RIM3γ and RIM4γ are key regulators of neuronal arborization.

The large isoforms of the Rab3 interacting molecule (RIM) family, RIM1α/β and RIM2α/β, have been shown to be centrally involved in mediating presynaptic active zone function. The RIM protein family contains two additional small isoforms, RIM3γ and RIM4γ, which are composed only of the RIM-specific C-terminal C2B domain and varying N-terminal sequences and whose function remains to be elucidated. Here, we report that both, RIM3γ and RIM4γ, play an essential role for the development of neuronal arborization and of dendritic spines independent of synaptic function.

Analyses of the spatiotemporal expression and subcellular localization of liprin-α proteins.

The members of the Liprin-α protein family, Liprin-α1-4, are scaffolding proteins that play important roles in the regulation of synapse assembly and maturation, vesicular trafficking, and cell motility. Recent evidence suggests that despite their high degree of homology, the four isoforms can be differentially regulated and fulfill diverging functions. However, to date their precise regional and subcellular distribution has remained elusive.

Presence of human herpes virus 6 DNA exclusively in temporal lobe epilepsy brain tissue of patients with history of encephalitis.

Temporal lobe epilepsy (TLE) is frequently associated with mesial temporal sclerosis (MTS). Many etiologic aspects of TLE are still unresolved. Here, we aimed to analyze the presence of human herpes virus 6 (HHV-6) DNA in distinct TLE pathologies.

RIM proteins and their role in synapse function.

Active zones are specialized areas of the plasma membrane in the presynaptic nerve terminal that mediate neurotransmitter release and synaptic plasticity. The multidomain proteins RIM1 and RIM2 are integral components of the cytomatrix at the active zone, interacting with most other active zone-enriched proteins as well as synaptic vesicle proteins. In the brain, RIMs are present in multiple isoforms (alpha, beta, gamma) diverging in their structural composition, which mediate overlapping and distinct functions.

Structure and evolution of RIM-BP genes: identification of a novel family member.

RIM-binding proteins (RIM-BPs) were identified as binding partners of the presynaptic active zone proteins RIMs as well as for voltage-gated Ca(2+)-channels. They were suggested to form a functional link between the synaptic-vesicle fusion apparatus and Ca(2+)-channels. Here we show that the RIM-BP gene family diversified in different stages during evolution, but retained their unique domain structure.

Redundant functions of RIM1alpha and RIM2alpha in Ca(2+)-triggered neurotransmitter release.

Alpha-RIMs (RIM1alpha and RIM2alpha) are multidomain active zone proteins of presynaptic terminals. Alpha-RIMs bind to Rab3 on synaptic vesicles and to Munc13 on the active zone via their N-terminal region, and interact with other synaptic proteins via their central and C-terminal regions. Although RIM1alpha has been well characterized, nothing is known about the function of RIM2alpha.