Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok

Article Abstract:

A 62 kDa protein (p62) that is related to the p120 Ras GTPase activating protein (rasGAP), was purified by an anti-phosphotyrosine antibody. Molecular cloning indicated the presence of a cDNA encoding a novel protein, p62(super dok) with little homology to others but with a prominent set of tyrosines and nearby sequences suggestive of SH2 binding sites. In cells, v-Abl tyrosine kinase binds and strongly phosphorylates p62(super dok) to the rasGAP. A monoclonal antibody, 2C4, to the rasGAP-associated p62 reacts with p62(super dok). Hence, p62(super dok) seems to be a major substrate of many tyrosine kinases.

Protein tyrosine kinase, Protein-tyrosine kinase

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Daxx, a novel fas-binding protein that activates JNK and apoptosis

Article Abstract:

A study was conducted on Daxx, a novel signaling protein that activates Jun N-terminal kinase (JNK) and apoptosis. Results indicate that overexpression of Daxx increases Fas-mediated apoptosis and activates the JNK pathway. While Daxx's C-terminal portion reacts with the Fas-binding domain JNK and apoptosis interact with a different region. Furthermore, although the apoptotic pathway is compatible with the FADD pathway, it is also sensitive to Bcl-2 and JNK's dominant-negative pathway inhibitor.

Cell receptors

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Proteases for cell suicide: functions and regulation of caspases

Article Abstract:

Apoptosis or the programmed cell death is mediated by a suicide machinery, the core component of this system is a family of proteases termed caspases. This review discusses physiochemical basis of caspases' transformation into active proteases, via a proteolytic regulatory process, whch eventually leads to apoptotic cell death.

United States, Physiological aspects, Proteases, Genetic regulation, Physiological regulation, Biological control systems, Cell metabolism

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