (jneurosci.org)
  • Hyaluronan-mediated CD44 interaction with RhoGEF and Rho kinase promotes Grb2-associated binder-1 phosphorylation and phosphatidylinositol 3-kinase signaling leading to cytokine (macrophage-colony stimulating factor) production and breast tumor progression. (uchicago.edu)
  • Signaling through the phosphatidylinositol 3′-kinase (PI3K) pathway is crucial for metabolic responses to insulin, and defects in PI3K signaling have been demonstrated in type 2 diabetes. (diabetesjournals.org)
  • 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)
  • Phosphatidylinositol 3′-kinase (PI3K) is a crucial signaling enzyme whose activity is regulated by a variety of biological stimuli, including insulin ( 1 ). (diabetesjournals.org)
  • Activated PI3K phosphorylates the 3′-position of the ring in inositol phospholipids, generating phosphatidylinositol ( 3 , 4 ), diphosphate, and phosphatidylinositol (3,4,5)-triphosphate (PIP3). (diabetesjournals.org)
  • 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)
  • It possesses an amino N-terminal Src-homology 3 domain (SH3) domain, followed by a proline-rich domain (PRR) and a substrate domain (SD). (wikipedia.org)
  • Kinetics of Src homology 3 domain association with the proline-rich domain of dynamins: specificity, occlusion, and the effects of phosphorylation. (uchicago.edu)
  • The SH3 domains associate with proline rich motifs on the guanine nucleotide releasing factor, Sos, stimulating GTP binding to Ras, which in turn activates MAPK and other signaling pathways. (rndsystems.com)
  • The protein phosphorylation-driven conformational change of p47(phox) enables its PX domain to bind to phosphoinositides, the interaction of which plays a crucial role in recruitment of p47(phox) from the cytoplasm to membranes and subsequent activation of the phagocyte oxidase. (embl.de)
  • It is known to act through protein phosphorylation via PRKA and through the activation of guanine nucleotide exchange factors like EPAC. (plos.org)
  • c-Src tyrosine kinase consists of the N-terminal unique region, the Src homology 3 (SH3), SH2, linker, kinase domain, and the regulatory C-terminal tail. (intechopen.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)
  • Altered membrane events induced selective inhibition of TCR-induced phosphorylation of regulatory P85 subunit of PI3K and AKT as well as abrogated calcium influx. (nature.com)
  • 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)
  • Functional diversity between PTPases is endowed by regulatory domains and subunits. (embl.de)
  • After establishing the sites phosphorylated by PDGFRβ, they show in vitro that the PDGFRβ-mediated phosphorylation activates the Abl2 kinase activity. (yale.edu)
  • 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)
  • 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)
  • This review comprehends literatures on leptin and leptin resistance and especially discusses what STAT3 phosphorylation would contribute to central leptin resistance. (biomedcentral.com)
  • Emerging evidence provided insight into the role of signal transducer and activator of transcription 3 (STAT3) in energy metabolism. (biomedcentral.com)
  • Signal transducer and activator of transcription 3 (STAT3) was initially showed to control acute-phase genes in response to interleukin-6 (IL-6) and epidermal growth factor (EGF) during inflammatory processes (1). (abwizbio.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)
  • mutated JAK2s also mediate GH activation of transmission transducer and activator of transcription 3 (Stat3), transmission transducer and activator of transcription 5b (Stat5b) and ERK1, but at reduced levels. (biobender.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)
  • 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)
  • Additionally, p130Cas/BCAR1 tyrosine phosphorylation on its substrate domain can be induced by cell stretching subsequent to changes in the rigidity of the extracellular matrix, allowing cells to respond to mechanical force changes in the cell environment. (wikipedia.org)
  • Following the substrate domain is the serine-rich domain, which forms a four-helix bundle. (wikipedia.org)
  • p130Cas/BCAR1 can undergo extensive changes in tyrosine phosphorylation that occur predominantly in the 15 YxxP repeats within the substrate domain and represent the major post-translational modification of p130Cas/BCAR1. (wikipedia.org)
  • Mutational analysis revealed that only the C1 and DH domains are essential for Vav3 GEF activity with the C1 region being involved in binding with the GTPase substrate. (cytoskeleton.com)
  • The lipid products of PI3K initiate phosphorylation and activation of Akt, which is believed to act as a downstream mediator of many of the metabolic effects of insulin ( 5 , 6 ). (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)
  • PTEN also has phosphoinositide 3′-phosphatase activity and is therefore capable of suppressing PI3K signaling by dephosphorylating PIP3 ( 11 , 12 ). (diabetesjournals.org)
  • Here we show for the first time by genome-wide two-hybrid screens and in vitro binding assays that the PX domain is a bona fide protein interaction domain. (embl.de)
  • RESULTS: N3SP uptake stimulated NHE3 activity at nmol/L concentrations under basal conditions and partially reversed the reduced NHE3 activity caused by elevated adenosine 3',5'-cyclic monophosphate, guanosine 3',5'-cyclic monophosphate, and Ca2+ in cell lines and in in vitro mouse intestine. (bvsalud.org)
  • Due to the capacity of p130Cas/BCAR1, as an adaptor protein, to interact with multiple partners and to be regulated by phosphorylation and dephosphorylation, its expression and phosphorylation can lead to a wide range of functional consequences. (wikipedia.org)
  • RTK-dependent p130Cas/BCAR1 tyrosine phosphorylation and the subsequent binding with specific downstream signaling molecule modulate cell processes such as actin cytoskeleton remodeling, cell adhesion, proliferation, migration, invasion and survival. (wikipedia.org)
  • Integrin-mediated p130Cas/BCAR1 phosphorylation upon adhesion to extracellular matrix (ECM) induces downstream signaling that is required for allowing cells to spread and migrate on the ECM. (wikipedia.org)
  • Both RTKs and integrin activation affect p130Cas/BCAR1 tyrosine phosphorylation and represent an efficient means by which cells utilize signals coming from growth factors and integrin activation to coordinate cell responses. (wikipedia.org)
  • p130Cas/BCAR1 is a scaffold protein characterized by several structural domains. (wikipedia.org)
  • p130Cas/BCAR1 tyrosine phosphorylation can result from a diverse range of extracellular stimuli, including growth factors, integrin activation, vasoactive hormones and peptides ligands for G-protein coupled receptors. (wikipedia.org)
  • These stimuli triggers p130Cas/BCAR1 tyrosine phosphorylation and its translocation from cytosol to the cell membrane. (wikipedia.org)
  • AND-34/BCAR3 (Breast Cancer Anti-Estrogen Resistance 3) associates with the focal adhesion adaptor protein, p130CAS/BCAR1. (molvis.org)
  • Basal levels of p130Cas phosphorylation were higher in AND-34 +/+ than in AND-34 −/− lens epithelium. (molvis.org)
  • 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)
  • Regions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligands. (uchicago.edu)
  • Tyrosine phosphorylation of GRB2 SH3 domains reduces binding to Sos and negatively regulates downstream signaling pathways including Ras, JNK and MAPK. (rndsystems.com)
  • Our research demonstrated that genipin suppresses STAT-3 phosphorylation and nuclear translocation, which may be attributed to the binding capacity of this compound to the Src homology-2 (SH2) domain of STAT-3. (biomedcentral.com)
  • Moreover, the ability of IL-10 to induce de novo synthesis of SOCS-3 in monocytes correlates with its ability to inhibit expression of many genes in these cells, including endotoxin-inducible cytokines such as tumor necrosis factor-alpha (TNF-alpha) and IL-1. (nih.gov)
  • Lasp1 (LIM and SH3 domain protein 1) promotes tumor proliferation and invasion in multiple cancer entities including non-small cell lung cancer (NSCLC). (oncotarget.com)
  • In conclusion, Lasp1 facilitated tumor proliferation and invasion of NSCLC through directly binding to FAK and enhancing the phosphorylation of FAK (Tyr397) and AKT (Ser473). (oncotarget.com)
  • The tensin family member cten (C-terminal tensin like) is an Src homology 2 (SH2) and phosphotyrosine binding domain-containing focal adhesion molecule that may function as a tumor suppressor. (rupress.org)
  • These results provide a novel mechanism whereby the SH2 domain of cten-mediated focal adhesion localization of DLC-1 plays an essential role in its tumor suppression activity. (rupress.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)
  • Inhibition of PTEN expression also dramatically reduced insulin concentrations in ob/ob mice, improved the performance of db/db mice during insulin tolerance tests, and increased Akt phosphorylation in liver in response to insulin. (diabetesjournals.org)
  • Non-activated Abl2 are kept inactive through an autoinhibitory mechanism involving intramolecular interactions with the Src homology 3 (SH3) and Src homology 2 (SH2) domains, but it has been proposed that interactions with cellular binding partners relieve the inhibition. (yale.edu)
  • Interestingly, inhibition of FAK signaling pathway attenuated the phosphorylation of AKT, but inhibition of AKT signaling pathway did not affect the phosphorylation of FAK. (oncotarget.com)
  • The purified enzyme is capable of utilising Ptdlns, PtdIns(4)P and PtdIns(4,5)P2 as substrates, the ratios of phosphorylation of these three lipids were similar with substrates presented as pure sonicated phospholipids. (ucl.ac.uk)
  • The power of the thiol proteinases to cleave a multitude of substrates in response to calcium mineral activation allows their involvement in a variety of cell processes offering cell motility, sign transduction, apoptosis, cell differentiation and legislation of the cytoskeleton (3). (exposed-skin-care.net)
  • Based on the amino acid sequence homology and biological activity in macrophages, Shimamoto et al ( 15 ) identified that HLP was identical to MSP ( 15 ). (spandidos-publications.com)
  • The aim of this study was to investigate the diversity of cagA 3′ variable region and the amino acid polymorphisms in the EPIYA segments of the CagA C-terminal region of H. pylori , and their association with gastroduodenal diseases. (biomedcentral.com)
  • It plays a key role during sperm capacitation [ 3 - 6 ] and the acrosomal exocytosis [ 7 - 10 ], where it affects different intracellular signalling pathways. (plos.org)
  • 2007 The SH2 domain of cten interacts with phosphotyrosine-containing protein. (researchensemble.com)
  • Phosphatidylinosilol 3-kinase (Ptdlns 3-kinase) activity is circumstantially correlated with mitogenic responses and transformation, however little is known about the enzyme. (ucl.ac.uk)
  • They then mutate the phosphorylation sites from tyrosines (one of the most common amino acids to be phosphorylated) to phenylalanine in order to prevent these phosphorylation events. (yale.edu)
  • Based on these results and the crystal structure of the JAK2 kinase domain name, we hypothesize that small changes in the conformation of the regions of JAK2 surrounding tyrosines 868, 966, and 972 due to kinase assay. (biobender.com)
  • Constructs were produced encoding JAK2 with each of the 15 tyrosines in the kinase domain name of JAK2 individually mutated to phenylalanine. (biobender.com)
  • however, due to the lack of full protein structural information, the mechanistic insight of p47phox phosphorylation in NADPH oxidase activation remains incomplete. (reading.ac.uk)
  • Activation of Src in human cancers employs a variety of mechanisms mainly including covalent modification, allosteric regulation, gene mutation. (xcessbio.com)
  • In addition ot Tyr705 phosphorylation, Ser727 is required for maximal activation although Tyr705 phopsohrylation plays a key activating role (7,8). (abwizbio.com)
  • The particularly phosphorylated tyrosine enables docking and following activation of some responding molecules filled with Src homology 2 or SH2 domains [33]. (thetechnoant.info)
  • Ser-379 phosphorylation disrupts H-bonds that link the C-terminal tail to the autoinhibitory region (AIR) and the tandem Src homology 3 (SH3) domains, allowing the AIR to undergo phosphorylation to expose the SH3 pocket for p22phox binding. (reading.ac.uk)
  • Both Crk II and CrkL are composed of a single SH2 domain, followed by two tandem SH3 domains. (ecmbio.com)
  • The inactive domains of tandem phosphatases can be divided into two classes. (embl.de)
  • recently found a highly selective small-molecule degrader of STAT-3, i.e. (biomedcentral.com)
  • Phosphorylation of p47(phox), a cytoplasmic activator of the microbicidal phagocyte oxidase (phox), elicits interaction of p47(phox) with phoinositides. (embl.de)
  • The phox homology (PX) domain protein interaction network in yeast. (embl.de)
  • A mutation in the lipid-binding pocket of Ypt35p that reduces lipid binding markedly does not affect these PX domain protein interactions, arguing that lipid binding uses a different interaction surface than protein binding. (embl.de)
  • Unexpectedly, the interaction between DLC-1 and the cten SH2 domain is independent of tyrosine phosphorylation of DLC-1. (rupress.org)
  • Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190. (embl-heidelberg.de)
  • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. (embl.de)
  • We identified SLAP2 and ABL2 as potent interaction partners of FLT3 through their SH2 domain. (lu.se)
  • Together with research on PTB domains of tensin1 and tensin2 it really is believed the fact that relationship of integrin β tails with PTB domains of cten and various other tensins is indie of tyrosine phosphorylation (Chen and Lo 2003 Calderwood Temocapril et al. (researchensemble.com)
  • Thus, the ability of IL-10 to inhibit gene expression in monocytes is associated with its ability to rapidly induce synthesis of SOCS-3. (nih.gov)
  • 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)
  • You can find over 440 noted mutations within the calpain 3 gene up to now, included in this 212 (50%) are missense mutations, a lot of which alter its catalytic activity (22). (exposed-skin-care.net)
  • The epithelial brush border sodium (Na+)/hydrogen (H+) exchanger 3 (NHE3) accounts for a major component of intestinal Na+ absorption and is inhibited in most diarrheas. (bvsalud.org)
  • HGF was cloned as a growth factor for hepatocytes ( 1 , 2 ), is identical to scatter factor (SF) and was originally discovered as a fibroblast-derived cell motility factor for epithelial cells ( 3 ). (spandidos-publications.com)
  • While Akt Ser 473 phosphorylation was readily detectable in AND-34 +/+ lens epithelial cells, it was markedly reduced in the AND-34 −/− lens epithelium. (molvis.org)
  • Direct Phosphorylation of SRC Homology 3 Domains by Tyrosine Kinase Receptors Disassembles Ligand-Induced Signaling Networks Molecular Cell , vol. 70 , nº 6. (inrs.ca)
  • Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1. (umbc.edu)
  • The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. (embl.de)
  • catalytic (c) domain (repeat 2). (umbc.edu)
  • 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 phox homology (PX) domain is a phosphoinositide-binding domain that is conserved from yeast to human. (embl.de)
  • The enzyme is activated by the second messenger PIP3 produced by PI′-3-kinase. (justia.com)
  • Thirty years earlier, however, the noted physiologist Hans Selye put forth the theory that adrenal GCs can enhance and mediate the cellular stress response ( 1 , 2 , 3 , 4 , 5 ). (aai.org)
  • Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. (embl.de)
  • Using a combination of in silico phosphorylation, molecular dynamics simulation and protein/protein docking, we discovered that the C-terminal tail of p47phox is critical for stabilizing its autoinhibited structure. (reading.ac.uk)
  • Ser-379 phosphorylation is a molecular switch which initiates p47phox conformational changes and NADPH oxidase-dependent superoxide production by cells. (reading.ac.uk)
  • Abundant evidence has indicated that STAT-3 may be a promising molecular target for cancer treatment. (biomedcentral.com)
  • Inhibiting of STAT-3 activity can be divided into two categories: regulating upstream genes of STAT-3 or directly binding to STAT-3 and suppressing its activity [ 7 ]. (biomedcentral.com)
  • One of these genes, SOCS-3 (Suppressor of Cytokine Signaling-3) is a member of a newly identified family of genes that inhibit JAK/STAT-dependent signaling. (nih.gov)
  • The N-terminal cytoplasmic domain of Yip1p and Yif1p mediates these interactions with PX domains. (embl.de)
  • The cytoplasmic region generally contains two copies of the PTPase domain. (embl.de)
  • B) Cten appearance is certainly induced by many growth elements and cytokines (shown in vibrant) through Ras-Mek-MAPK … Framework Human cten is certainly a 715-residue polypeptide which includes two conserved domains: the SH2 area and PTB area (Lo and Lo 2002 1 Both had been originally defined as binding modules for phosphotyrosine-containing peptides. (researchensemble.com)
  • As the main component, extracellular structure contains some cysteine-rich repeats domains marked as D1-D2-D3 in GFRα1-3, and D2-D3 in GFRα4 ( Figure 1 a ). (medsci.org)