Výsledky vyhledávání - "Tyrosine-Protein Kinase (Tyrosine Kinase)"

Disturbances in PP2A methylation and one-carbon metabolism compromise Fyn distribution, neuritogenesis, and APP regulation

Autor: Jean-Marie Sontag, Goce Taleski, Diana Schuhmacher, Estelle Sontag, Henry Su

Publikováno v: The Journal of Biological Chemistry

The nonreceptor protein tyrosine kinase Fyn and protein Ser/Thr phosphatase 2A (PP2A) are major multifunctional signaling molecules. Deregulation of Fyn and altered PP2A methylation are implicated in cancer and Alzheimer's disease (AD). Here, we test

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68dc235bb9757b5a3d752f93788ff7e8
https://pubmed.ncbi.nlm.nih.gov/33380425

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A dock and coalesce mechanism driven by hydrophobic interactions governs Cdc42 binding with its effector protein ACK

Autor: Tetley, George J. N., Mott, Helen R., Cooley, R. Neil, Owen, Darerca

Publikováno v: The Journal of Biological Chemistry

Cdc42 is a Rho-family small G protein that has been widely studied for its role in controlling the actin cytoskeleton and plays a part in several potentially oncogenic signaling networks. Similar to most other small G proteins, Cdc42 binds to many do

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31521ae3b4bed12d3c3b80a8cc44b1e7
https://www.repository.cam.ac.uk/handle/1810/264658

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Syk and Src Family Kinases Regulate C-type Lectin Receptor 2 (CLEC-2)-mediated Clustering of Podoplanin and Platelet Adhesion to Lymphatic Endothelial Cells

Autor: Bernhard Nieswandt, Ying-Jie Wang, Steve P. Watson, Dylan M. Owen, Craig E. Hughes, Leyre Navarro-Núñez, David A. Jackson, Michael L. Dustin, Natalie S. Poulter, Eelo Gitz, Michael R. Douglas, Alice Y. Pollitt, Steven G. Thomas

Publikováno v: The Journal of Biological Chemistry

Background: The interaction of platelet CLEC-2 with Podoplanin is critical for development of the lymphatics. Results: CLEC-2 forms a central cluster upon engagement with Podoplanin, which clusters Podoplanin. Clustering is dependent on Syk and is cr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab8cb6bf2688a85fac3da1e893a80e28
https://doi.org/10.1074/jbc.m114.584284

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Interactions of STAP-2 with Brk and STAT3 Participate in Cell Growth of Human Breast Cancer Cells

Autor: Yuichi Sekine, Misa Nakasuji, Osamu Ikeda, Asuka Nanbo, Tadashi Matsuda, Akihiro Mizushima, Kenji Oritani, Yuto Miyasaka, Akihiko Yoshimura, Chikako Yamamoto, Ryuta Muromoto

Publikováno v: Journal of Biological Chemistry. 285:38093-38103

Signal transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein, which contains pleckstrin homology (PH) and Src homology 2 (SH2)-like domains, as well as a signal transducer and an activator of transcription 3 (STAT3)-binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::084134c2d2bf7ba39205f3567703537a
https://doi.org/10.1074/jbc.m110.162388

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Regulated Phosphorylation of a Major UDP-glucuronosyltransferase Isozyme by Tyrosine Kinases Dictates Endogenous Substrate Selection for Detoxification*

Autor: Partha S. Mitra, Sunit K. Chakraborty, Nikhil K. Basu, Ida S. Owens, Tapas Saha, Mousumi Basu

Publikováno v: The Journal of Biological Chemistry

Whereas UDP-glucuronosyltransferase-2B7 is widely distributed in different tissues, it preferentially detoxifies genotoxic 4-OH-estradiol and 4-OH-estrone (4-OHE(1)) with barely detectable 17β-estradiol (E(2)) conversion following expression in COS-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e02dfcd1ecbaa88ba34e73540b707930
http://europepmc.org/articles/PMC3020772

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Distinct acute lymphoblastic leukemia (ALL)-associated Janus Kinase 3 (JAK3) mutants exhibit different cytokine-receptor requirements and JAK-inhibitor specificities

Autor: Jean-Christophe Renauld, Elisabetta Flex, Sandrine Degryse, Jan Cools, Laurent Knoops, Tekla Hornakova, Marco Tartaglia, Elisabeth Losdyck, Stefan N. Constantinescu, Olga Gielen, Lorraine Springuel

Publikováno v: Journal of Biological Chemistry, Vol. 290, no. 48, p. 29022-29034 (2015)

JAK1 and JAK3 are recurrently mutated in acute lymphoblastic leukemia. These tyrosine kinases associate with heterodimeric cytokine receptors such as IL-7 receptor or IL-9 receptor, in which JAK1 is appended to the specific chain, and JAK3 is appende

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1deb3d95fd0dfca2ff6d4dc508b94953
https://hdl.handle.net/2078.1/166226

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Intramolecular dynamics within the N-Cap-SH3-SH2 regulatory unit of the c-Abl tyrosine kinase reveal targeting to the cellular membrane

Autor: Yraima Cordeiro, Giulia D. S. Ferretti, Jerson L. Silva, Elen G. Pereira, Guilherme A. P. de Oliveira, Ana Paula Valente

Publikováno v: The Journal of Biological Chemistry

Background: c-Abl regulates cell signaling and participates in leukemia pathogenesis via Bcr-Abl chimeric protein. Results: N-Cap and SH3 residues acquire μs-ms motions within the regulatory unit and membrane anchoring upon protein activation. Concl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::135a7a6f127dfdf99a044c555e1cf144
https://pubmed.ncbi.nlm.nih.gov/23928308

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Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling

Autor: Rajeshwari R. Valiathan, Richard Arkwright, Hsueh Liang Fu, Malika Kumarasiri, Kiran V. Mahasenan, Gunjan Agarwal, Rafael Fridman, Shahriar Mobashery, Cosmin Mihai, Paul H. Huang, Anjum Sohail

The discoidin domain receptors (DDRs) are receptor tyrosine kinases that recognize collagens as their ligands. DDRs display unique structural features and distinctive activation kinetics, which set them apart from other members of the kinase superfam

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cfcce219831d0b11cb77e457bd0d770
https://hdl.handle.net/11541.2/121231

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Syk-dependent phosphorylation of CLEC-2: a novel mechanism of hem-immunoreceptor tyrosine-based activation motif signaling

Autor: Sonia, Séverin, Alice Y, Pollitt, Leyre, Navarro-Nuñez, Craig A, Nash, Diego, Mourão-Sá, Johannes A, Eble, Yotis A, Senis, Steve P, Watson

Publikováno v: The Journal of Biological Chemistry

The C-type lectin-like receptor CLEC-2 signals via phosphorylation of a single cytoplasmic YXXL sequence known as a hem-immunoreceptor tyrosine-based activation motif (hemITAM). In this study, we show that phosphorylation of CLEC-2 by the snake toxin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6eca7efe8f24d514307f95b15ee630a4
https://pubmed.ncbi.nlm.nih.gov/21098033

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