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Journal articles on the topic "SH2 domain family"
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Panchamoorthy, G., T. Fukazawa, L. Stolz, G. Payne, K. Reedquist, S. Shoelson, Z. Songyang, L. Cantley, C. Walsh, and H. Band. "Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn." Molecular and Cellular Biology 14, no. 9 (September 1994): 6372–85. http://dx.doi.org/10.1128/mcb.14.9.6372-6385.1994.
Full textAbstract:
The Src family protein tyrosine kinases participate in signalling through cell surface receptors that lack intrinsic tyrosine kinase domains. All nine members of this family possess adjacent Src homology (SH2 and SH3) domains, both of which are essential for repression of the enzymatic activity. The repression is mediated by binding between the SH2 domain and a C-terminal phosphotyrosine, and the SH3 domain is required for this interaction. However, the biochemical basis of functional SH2-SH3 interaction is unclear. Here, we demonstrate that when the SH2 and SH3 domains of p59fyn (Fyn) were present as adjacent domains in a single protein, binding of phosphotyrosyl peptides and proteins to the SH2 domain was enhanced, whereas binding of a subset of cellular polypeptide ligands to the SH3 domain was decreased. An interdomain communication was further revealed by occupancy with domain-specific peptide ligands: occupancy of the SH3 domain with a proline-rich peptide enhanced phosphotyrosine binding to the linked SH2 domain, and occupancy of the SH2 domain with phosphotyrosyl peptides enhanced binding of certain SH3-specific cellular polypeptides. Second, we demonstrate a direct binding between purified SH2 and SH3 domains of Fyn and Lck Src family kinases. Heterologous binding between SH2 and SH3 domains of closely related members of the Src family, namely, Fyn, Lck, and Src, was also observed. In contrast, Grb2, Crk, Abl, p85 phosphatidylinositol 3-kinase, and GTPase-activating protein SH2 domains showed lower or no binding to Fyn or Lck SH3 domains. SH2-SH3 binding did not require an intact phosphotyrosine binding pocket on the SH2 domain; however, perturbations of the SH2 domain induced by specific high-affinity phosphotyrosyl peptide binding abrogated binding of the SH3 domain. SH3-SH2 binding was observed in the presence of proline-rich peptides or when a point mutation (W119K) was introduced in the putative ligand-binding pouch of the Fyn SH3 domain, although these treatments completely abolished the binding to p85 phosphatidylinositol 3-kinase and other SH3-specific polypeptides. These biochemical SH2-SH3 interactions suggest novel mechanisms of regulating the enzymatic activity of Src kinases and their interactions with other proteins.
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Panchamoorthy, G., T. Fukazawa, L. Stolz, G. Payne, K. Reedquist, S. Shoelson, Z. Songyang, L. Cantley, C. Walsh, and H. Band. "Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn." Molecular and Cellular Biology 14, no. 9 (September 1994): 6372–85. http://dx.doi.org/10.1128/mcb.14.9.6372.
Full textAbstract:
The Src family protein tyrosine kinases participate in signalling through cell surface receptors that lack intrinsic tyrosine kinase domains. All nine members of this family possess adjacent Src homology (SH2 and SH3) domains, both of which are essential for repression of the enzymatic activity. The repression is mediated by binding between the SH2 domain and a C-terminal phosphotyrosine, and the SH3 domain is required for this interaction. However, the biochemical basis of functional SH2-SH3 interaction is unclear. Here, we demonstrate that when the SH2 and SH3 domains of p59fyn (Fyn) were present as adjacent domains in a single protein, binding of phosphotyrosyl peptides and proteins to the SH2 domain was enhanced, whereas binding of a subset of cellular polypeptide ligands to the SH3 domain was decreased. An interdomain communication was further revealed by occupancy with domain-specific peptide ligands: occupancy of the SH3 domain with a proline-rich peptide enhanced phosphotyrosine binding to the linked SH2 domain, and occupancy of the SH2 domain with phosphotyrosyl peptides enhanced binding of certain SH3-specific cellular polypeptides. Second, we demonstrate a direct binding between purified SH2 and SH3 domains of Fyn and Lck Src family kinases. Heterologous binding between SH2 and SH3 domains of closely related members of the Src family, namely, Fyn, Lck, and Src, was also observed. In contrast, Grb2, Crk, Abl, p85 phosphatidylinositol 3-kinase, and GTPase-activating protein SH2 domains showed lower or no binding to Fyn or Lck SH3 domains. SH2-SH3 binding did not require an intact phosphotyrosine binding pocket on the SH2 domain; however, perturbations of the SH2 domain induced by specific high-affinity phosphotyrosyl peptide binding abrogated binding of the SH3 domain. SH3-SH2 binding was observed in the presence of proline-rich peptides or when a point mutation (W119K) was introduced in the putative ligand-binding pouch of the Fyn SH3 domain, although these treatments completely abolished the binding to p85 phosphatidylinositol 3-kinase and other SH3-specific polypeptides. These biochemical SH2-SH3 interactions suggest novel mechanisms of regulating the enzymatic activity of Src kinases and their interactions with other proteins.
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Richard, S., D. Yu, K. J. Blumer, D. Hausladen, M. W. Olszowy, P. A. Connelly, and A. S. Shaw. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1." Molecular and Cellular Biology 15, no. 1 (January 1995): 186–97. http://dx.doi.org/10.1128/mcb.15.1.186.
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src family tyrosine kinases contain two noncatalytic domains termed src homology 3 (SH3) and SH2 domains. Although several other signal transduction molecules also contain tandemly occurring SH3 and SH2 domains, the function of these closely spaced domains is not well understood. To identify the role of the SH3 domains of src family tyrosine kinases, we sought to identify proteins that interacted with this domain. By using the yeast two-hybrid system, we identified p62, a tyrosine-phosphorylated protein that associates with p21ras GTPase-activating protein, as a src family kinase SH3-domain-binding protein. Reconstitution of complexes containing p62 and the src family kinase p59fyn in HeLa cells demonstrated that complex formation resulted in tyrosine phosphorylation of p62 and was mediated by both the SH3 and SH2 domains of p59fyn. The phosphorylation of p62 by p59fyn required an intact SH3 domain, demonstrating that one function of the src family kinase SH3 domains is to bind and present certain substrates to the kinase. As p62 contains at least five SH3-domain-binding motifs and multiple tyrosine phosphorylation sites, p62 may interact with other signalling molecules via SH3 and SH2 domain interactions. Here we show that the SH3 and/or SH2 domains of the signalling proteins Grb2 and phospholipase C gamma-1 can interact with p62 both in vitro and in vivo. Thus, we propose that one function of the tandemly occurring SH3 and SH2 domains of src family kinases is to bind p62, a multifunctional SH3 and SH2 domain adapter protein, linking src family kinases to downstream effector and regulatory molecules.
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Dumas, Caroline, Anna Schmoker, Shannon Bennett, Amara Chittenden, Chelsea Darwin, Helena Gaffney, Hannah Lewis, et al. "Novel Interactors of the SH2 Domain of the Signaling Adaptors CRK and CRKL Identified in Neuro2A Cells." American Journal of Undergraduate Research 19, no. 3 (December 31, 2022): 47–55. http://dx.doi.org/10.33697/ajur.2022.068.
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CT10 regulator of kinase (CRK) and CRK-like (CRKL) form a family of signaling adaptor proteins that serve important roles in the regulation of fundamental cellular processes, including cell motility and proliferation, in a variety of cell types. The Src Homology 2 (SH2) domain of CRK and CRKL interacts with proteins containing phosphorylated tyrosine-X-X-proline (pYXXP) motifs, facilitating complex formation during signaling events. A handful of CRK/CRKL-SH2-specific interactors have been identified to date, although in silico analyses suggest that many additional interactors remain to be found. To identify CRK/CRKL-SH2 interactors with potential involvement in neuronal development, we conducted a mass spectrometry-based proteomics screen using a neuronal cell line (Neuro2A, or N2A). This resulted in the identification of 132 (6 known and 126 novel) YXXP-containing CRK/CRKL-SH2 interactors, of which 77 were stimulated to bind to the CRK/CRKL-SH2 domain following tyrosine phosphatase inhibition. Approximately half of the proteins identified were common interactors of both the CRK- and CRKL-SH2 domains. However, both CRK family member SH2 domains exhibited unique binding partners across experimental replicates. These findings reveal an abundance of novel neuronal CRK/CRKL-SH2 domain binding partners and suggest that CRK family SH2 domains possess undescribed docking preferences beyond the canonical pYXXP motif. KEYWORDS: CRK; CRKL; SH2; LC-MS/MS; Proteomics; Neurodevelopment; Signal Transduction
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Li, Minghua, Zhiqin Li, David L. Morris, and Liangyou Rui. "Identification of SH2B2β as an Inhibitor for SH2B1- and SH2B2α-Promoted Janus Kinase-2 Activation and Insulin Signaling." Endocrinology 148, no. 4 (April 1, 2007): 1615–21. http://dx.doi.org/10.1210/en.2006-1010.
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The SH2B family has three members (SH2B1, SH2B2, and SH2B3) that contain conserved dimerization (DD), pleckstrin homology, and SH2 domains. The DD domain mediates the formation of homo- and heterodimers between members of the SH2B family. The SH2 domain of SH2B1 (previously named SH2-B) or SH2B2 (previously named APS) binds to phosphorylated tyrosines in a variety of tyrosine kinases, including Janus kinase-2 (JAK2) and the insulin receptor, thereby promoting the activation of JAK2 or the insulin receptor, respectively. JAK2 binds to various members of the cytokine receptor family, including receptors for GH and leptin, to mediate cytokine responses. In mice, SH2B1 regulates energy and glucose homeostasis by enhancing leptin and insulin sensitivity. In this work, we identify SH2B2β as a new isoform of SH2B2 (designated as SH2B2α) derived from the SH2B2 gene by alternative mRNA splicing. SH2B2β has a DD and pleckstrin homology domain but lacks a SH2 domain. SH2B2β bound to both SH2B1 and SH2B2α, as demonstrated by both the interaction of glutathione S-transferase-SH2B2β fusion protein with SH2B1 or SH2B2α in vitro and coimmunoprecipitation of SH2B2β with SH2B1 or SH2B2α in intact cells. SH2B2β markedly attenuated the ability of SH2B1 to promote JAK2 activation and subsequent tyrosine phosphorylation of insulin receptor substrate-1 by JAK2. SH2B2β also significantly inhibited SH2B1- or SH2B2α-promoted insulin signaling, including insulin-stimulated tyrosine phosphorylation of insulin receptor substrate-1. These data suggest that SH2B2β is an endogenous inhibitor of SH2B1 and/or SH2B2α, negatively regulating insulin signaling and/or JAK2-mediated cellular responses.
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Songyang, Z., S. E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X. R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, and T. Yi. "Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav." Molecular and Cellular Biology 14, no. 4 (April 1994): 2777–85. http://dx.doi.org/10.1128/mcb.14.4.2777-2785.1994.
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Src homology 2 (SH2) domains provide specificity to intracellular signaling by binding to specific phosphotyrosine (phospho-Tyr)-containing sequences. We recently developed a technique using a degenerate phosphopeptide library to predict the specificity of individual SH2 domains (src family members, Abl, Nck, Sem5, phospholipase C-gamma, p85 subunit of phosphatidylinositol-3-kinase, and SHPTP2 (Z. Songyang, S. E. Shoelson, M. Chaudhuri, G. Gish, T. Pawson, W. G. Haser, F. King, T. Roberts, S. Ratnofsky, R. J. Lechleider, B. G. Neel, R. B. Birge, J. E. Fajardo, M. M. Chou, H. Hanafusa, B. Schaffhausen, and L. C. Cantley, Cell 72:767-778, 1993). We report here the optimal recognition motifs for SH2 domains from GRB-2, Drk, Csk, Vav, fps/fes, SHC, Syk (carboxy-terminal SH2), 3BP2, and HCP (amino-terminal SH2 domain, also called PTP1C and SHPTP1). As predicted, SH2 domains from proteins that fall into group I on the basis of a Phe or Tyr at the beta D5 position (GRB-2, 3BP2, Csk, fps/fes, Syk C-terminal SH2) select phosphopeptides with the general motif phospho-Tyr-hydrophilic (residue)-hydrophilic (residue)-hydrophobic (residue). The SH2 domains of SHC and HCP (group III proteins with Ile, Leu, of Cys at the beta D5 position) selected the general motif phospho-Tyr-hydrophobic-Xxx-hydrophobic, also as predicted. Vav, which has a Thr at the beta D5 position, selected phospho-Tyr-Met-Glu-Pro as the optimal motif. Each SH2 domain selected a unique optimal motif distinct from motifs previously determined for other SH2 domains. These motifs are used to predict potential sites in signaling proteins for interaction with specific SH2 domain-containing proteins. The Syk SH2 domain is predicted to bind to Tyr-hydrophilic-hydrophilic-Leu/Ile motifs like those repeated at 10-residue intervals in T- and B-cell receptor-associated proteins. SHC is predicted to bind to a subgroup og these same motifs. A structural basis for the association of Csk with Src family members is also suggested from these studies.
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Songyang, Z., S. E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X. R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, and T. Yi. "Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav." Molecular and Cellular Biology 14, no. 4 (April 1994): 2777–85. http://dx.doi.org/10.1128/mcb.14.4.2777.
Full textAbstract:
Src homology 2 (SH2) domains provide specificity to intracellular signaling by binding to specific phosphotyrosine (phospho-Tyr)-containing sequences. We recently developed a technique using a degenerate phosphopeptide library to predict the specificity of individual SH2 domains (src family members, Abl, Nck, Sem5, phospholipase C-gamma, p85 subunit of phosphatidylinositol-3-kinase, and SHPTP2 (Z. Songyang, S. E. Shoelson, M. Chaudhuri, G. Gish, T. Pawson, W. G. Haser, F. King, T. Roberts, S. Ratnofsky, R. J. Lechleider, B. G. Neel, R. B. Birge, J. E. Fajardo, M. M. Chou, H. Hanafusa, B. Schaffhausen, and L. C. Cantley, Cell 72:767-778, 1993). We report here the optimal recognition motifs for SH2 domains from GRB-2, Drk, Csk, Vav, fps/fes, SHC, Syk (carboxy-terminal SH2), 3BP2, and HCP (amino-terminal SH2 domain, also called PTP1C and SHPTP1). As predicted, SH2 domains from proteins that fall into group I on the basis of a Phe or Tyr at the beta D5 position (GRB-2, 3BP2, Csk, fps/fes, Syk C-terminal SH2) select phosphopeptides with the general motif phospho-Tyr-hydrophilic (residue)-hydrophilic (residue)-hydrophobic (residue). The SH2 domains of SHC and HCP (group III proteins with Ile, Leu, of Cys at the beta D5 position) selected the general motif phospho-Tyr-hydrophobic-Xxx-hydrophobic, also as predicted. Vav, which has a Thr at the beta D5 position, selected phospho-Tyr-Met-Glu-Pro as the optimal motif. Each SH2 domain selected a unique optimal motif distinct from motifs previously determined for other SH2 domains. These motifs are used to predict potential sites in signaling proteins for interaction with specific SH2 domain-containing proteins. The Syk SH2 domain is predicted to bind to Tyr-hydrophilic-hydrophilic-Leu/Ile motifs like those repeated at 10-residue intervals in T- and B-cell receptor-associated proteins. SHC is predicted to bind to a subgroup og these same motifs. A structural basis for the association of Csk with Src family members is also suggested from these studies.
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Mayer, B. J., and D. Baltimore. "Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase." Molecular and Cellular Biology 14, no. 5 (May 1994): 2883–94. http://dx.doi.org/10.1128/mcb.14.5.2883-2894.1994.
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We have used in vitro mutagenesis to examine in detail the roles of two modular protein domains, SH2 and SH3, in the regulation of the Abl tyrosine kinase. As previously shown, the SH3 domain suppresses an intrinsic transforming activity of the normally nontransforming c-Abl product in vivo. We show here that this inhibitory activity is extremely position sensitive, because mutants in which the position of the SH3 domain within the protein is subtly altered are fully transforming. In contrast to the case in vivo, the SH3 domain has no effect on the in vitro kinase activity of the purified protein. These results are consistent with a model in which the SH3 domain binds a cellular inhibitory factor, which in turn must physically interact with other parts of the kinase. Unlike the SH3 domain, the SH2 domain is required for transforming activity of activated Abl alleles. We demonstrate that SH2 domains from other proteins (Ras-GTPase-activating protein, Src, p85 phosphatidylinositol 3-kinase subunit, and Crk) can complement the absence of the Abl SH2 domain and that mutants with heterologous SH2 domains induce altered patterns of tyrosine-phosphorylated proteins in vivo. The positive function of the SH2 domain is relatively position independent, and the effect of multiple SH2 domains appears to be additive. These results suggest a novel mechanism for regulation of tyrosine kinases in which the SH2 domain binds to, and thereby enhances the phosphorylation of, a subset of proteins phosphorylated by the catalytic domain. Our data also suggest that the roles of the SH2 and SH3 domains in the regulation of Abl are different in several respects from the roles proposed for these domains in the closely related Src family of tyrosine kinases.
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Mayer, B. J., and D. Baltimore. "Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase." Molecular and Cellular Biology 14, no. 5 (May 1994): 2883–94. http://dx.doi.org/10.1128/mcb.14.5.2883.
Full textAbstract:
We have used in vitro mutagenesis to examine in detail the roles of two modular protein domains, SH2 and SH3, in the regulation of the Abl tyrosine kinase. As previously shown, the SH3 domain suppresses an intrinsic transforming activity of the normally nontransforming c-Abl product in vivo. We show here that this inhibitory activity is extremely position sensitive, because mutants in which the position of the SH3 domain within the protein is subtly altered are fully transforming. In contrast to the case in vivo, the SH3 domain has no effect on the in vitro kinase activity of the purified protein. These results are consistent with a model in which the SH3 domain binds a cellular inhibitory factor, which in turn must physically interact with other parts of the kinase. Unlike the SH3 domain, the SH2 domain is required for transforming activity of activated Abl alleles. We demonstrate that SH2 domains from other proteins (Ras-GTPase-activating protein, Src, p85 phosphatidylinositol 3-kinase subunit, and Crk) can complement the absence of the Abl SH2 domain and that mutants with heterologous SH2 domains induce altered patterns of tyrosine-phosphorylated proteins in vivo. The positive function of the SH2 domain is relatively position independent, and the effect of multiple SH2 domains appears to be additive. These results suggest a novel mechanism for regulation of tyrosine kinases in which the SH2 domain binds to, and thereby enhances the phosphorylation of, a subset of proteins phosphorylated by the catalytic domain. Our data also suggest that the roles of the SH2 and SH3 domains in the regulation of Abl are different in several respects from the roles proposed for these domains in the closely related Src family of tyrosine kinases.
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Margolis, Ben. "The GRB family of SH2 domain proteins." Progress in Biophysics and Molecular Biology 62, no. 3 (January 1994): 223–44. http://dx.doi.org/10.1016/0079-6107(94)90013-2.
Full textDissertations / Theses on the topic "SH2 domain family"
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Larson, Stefan M. "A comprehensive sequence alignment analysis and structure comparison of the SH3 domain family." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0002/MQ46094.pdf.
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Spiess, Matthias. "Evolution of the SH3 domain protein interaction networks in yeast : functions and interactions of the Lsb1 and Lsb2 protein family." Strasbourg, 2010. https://publication-theses.unistra.fr/public/theses_doctorat/2010/SPIESS_Matthias_2010.pdf.
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Chez S. Cerevisiae, les nutriments, les lipides et les protéines membranaires sont internalisés par endocytose. Ce processus requiert des filaments d’actine dynamiques. Un facteur clé pour la polymérisation de l’actine est le nucléateur Arp2/3, activé par des facteurs de promotion de la nucléation (NPF). Pendant l’endocytose, la polymérisation de l’actine est initiée, entre autre, par les NPFs Las17 et les myosines de type I. Nous avons caractérisé deux protéines, Lsb1 et Lsb2 qui lient Las17 par leurs domaines SH3 et qui inhibent in vitro la polymérisation de l’actine dépendante du complexe Arp2/3. Lsb1 et Lsb2 colocalisent avec des protéines du cytosquelette, Las17, Abp1 et Sla1 et influencent la stabilité de Las17 in vivo. Nous avons ainsi identifié deux nouveaux régulateurs négatifs de l’activité NPF de Las17 ce qui permet de mieux comprendre son rôle dans la polymérisation de l’actine et l’endocytose. Nous avons également caractérisé chez des levures S. Cerevisiae, A. Gossypii, C. Albicans et S. Pombe des réseaux d’interactions protéine-protéine à travers des spécificités de liaison des domaines SH3 par la technique SPOT. Une conservation de la spécificité des myosines de type I, connu par ailleurs, a été montrée par analyse bioinformatique et valide notre méthode. De plus, nous montrons que la fonction de la myosine I de recruter la machinerie de polymérisation dans un extrait de S. Cerevisiae est conservée de S. Cerevisiae à A. Gossypii. Nous faisons des analyses similaires pour de nombreuses autres protéines à domaine SH3 ce qui nous permettra de prédire des interactions protéines-protéines ainsi de mieux comprendre l’évolution des réseaux d’interaction protéiqueIn S. Cerevisiae, nutrients, lipids and membrane proteins are internalized by endocytosis. These processes require dynamic actin filament assembly. A key factor for actin polymerization is the nucleating complex Arp2/3 that is activated by nucleation promoting factors (NPF). During the process of endocytosis, a strong NPF activity is exhibited by Las17, the unique S. Cerevisiae homolog of WASP and the type I myosin, Myo5, among others. Here, we characterize two SH3 domain containing proteins Lsb1 and Lsb2. We could show that both proteins bind to the proline rich sequence of the NPF Las17 via their SH3 domains and efficiently inhibit Las17 induced Arp2/3-dependent actin polymerization in vitro. We could also show that Lsb1 and Lsb2 partially colocalize with Las17 and that they influence the stability of Las17 in vivo. However, we did not detect any defect in endocytosis for the single or double deletion mutants of LSB1 and LSB2. In conclusion, we identified two new negative regulators of the NPF activity of Las17 that will help us to further understand actin nucleation and endocytosis. The characterization of the SH3 domain binding specificity in four yeast species S. Cerevisiae, A. Gossypii, C. Albicans and S. Pombe showed high conservation of the type I myosin specificity during evolution, validating our method. The ability of type I myosin to recruit the actin polymerization machinery in S. Cerevisiae is conserved from S. Cerevisiae to A. Gossypii. Similar analysis of numerous other SH3 domains, including Lsb1 and Lsb2, is in progress, which will allow us to predict new protein-protein interactions and to gain insights into the evolution of protein interaction networks
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Picard, Christophe. "Régulations intramoléculaires et intermoléculaires des membres de la famille Src : implication des interactions du domaine SH3 avec l'interdomaine." Aix-Marseille 2, 2003. http://www.theses.fr/2003AIX20658.
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Les protéines Tyrosine kinase de la famille Src sont impliquées dans de nombreux processus physiologiques. Leur activité est régulée par des mécanismes qui modifient les contraintes moléculaires. Notre travail a apporté de nouvelles connaissances sur le rôle du domaine d'interaction SH3 et de l'interdomaine dans la régulation inter-et intra-moléculaire des protéines Src. Nous avons déterminé le mécanisme explicitant la spécificité d'interaction des protéines virales Nef pour le domaine SH3 de certaines protéines Src. De plus, nous avons validé un modèle d'étude de la pathogénie du SIDA. Enfin, l'analyse des deux isoformes de Fyn qui diffèrent par leur interdomaine nous a permis de mieux comprendre l'émergence du système immunitaire adaptatif et la fonction des interdomaines dans la sélection des substrats et dans la régulation intramoléculaire des protéines Src. Les conséquences potentielles morbides et thérapeutiques des anomalies de la réglation des protéines Src sont discutées.
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Arold, Stefan. "Etude structurale et thermodynamique de l'interaction de la protéine Nef des virus d'immunodéficience avec les domaines SH3 de protéine-tyrosine kinases de la famille Src." Montpellier 1, 1998. http://www.theses.fr/1998MON13510.
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Wang, Chung-Kang, and 王仲康. "Functional characterization of Derlin family member: The importance of SHP box and C-terminal α-domain." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/kc5633.
Full textBooks on the topic "SH2 domain family"
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Lambert, Véronique. The Adornes Domain and the Jerusalem Chapel in Bruges. Translated by Ian Connerty. NL Amsterdam: Amsterdam University Press, 2018. http://dx.doi.org/10.5117/9789462989924.
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Bruges, middle of the 15th century. Anselm Adornes, scion of a rich patrician family, creates a magnificent domain in the heart of the city : an elegant mansion, beautiful gardens, several charitable almshouses and the spectacular Chapel of Jerusalem. It is a place that every right-minded resident of Bruges and every tourist must see. The history of the Adornes domain is truly remarkable, remaining in the unbroken possession of the same family for six centuries. It has survived storms and setbacks, the secularism of the French Revolution, the fury of two world wars and inevitable periods of disinterest. 'In this book Véronique Lambert allows us to share in the hopes and fears, joys and sorrows, trials and tribulations that mark the milestones in the Adornes family saga. Within the boundaries of historical interpretation and based on extensive research, she unfolds a fascinating tale of ambitious adventurers, charismatic personalities, flamboyant lords and ordinary mortals, but each imbued with the family's traditional willpower and energy'. Let yourself be enchanted by this fascinating piece of our cultural heritage, which deserves to be more widely known.
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Larson, Stefan M. A comprehensive sequence alignment analysis and structure comparison of the SH3 domain family. Ottawa: National Library of Canada, 1999.
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Doubleday, Veronica. Zainab Herawi. University of Illinois Press, 2017. http://dx.doi.org/10.5406/illinois/9780252037245.003.0011.
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This chapter deals with the life and career of Zainab Herawi. She began her singing career as a child apprentice in the Herat region of Afghanistan in the 1940s, within the context of a class-based society, where singing by women was considered to be morally questionable. Zainab's is a story of unfulfilled fame because, although she was invited to sing for Kabul Radio when twenty-seven, family and background pressures and constraints led to her returning home, where she continued to sing for wedding celebrations. As a series of choices and struggles involving the interfacing domains of family, location, religion, and vocality, her life as a local singer with a large family was one of frequent anguish and frustration; yet her songs live on in the narratives and performances of musician and scholar Veronica Doubleday.
Book chapters on the topic "SH2 domain family"
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Cicchetti, Piera, and David Baltimore. "[17] Identification of 3BP-1 in cDNA expression library by SH3 domain screening." In Small GTPases and Their Regulators Part B: Rho Family, 140–48. Elsevier, 1995. http://dx.doi.org/10.1016/0076-6879(95)56019-x.
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Aronson, Amy. "“Marriage under Two Roofs”: Feminism and Family Life." In Crystal Eastman, 243–68. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780199948734.003.0011.
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Crystal Eastman ardently pursued equalitarian feminism but also asserted that feminism must have three parts: politics and public policy; wages and the workplace; and—the distinctive final portion—the private domain of love, marriage, and the family. She believed millions of women like herself experienced acute feminist concerns not merely in the battle for economic opportunity in the workforce, or political representation and voice, but also from conflicts between their desire for the rewards of life beyond the home and for the rewards of family as well. She pursued this missing policy analysis for the rest of her life, advocating birth control in the feminist program, the endowment of motherhood, and feminist child-rearing and education. In unpublished articles, she also explored wages for wives and single motherhood by choice. All the while, Eastman was experimenting with a variety of novel approaches to integrating her feminism in own her marriage and family life.
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Ibrahim, Farhana. "Blood and Water." In From Family to Police Force, 117–37. Cornell University Press, 2021. http://dx.doi.org/10.7591/cornell/9781501759536.003.0005.
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This chapter advances with forms of policing that may be continuous across the domains of the state and family even though they may operate within different moral universes. Notwithstanding forms of bureaucratic rationality that are believed to structure practices of governmentality of which policing is a key component, the police rely on ways of seeing that often rely on intuitive assessments of who is inside or outside the law. Similarly, as the chapter emphasizes, an imbalance in the flow of information, suspicion, and trust in the family may threaten to destabilize the traditional order. Even as the “Bengali” wife is seen as a threatening outsider to the state, she may be a desired wife or daughter-in-law within the family, her lack of familiarity being her biggest appeal. The chapter then shifts to argue that traditional consanguineous marriages may at times jeopardize the delicate balance of information management. It stresses that the key fault lines are not necessarily between kin and nonkin or between “wife givers” and “wife takers,” the key categories through which much of South Asian kinship has been understood, but through the management of generational cohorts and the use of lateral surveillance therein. The availability of the “Bengali” wife who is an “outsider” allows the family to circumvent the crisis of intimate knowledge attendant on marrying within the family while also saving face by not marrying a different (possibly lesser) local Muslim caste.
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Easley, Alexis. "Frances Brown and the ‘Modern’ Market for Print." In New Media and the Rise of the Popular Woman Writer, 1832-1860, 171–200. Edinburgh University Press, 2021. http://dx.doi.org/10.3366/edinburgh/9781474475921.003.0006.
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In this chapter, I focus on a writer who got her start writing poetry and prose for the cheap popular press: Frances Brown. Like Cook, Brown was working class, but her impoverished upbringing as the daughter of a postmaster in a remote Ulster village placed her on a lower rung of the social ladder than Cook with fewer resources at her disposal. She lost her sight to smallpox when she was eighteen months old and learned about the world by listening to her siblings’ lessons and having family members read aloud to her. Once she began writing, her sister Rebecca served as her amanuensis. She began her career contributing poetry to the Irish Penny Journal, later published her work in the Penny Magazine, and developed an extensive career contributing poetry and prose to Chambers’s Edinburgh Journal. Her careful navigation of the market for popular literature reveals the importance of cheap media formats (with differing levels of copyright protection) in a fashioning a writing career. Even though Brown’s work was often repurposed by scissors-and-paste journalists as if it were free content within the public domain, she was successful in establishing a celebrity identity and publishing her work in book form.
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Lakshmivarahan, S., and Sudarshan K. Dhall. "Size vs. Depth Trade-Off In Parallel Prefix Circuits." In Parallel Computing Using the Prefix Problem. Oxford University Press, 1994. http://dx.doi.org/10.1093/oso/9780195088496.003.0013.
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Ladner-Fischer [1980] was the first one to demonstrate size vs. depth trade-off in parallel prefix circuits. In this Chapter, a lower bound from Snir [1986] on (size + depth) for prefix circuits is first derived. Several designs of parallel prefix circuits with optimal (size + depth) trade-offs are described. In this section, we derive a lower bound from Snir [1986] on the sum of depth and size of a class of prefix circuits. Let x = { x1, x2, • • • , XN }, be a set of N variables. Let D be the domain over which elements of x take their values, and let FN = { f1, f 2, . . . , fN } be a set of functions satisfying the following conditions: (SR1) fi, depends only on the variables x1, x2 , • • • xi, and (SR2) For each variable xi, i = 1, 2, • • • , N, there exist values ai, in D, such that, the set of functions fj |xi = ai = fj(x1,x2, . . . , xi-1, xi = ai, xi+1, . . . , xj), j=1,2, . . . , N, contains a family of (N - 1) functions satisfying these conditions. The family FN satisfying these two conditions is called a self reducible family of functions. Clearly, fi (x1, x2, . . . , xi) = x1 o x2 o . . . o xi, 1 ≤ i ≤ N, satisfies these conditions. Following is an example of a self-reducible family of functions. An associative binary operation θ is said to be non-trivial if the following conditions are satisfied: (i) Let z = x θ y. Then z depends on both x and y, that is, θ is not a projection, nor a constant operation, and (ii) There exists a (right) unit element e of θ, such that, x = x θ e.
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"Core surgical skills." In Tasks for Part 3 MRCOG Clinical Assessment, edited by Sambit Mukhopadhyay and Medha Sule. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780198757122.003.0011.
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This task assesses the following clinical skills: … ● Patient safety ● Communication with patients and their relatives ● Information gathering ● Applied clinical knowledge … Sarah Bener is a 28- year- old lady in her second pregnancy. She has had an elective caesarean section in her last pregnancy for a breech delivery two years ago. She has no other health problems and her pregnancy has progressed well so far. She is currently 36 weeks pregnant and has presented to the antenatal clinic to discuss the mode of delivery. You have 10 minutes for this task (+ 2mins initial reading time) Please read instructions to candidate and actor. This station assesses the candidate’s ability to come to a shared decision after discussing the pros and cons of both the options. Please do not interrupt or prompt. Record your overall clinical impression of the candidate for each domain (e.g. should this performance be pass, borderline or a fail). You are Sarah Bener, a 28- year- old house wife. You are 36 weeks pregnant. You are healthy and so far your pregnancy had progressed smoothly. You feel good baby movements. The screening test as well as the baby’s scan at 20 weeks has been normal. You have one child, Imogen, born by caesarean section two years ago. It was an elective caesarean section as Imogen was in breech position. They did try turning her (ECV), but was unsuccessful. You were very much looking forward to a normal delivery and were disappointed that you needed a caesarean section. The caesarean section was straightforward, without any complications. But you needed a few days to recover at home. You are keen to have a normal delivery this time, but want to know the options and risks of the mode of delivery. Both you and your husband have always wanted a large family, so want to know the implications of a second section. If the candidate does not mention VBAC, say that you have heard of this and can they explain more about it.
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"Puerperal problems." In Tasks for Part 3 MRCOG Clinical Assessment, edited by Sambit Mukhopadhyay and Medha Sule. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780198757122.003.0018.
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This task assesses the following clinical skills: … ● Patient safety ● Communication with patients and their relatives ● Information gathering ● Applied clinical knowledge … Anna Polanska, a 34- year- old woman, is ten days postpartum. Anna underwent induction of labour for reduced foetal movements and small for gestational age and had a ventouse delivery complicated by a third degree tear. She was discharged home, but her baby is on the neonatal unit. She has been referred by her GP as Anna is feeling very tearful over the last few days and is low in mood. She has not been sleeping well and has intrusive thoughts. You are the registrar on call on the delivery suite and have been asked to assess Anna. Your task is to: … ● Take an appropriate history ● Organize the immediate management … You have 10 minutes for this task (+ 2mins initial reading time). Please read instruction to candidate and role player. This clinical assessment task is to assess the communication skills of the candidates and assess their understanding of the factors predisposing to postnatal depression. It also assesses if the candidates are aware of the next steps of management in such a case. Record your overall clinical impression of the candidate for each domain (i.e. should this performance be pass, borderline, or a fail). For marking the impression on communication skills, please consult the role player. You are Anna Polanska, a 34- year- old, asylum seeker and have been in the UK for the last 18 months. You have no support from your ex- partner and do not have any family in the UK. You gave birth to your first child ten days ago. You booked late in this pregnancy as you were contemplating terminating the pregnancy but found out on your first scan that you were already 24 weeks pregnant and so decided to continue with the pregnancy. You were told your blood tests were normal at booking. Your community midwife has been on sick leave and you have no money to attend hospital visits. You have not attended a few of your antenatal clinic appointments. You smoke up to 20 cigarettes per day.
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Nunn, J. H., and G. Wright. "Childhood impairment and disability." In Paediatric Dentistry. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198789277.003.0026.
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An impairment becomes a disability for a child only if he/she is unable to carry out the normal activities of his/her peer group. For example, a child who has broken an arm is temporarily ‘disabled’ by not being able to eat and write in the normal way. However, impairment is a permanent feature in the lives of some children, although it may become a disability only if they are unable to take part in everyday activities, such as communicating with others, climbing stairs, and toothbrushing. A more contemporary view is one that moves away from the medicalization of impairment to a consideration of ability and functioning, enshrined in the World Health Organization’s International Classification of Functioning, Disability, and Impairment (ICF). In this definition, a number of domains are classified from body, individual, and societal perspectives. This approach is less stigmatizing and more enabling of children with impairments. There are a number of reasons why children with impairments merit special consideration for dental care. 1. The oral health of some children with disabilities is different from that of their healthy peers—for example, the greater prevalence of periodontal disease in people with Down syndrome and of tooth-wear in those with cerebral palsy. 2. The prevention of dental disease in disabled children needs to be a higher priority than for so-called normal peers because dental disease, its sequelae, or its treatment may be life-threatening—for example, the risk of infective endocarditis from oral organisms in children with significant congenital heart defects. 3. Treatment planning and the provision of dental care may need to be modified in view of the patient’s capabilities, likely future cooperation, and home care—for example, the feasibility of providing a resin-bonded bridge for a teenager with cerebral palsy, poorly controlled epilepsy, and inadequate home oral care. In the light of these considerations, do such children need special dental care? Most of the studies that have been undertaken on disabled children have indicated that the majority can in fact be treated in a dental surgery in the normal way, together with the rest of their family.
Conference papers on the topic "SH2 domain family"
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Shen, Kexin, Heather R. Dorman, Haibin Shi, Ravi K. Patel, Jamie A. Moroco, John R. Engen, and Thomas E. Smithgall. "Abstract 2377: The AML linked Src family kinase Fgr is uncoupled from SH2 and SH3 domain regulation and drives oncogenic transformation." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2377.
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Rust, Heather L., Jamie A. Moroco, John J. Alvarado, John J. Engen, and Thomas E. Smithgall. "Abstract B190: Allosteric modulation of Src family kinases via SH3 domain displacement." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; November 5-9, 2015; Boston, MA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1535-7163.targ-15-b190.
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