Unique MAP Kinase binding sites
نویسندگان
چکیده
منابع مشابه
Phosphorylation of Bicoid on MAP-kinase sites
Polarity along the anteroposterior axis of the Drosophila embryo is established by the activity of maternal gene products deposited into the egg during oogenesis. These activities direct specialised domains of zygotic gene expression required for the determination of cell fate (St. Johnston and Nüsslein-Volhard, 1992). The anterior system, which is required for the formation of the head and the...
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The calcium binding sites of Bakers' Yeast Transketolase (TK) was elucidated by estimating the pKa values of the functional groups that bind to calcium. These pKa's were found to be 6.25 and 7.2 relating to the pKa's of the two immidazol moieties of histidine residues on the enzyme. The rate of the binding of calcium to the enzyme was obtained separately as a function of pH. Maximum values ...
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Focal adhesion kinase (FAK) is a protein tyrosine kinase that is ubiquitously expressed, recruited to focal adhesions, and engages in a variety of cellular signaling pathways. Diverse cellular responses, such as cell migration, proliferation, and survival, are regulated by FAK. Prior to activation, FAK adopts an autoinhibited conformation in which the FERM domain binds the kinase domain, blocki...
متن کاملPhosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase kinase and MAP kinase.
Xenopus 45-kDa mitogen-activated protein (MAP) kinase kinase (MAPKK) is a serine/threonine/tyrosine kinase, which activates MAP kinase (MAPK) by phosphorylating its threonine and tyrosine residues. MAPKK is active only when its threonine and/or serine residues are phosphorylated. We have identified from Xenopus eggs two protein kinases responsible for phosphorylation of MAPKK. The two kinases a...
متن کاملTwo adjacent docking sites in the yeast Hog1 mitogen-activated protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase.
Functional interactions between a mitogen-activated protein kinase (MAPK) and its regulators require specific docking interactions. Here, we investigated the mechanism by which the yeast osmoregulatory Hog1 MAPK specifically interacts with its activator, the MAPK kinase Pbs2, and its major inactivator, the protein phosphatase Ptp2. We found, in the N-terminal noncatalytic region of Pbs2, a spec...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
سال: 2008
ISSN: 1570-9639
DOI: 10.1016/j.bbapap.2007.09.016