BIOMAT Database Logo BIOMAT Database Logo

The epidermal growth factor receptor tyrosine kinase phosphorylates connexin32. 1998

J A Díez, and M Elvira, and A Villalobo
Instituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.

The epidermal growth factor (EGF) receptor purified by calmodulin-affinity chromatography from solubilized rat liver plasma membranes phosphorylates connexin32 in gap junction plaques isolated from the same origin. Phosphorylation of connexin32 was stimulated by EGF and mainly occurs at tyrosine residue(s), although phosphorylation of serine and threonine residues was also detected. The kinetics parameters for the phosphorylation of connexin32 parallel those for the transphosphorylation of the EGF receptor. m-Calpain proteolyzes phosphoconnexin32, and its major 26 kDa proteolytic fragment only contains phosphotyrosine residue(s). Calmodulin binds to connexin32 in the absence of calcium and prevents in great extent its phosphorylation by the EGF receptor tyrosine kinase.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D002147 Calmodulin A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels. Calcium-Dependent Activator Protein,Calcium-Dependent Regulator,Bovine Activator Protein,Cyclic AMP-Phosphodiesterase Activator,Phosphodiesterase Activating Factor,Phosphodiesterase Activator Protein,Phosphodiesterase Protein Activator,Regulator, Calcium-Dependent,AMP-Phosphodiesterase Activator, Cyclic,Activating Factor, Phosphodiesterase,Activator Protein, Bovine,Activator Protein, Calcium-Dependent,Activator Protein, Phosphodiesterase,Activator, Cyclic AMP-Phosphodiesterase,Activator, Phosphodiesterase Protein,Calcium Dependent Activator Protein,Calcium Dependent Regulator,Cyclic AMP Phosphodiesterase Activator,Factor, Phosphodiesterase Activating,Protein Activator, Phosphodiesterase,Protein, Bovine Activator,Protein, Calcium-Dependent Activator,Protein, Phosphodiesterase Activator,Regulator, Calcium Dependent
D002154 Calpain Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4. Calcium-Activated Neutral Protease,Calcium-Dependent Neutral Proteinase,Ca2+-Activated Protease,Calcium-Activated Neutral Proteinase,Calcium-Activated Protease,Calcium-Dependent Neutral Protease,Calpain I,Calpain II,Desminase,Ca2+ Activated Protease,Calcium Activated Neutral Protease,Calcium Activated Neutral Proteinase,Calcium Activated Protease,Calcium Dependent Neutral Protease,Calcium Dependent Neutral Proteinase,Neutral Protease, Calcium-Activated,Neutral Protease, Calcium-Dependent,Neutral Proteinase, Calcium-Activated,Neutral Proteinase, Calcium-Dependent,Protease, Ca2+-Activated,Protease, Calcium-Activated,Protease, Calcium-Activated Neutral,Protease, Calcium-Dependent Neutral,Proteinase, Calcium-Activated Neutral,Proteinase, Calcium-Dependent Neutral
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D004815 Epidermal Growth Factor A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form. EGF,Epidermal Growth Factor-Urogastrone,Urogastrone,Human Urinary Gastric Inhibitor,beta-Urogastrone,Growth Factor, Epidermal,Growth Factor-Urogastrone, Epidermal,beta Urogastrone
D000097002 Gap Junction beta-1 Protein A GAP JUNCTION beta subunit containing four transmembrane domains expressed in myelinating SCHWANN CELLS and is localized to peripheral MYELIN (e.g., noncompact myelin in the paranode and Schmitt-Lanterman incisures). Mutations in the human gene GJB1 are associated with X-linked CHARCOT-MARIE-TOOTH DISEASE type 1 (CMT1X). Connexin 32,Connexin 32 Protein,Cx32 Protein,GJB1 Protein,Gap Junction B1,Gap Junction beta1 Protein,Gap Junction beta 1 Protein,Protein, Connexin 32,Protein, Cx32,Protein, GJB1

Related Publications

J A Díez, and M Elvira, and A Villalobo
C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.
February 1984, The Journal of biological chemistry,
J A Díez, and M Elvira, and A Villalobo
c-Src phosphorylates epidermal growth factor receptor on tyrosine 845.
October 1995, Biochemical and biophysical research communications,
J A Díez, and M Elvira, and A Villalobo
Epidermal growth factor receptor tyrosine kinase inhibitors.
June 2004, British journal of cancer,
J A Díez, and M Elvira, and A Villalobo
Epidermal growth factor receptor tyrosine kinase inhibitors.
August 2002, Current opinion in pharmacology,
J A Díez, and M Elvira, and A Villalobo
Calmodulin inhibits the epidermal growth factor receptor tyrosine kinase.
July 1992, The Journal of biological chemistry,
J A Díez, and M Elvira, and A Villalobo
Sensitivities to various epidermal growth factor receptor-tyrosine kinase inhibitors of uncommon epidermal growth factor receptor mutations L861Q and S768I: What is the optimal epidermal growth factor receptor-tyrosine kinase inhibitor?
August 2016, Cancer science,
J A Díez, and M Elvira, and A Villalobo
Epidermal growth factor receptor tyrosine kinase inhibitor-resistant disease.
March 2013, Journal of clinical oncology : official journal of the American Society of Clinical Oncology,
J A Díez, and M Elvira, and A Villalobo
Epidermal growth factor receptor first generation tyrosine-kinase inhibitors.
November 2019, Translational lung cancer research,
J A Díez, and M Elvira, and A Villalobo
Small-molecule epidermal growth factor receptor tyrosine kinase inhibitors.
January 2003, The oncologist,
J A Díez, and M Elvira, and A Villalobo
Resistance to epidermal growth factor receptor tyrosine kinase inhibitors.
November 2009, Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer,
Copied contents to your clipboard!