The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation

Article Abstract:

Experiment was conducted to describe the characterization and the molecular cloning of IKKbeta, a second component of the IKK complex. IKKbeta is closely related to the IKKalpha structure and also contains a kinase domain, a helix-loop-helix and a leucine zipper. Research shows that the functional IKK complex contains both IKKbeta and IKKalpha and that both protein kinases play important roles in IkappaB phosphorylation and NF-kappaB activation. Results suggest that their helix-loop-helix motifs may be involved in interactions with essential regulatory subunits.

Cloning, Cell interaction, Cell interactions

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MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption

Article Abstract:

A study was conducted to describe the molecular cloning, distribution, activation mechanism and overexpression of two MARK proteins from rat. The findings indicate that MARKs phosphorylate microtubule-associated proteins and can potentially disrupt the microtubule network. Upstream factors may phosphorylate active MARKs which could provide a mechanism by which the stability of the cytoskeleton is controlled by extracellular signals.

Microtubules

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C-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions

Article Abstract:

The mechanics of phosphorylation of distinct substrates by structurally related serine/threonine kinases is investigated. Such a specificity is elucidated by examining the interaction between the Jun kinases and Jun proteins, specifically c-Jun. Results show that heterodimerization affects the recognition of transcription factors via signal-regulated protein kinases.

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