Protein kinase D signaling.

ROZENGURT E, REY O, WALDRON RT.

JOURNAL OF BIOLOGICAL CHEMISTRY

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Año: 2005 p. 13205 - 13208

0021-9258

A rapid increase in the synthesis of lipid-derived second messengers with subsequent activation of protein phosphorylation cascades has emerged as one of the fundamental mechanisms of signal transduction in animal cells. A plethora of external signals, including hormones, neurotransmitters, growth factors, cytokines, bioactive lipids, and tastants promote the stimulation of the isoforms of the PLC family, including β, γ, δ, and ϵ. PLCs catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate to produce two second messengers: inositol 1,4,5-P3, which triggers the release of Ca2+ from internal stores, and DAG, which elicits cellular responses through a variety of effectors . The most prominent intracellular targets of DAG are the classic (α, β, γ) and novel (δ, ϵ, η, θ) isoforms of PKC, which are differentially expressed in cells and tissues. The mechanisms by which PKC-mediated signals are propagated to critical downstream targets remain incompletely understood. Protein kinase D (PKD), the founding member of a new family of serine/threonine protein kinases and the subject of this minireview, occupies a unique position in the signal transduction pathways initiated by DAG and PKC. PKD not only is a direct DAG target but also lies downstream of PKCs in a novel signal transduction pathway implicated in the regulation of multiple fundamental biological processes.