Tyrosine protein kinase substrate p36: A member of the annexin family of Ca2+/phospholipid-binding proteins
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Views and Reviews Tyrosine Protein Kinase Substrate p 36 : A Member of the Annexin Family of Ca 2 - I - / P hosphol ipid - Bindi ng Proteins
Ten years ago a protein of apparent M, 36,000 was identified as a major cellular target for the transforming tyrosine kinase encoded by the src oncogene. In a series of in vivo labeling experiments, Radke and Martin [1979], Radke et al. [1980], and Erikson and Erikson [1980] showed that p36 is phosphorylated on tyrosine residues when chicken embryo fibroblasts are transformed by Rous sarcoma vi...
متن کاملTyrosine kinase substrate annexin II (p36)--biochemical characterization and conservation among species.
secreted then degraded by endogenous proteases, because placental annexin 4 was not degraded when added to prostate fluid and incubated at 37°C. The collective concentrations of annexin 1 , des-( 1 -29)-annexin 1, and annexin 5 in prostate fluid and seminal plasma were 1.3% and 0.2% of the total protein, respectively. This is consistent with their secretion by the prostate and subsequent diluti...
متن کاملStructural analysis of p36, a Ca2+/lipid-binding protein of the annexin family, by proteolysis and chemical fragmentation.
Limited proteolysis of the core domain of the 36-kDa protein p36 by trypsin gives a first insight into the structural organization of the four annexin repeats. Trypsin opens only a single peptide bond, situated between residues 204 and 205. The two fragments (of 20 kDa and 15 kDa), each containing two annexin repeats, remain as a tight complex (nicked core), which binds phospholipids in a Ca2(+...
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Background: When Staphylococcus aureus is grown in the presence of high concentration of external glucose, this sugar is phosphorylated by glucokinase (glkA) to form glucose-6-phosphate. This product subsequently enters into anabolic phase, which favors biofilm formation. The presence of ROK (repressor protein, open reading frame, sugar kinase) motif, phosphate-1 and -2 sites, and tyrosine kina...
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Microtubules are central to the spatial organization of diverse membrane-trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH(2)-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to o...
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ژورنال
عنوان ژورنال: Cell Motility and the Cytoskeleton
سال: 1989
ISSN: 0886-1544,1097-0169
DOI: 10.1002/cm.970140402