Functional expression of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors in cerebellar granule cells requires stargazin, a member of a large family of four-pass transmembrane proteins. Here, we define a family of transmembrane AMPA receptor regulatory proteins (TARPs), which comprise stargazin, γ-3, γ-4, and γ-8, but not related proteins, that mediate surface expression of AMPA receptors. TARPs exhibit discrete and complementary patterns of expression in both neurons and glia in the developing and mature central nervous system. In brain regions that express multiple isoforms, such as cerebral cortex, TARP–AMPA receptor complexes are strictly segregated, suggesting distinct roles for TARP isoforms. TARPs interact with AMPA receptors at the postsynaptic density, and surface expression of mature AMPA receptors requires a TARP. These studies indicate a general role for TARPs in controlling synaptic AMPA receptors throughout the central nervous system.

https://rupress.org/jcb/article-pdf/161/4/805/1308397/jcb1614805.pdf

Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins

http://www.physiology.uiowa.edu/campbell/Publications/PDF/314Arikkath.pdf

Auxiliary subunits: essential components of the voltage-gated calcium channel complex.

Calcium channel β subunits have marked effects on the trafficking and on several of the biophysical properties of all high voltage activated calcium channels. In this article I shall review information on the different genes, on the structure of the β subunits, and on their differential expression and post-translational modification. Their role in trafficking and assembly of the calcium channel heteromultimer will be described, and I will then review their effects on voltage-dependent and kinetic properties, stressing the differences between palmitoylated β2a and the other β subunits. Evidence for effects on calcium channel pharmacology will also be examined. I shall discuss the hypothesis that β subunits can bind reversibly to calcium channels, and examine their role in the G protein modulation of calcium channels. Finally, I shall describe the consequences of knock-out of different β subunit genes, and describe evidence for the involvement of β subunits in disease.

/pdf/beta-subunits-of-voltage-gated-calcium-channels-36gfu8wapp.pdf

Beta subunits of voltage-gated calcium channels.

The Expanding Social Network of Ionotropic Glutamate Receptors: TARPs and Other Transmembrane Auxiliary Subunits

Calcium regulates a wide spectrum of physiological processes such as heartbeat, muscle contraction, neuronal communication, hormone release, cell division, and gene transcription. Major entryways f...

The β Subunit of Voltage-Gated Ca2+ Channels

We have cloned and characterized a new member of the voltage-dependent Ca2+ channel γ subunit family, with a novel gene structure and striking properties. Unlike the genes of other potential γ subunits identified by their homology to the stargazin gene, CACNG7 is a five-, and not four-exon gene whose mRNA encodes a protein we have designated γ7. Expression of human γ7 has been localized specifically to brain. N-type current through CaV2.2 channels was almost abolished when co-expressed transiently with γ7 in either Xenopus oocytes or COS-7 cells. Furthermore, immunocytochemistry and western blots show that γ7 has this effect by causing a large reduction in expression of CaV2.2 rather than by interfering with trafficking or biophysical properties of the channel. No effect of transiently expressed γ7 was observed on pre-existing endogenous N-type calcium channels in sympathetic neurones. Low homology to the stargazin-like γ subunits, different gene structure and the unique functional properties of γ7 imply that it represents a distinct subdivision of the family of proteins identified by their structural and sequence homology to stargazin.

/pdf/the-novel-product-of-a-five-exon-stargazin-related-gene-4dy0bsqtyv.pdf

The novel product of a five-exon stargazin-related gene abolishes CaV2.2 calcium channel expression

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The novel product of a five-exon stargazin-related gene abolishes CaV2.2 calcium channel expression