Solution structure of BID, an intracellular amplifier of apoptotic signaling

Article Abstract:

The solution structure of the cross-talk agent BID is determined. This proapoptosis member of the BCL2 regulatory family is shown to consist of eight alpha helices arranged in a compact fold homologous to BCL-X(sub L). It is also shown that the hydrophobic cleft of BCL-X(sub L), which binds to the BAK BH3 domain, readily interacts with the BH3 domain-containing helix. Structural data on the BCL-X(sub L)-BAK BH3 peptide complex is then used to model the heterodimerization between BCL-X(sub L) and the full-length BID by superimposing the BH3 domains of BAK and BID.

Membrane proteins, Cellular signal transduction

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The regulation of anoikis: MEKK-1 activation requires cleavage by caspases

Article Abstract:

A DEVD motif-specific caspase that cleaves MEKK-1 specifically occurs when cells lose matrix contact. Overexpression results in apoptosis stimulation by the MEKK-1 cleavage product, sensitization of cells to anoikis by the wild type, full-length MEKK-1 and cell protection against anoikis by a cleavage-resistant mutant of MEKK-1. The findings indicate that caspases can induce apoptosis through MEKK-1 activation.

Protein kinases, Extracellular matrix

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Caspases: intracellular signaling by proteolysis

Article Abstract:

A new breed of viral proteases has evolved with a new set of diverse structures and biological functions. The evolved protease sequence has the capability of associating with the viral genome, becoming a core protein, cleaving peptide bonds through posttranslational modification and dimerization. Colocalization of enzyme and substrate within a virion compensates for the structural compromises.

Analysis, Proteolysis, Post-translational modification

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