Publications by authors named "Chikako Kikuchi"

Social recognition memory (SRM) is a key determinant of social interactions. While the cerebellum emerges as an important region for social behavior, how cerebellar activity affects social functions remains unclear. We selectively increased the excitability of molecular layer interneurons (MLIs) to suppress Purkinje cell firing in the mouse cerebellar vermis.

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Purkinje cell dendrites convert excitatory climbing fiber input into signals that instruct plasticity and motor learning. Modulation of instructive signaling may increase the range in which learning is encoded, yet the mechanisms that allow for this are poorly understood. We found that optogenetic activation of molecular layer interneurons (MLIs) that inhibit Purkinje cells suppressed climbing-fiber-evoked dendritic Ca spiking.

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Article Synopsis
  • The cerebellar system is crucial for refining motor actions, with Purkinje cells being the main output of the cerebellar cortex, influenced by various types of inputs.
  • Molecular layer interneurons (MLIs) play a significant role in modulating Purkinje cell activity through feed-forward inhibition, relying on excitatory signals from parallel fibers.
  • A newly developed knock-in mouse line utilizing Cre recombinase allows researchers to specifically target MLIs for study, enabling the examination of their effects on cerebellar function without affecting other cell types.
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  • Cephalostatin 1, OSW-1, ritterazine B, and schweinfurthin A are natural compounds that inhibit the growth of human cancer cells but their exact cellular targets were initially unknown.
  • Recent research identified these compounds as targeting oxysterol binding protein (OSBP) and its related protein ORP4L, which are not previously linked to cancer cell survival.
  • The compounds, now termed ORPphilins, serve as tools to explore the cellular functions of OSBP and ORP4L, potentially revealing their roles in human diseases.
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Many extracellular signals stimulate phosphatidylinositol-3-kinase, which in turn activates the Rac1 GTPase, the protein kinase Akt and the Akt Thr 308 upstream kinase PDK1. Active Rac1 stimulates a number of events, including substrate phosphorylation by a subgroup of the PAK family of kinases. The combined effects of Rac1, PDK1 and Akt are crucial for cell migration, growth, survival, metabolism and tumorigenesis.

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