Title: Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D
Authors: Jamora, C
Yamanouye, N
Van Lint, Johan
Laudenslager, J
Vandenheede, Jackie
Faulkner, D J
Malhotra, V # ×
Issue Date: 23-Aug-1999
Series Title: Cell. vol:98 issue:1 pages:59-68
Abstract: We have shown previously that the betagamma subunits of the heterotrimeric G proteins regulate the organization of the pericentriolarly localized Golgi stacks. In this report, evidence is presented that the downstream target of Gbetagamma is protein kinase D (PKD), an isoform of protein kinase C. PKD, unlike other members of this class of serine/threonine kinases, contains a pleckstrin homology (PH) domain. Our results demonstrate that Gbetagamma directly activates PKD by interacting with its PH domain. Inhibition of PKD activity through the use of pharmacological agents, synthetic peptide substrates, and, more specifically, the PH domain of PKD prevents Gbetagamma-mediated Golgi breakdown. Our findings suggest a possible mechanism by which the direct interaction of Gbetagamma with PKD regulates the dynamics of Golgi membranes and protein secretion.
ISSN: 0092-8674
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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