Synaptic transmission: well-placed modulators.

I D Forsythe; M Barnes-Davies

doi:10.1016/s0960-9822(06)00175-8

Home/Archive/PubMed

PubMed · 9197230

Synaptic transmission: well-placed modulators.

I D Forsythe·M Barnes-Davies

View original source ↗Export metadata ↓

Abstract

Metabotropic glutamate receptors are involved in the modulation of synaptic transmission; their localization in perisynaptic areas would appear to limit their activation by endogenous glutamate, but recent reports suggest that this strategic placement allows use-dependent activation of these synaptic modulators.

Explore related subjects

Cell Compartmentation Glutamic Acid Models, Neurological Neuronal Plasticity Receptors, AMPA Receptors, Metabotropic Glutamate Receptors, N-Methyl-D-Aspartate Synaptic Transmission Journal Article Review

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

I D Forsythe, M Barnes-Davies. 1997-06-01. Synaptic transmission: well-placed modulators.. https://doi.org/10.1016/s0960-9822(06)00175-8

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2006

New component of ESCRT-I regulates endosomal sorting complex assembly.

The endosomal sorting complex required for transport (ESCRT) complexes play a critical role in receptor down-regulation and retroviral budding. Although the crystal structures of two ESCRT complexes have been determined, the molecular mechanisms underlying the assembly and regulation of the ESCRT machinery are still poorly understood. We identify a new component of the ESCRT-I complex, multivesicular body sorting factor of 12 kD (Mvb12), and demonstrate that Mvb12 binds to the coiled-coil domain of the ESCRT-I subunit vacuolar protein sorting 23 (Vps23). We show that ESCRT-I adopts an oligomeric state in the cytosol, the formation of which requires the coiled-coil domain of Vps23, as well as Mvb12. Loss of Mvb12 results in the disassembly of the ESCRT-I oligomer and the formation of a stable complex of ESCRT-I and -II in the cytosol. We propose that Mvb12 stabilizes ESCRT-I in an oligomeric, inactive state in the cytosol to ensure that the ordered recruitment and assembly of ESCRT-I and -II is spatially and temporally restricted to the surface of the endosome after activation of the MVB sorting reaction.

Cell Compartmentation↗

PubMed2006

Pom1 kinase links division plane position to cell polarity by regulating Mid1p cortical distribution.

In fission yeast, Mid1p, a major determinant for division plane position, defines a medial cortical compartment where it recruits myosin II at the onset of mitosis to initiate contractile ring assembly. How Mid1p is restricted to the medial cortex is unknown. We report here that in a pom1 polarity mutant, which displays a monopolar growth pattern, Mid1p distribution expands towards the non-growing cell tip, uncoupling Mid1p localization from nuclear position. This accounts for the displacement of the contractile ring during mitosis. By contrast, Mid1p localization is normal in a bud6Delta strain, indicating that Mid1p misdistribution is not a general consequence of monopolar growth. We conclude that Pom1 kinase acts as a negative regulator of Mid1p distribution, excluding Mid1p from non-growing ends, whereas a Pom1-independent mechanism prevents Mid1p association with growing ends. Our work therefore provides evidence that cell polarity regulators influence the distribution of Mid1p, linking division plane position to cell polarity.

Cell Compartmentation↗

PubMed2006

Dynamic subcompartmentalization of the mitochondrial inner membrane.

The inner membrane of mitochondria is organized in two morphologically distinct domains, the inner boundary membrane (IBM) and the cristae membrane (CM), which are connected by narrow, tubular cristae junctions. The protein composition of these domains, their dynamics, and their biogenesis and maintenance are poorly understood at the molecular level. We have used quantitative immunoelectron microscopy to determine the distribution of a collection of representative proteins in yeast mitochondria belonging to seven major processes: oxidative phosphorylation, protein translocation, metabolite exchange, mitochondrial morphology, protein translation, iron-sulfur biogenesis, and protein degradation. We show that proteins are distributed in an uneven, yet not exclusive, manner between IBM and CM. The individual distributions reflect the physiological functions of proteins. Moreover, proteins can redistribute between the domains upon changes of the physiological state of the cell. Impairing assembly of complex III affects the distribution of partially assembled subunits. We propose a model for the generation of this dynamic subcompartmentalization of the mitochondrial inner membrane.

Cell Compartmentation↗