G(beta gamma)-mediated regulation of Golgi organization is through the direct activation of protein kinase D

Article Abstract:

Studies have revealed that protein kinase D is a downstream target of G(beta gamma) and plays a critical role in the regulation of Golgi structure and function. Initial experiments involved the analysis of the effects of a variety of inhibitors of protein kinases in an attempt to reveal the class of components that might be the downstream of G(beta gamma). Findings indicate that a possible mechanism by which the direct interaction of G(beta gamma) with protein kinase D regulates the dynamics of Golgi membranes and protein secretion.

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Signaling via mitogen-activated protein kinase kinase (MEK1) is required for Golgi fragmentation during mitosis

Article Abstract:

Research was conducted to characterize an assay associated with Golgi fragmentation in permeabilized rat kidney cells utilizing mitotic normal rat kidney cell-based extracts. Cells were incubated with various concentrations of ERK2 while mitotic extract was pretreated with specific inhibitors. Results showed extensive fragmentation of the complex and indicated that the endocytic vesicle fusion in vitro was characterized by p34(super cdc2) kinase.

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Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone

Article Abstract:

Ilimaquinone (IQ), a major metabolite of several dictyoceratid sponges, causes golgi membranes to break down into small vesicular structures called Vesiculated Golgi Membranes (VGM). IQ then inhibits vesicular protein transport by affecting an early step in the vesicle formation. IQ also causes depolarization of cytoplasmic microtubules.

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