Neural localization of addicsin in mouse brain

Akiduki, Saori; Ochiishi, Tomoyo; Ikemoto, Mitsushi

doi:10.1016/j.neulet.2007.08.056

Cited by 12 publications

(11 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, our protein fractionation analysis using mouse whole brain lysates prepared in PBS, NaCl, or Na 2 CO 3 buffer, all indicate that addicsin is predominantly present in the S1 soluble fraction, while the ER transmembrane protein calnexin is present in the P2 pellet fraction (Ikemoto et al, 2002). Our subcellular fractionation analysis with highly purified synaptic fractions prepared from mouse forebrain also support the notion that addicsin is present in the cytoplasmic and presynaptic membrane fractions (Akiduki et al, 2007). Furthermore, immunocytochemical studies reveal that addicsin is present in both the plasma membrane and the intracellular compartments, including the ER (Ikemoto et al, 2002;Watabe et al, 2007Watabe et al, , 2008.…”

Section: Addicsinsupporting

confidence: 76%

“…Indeed, later in this chapter, we discuss evidence that addicsin participates in intracellular protein trafficking of neurotransmitter receptors. Addicsin is widely distributed in the brain (Akiduki et al, 2007;Butchbach et al, 2002). In the mature CNS, addicsin is expressed in the cerebral cortex, amygdala, striatum, hippocampus (CA1-3 fields), dentate gyrus, and cerebellum.…”

Section: Addicsinmentioning

confidence: 99%

“…In the mature CNS, addicsin is expressed in the cerebral cortex, amygdala, striatum, hippocampus (CA1-3 fields), dentate gyrus, and cerebellum. Addicsin is expressed in the somata of glutamatergic and GABAergic neurons and exhibits presynaptic localization in restricted regions such as CA3 stratum lucidum (Akiduki et al, 2007). In situ hybridization analysis reveals that addicsin mRNA is widely distributed in the brain, predominantly expressed in principal neurons, including glutamatergic and GABAergic neurons in the mature CNS (Inoue et al, 2005).…”

Section: Addicsinmentioning

confidence: 99%

See 2 more Smart Citations

Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin

Ikemoto¹,

Arano²

2012

Biochemistry

View full text Add to dashboard Cite

Section: Addicsinsupporting

confidence: 76%

Section: Addicsinmentioning

confidence: 99%

Section: Addicsinmentioning

confidence: 99%

See 1 more Smart Citation

Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin

Ikemoto¹,

Arano²

2012

Biochemistry

View full text Add to dashboard Cite

“…Addicsin/GTRAP3-18 is widely distributed in various tissues, including the brain (19,20). In the CNS, addicsin is predominantly expressed in the principal neurons of the mature brain such as the pyramidal cells and ␥-aminobutyric acid-ergic interneurons scattered in the hippocampal formation (21,22). Addicsin is thought to be localized in intracellular compartments and implicated in intracellular trafficking events, because it is a member of the prenylated Rab acceptor 1 domain family, member 3 (PRAF3) (23).…”

mentioning

confidence: 99%

Modulation of the Neural Glutamate Transporter EAAC1 by the Addicsin-interacting Protein ARL6IP1

Akiduki

Ikemoto

2008

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Addicsin (Arl6ip5) is a murine homologue of rat glutamate transporter-associated protein 3-18 (GTRAP3-18), a putative negative modulator of Na ؉ -dependent neural glutamate transporter-excitatory amino acid carrier 1 (EAAC1). Here we report that ADP-ribosylation factor-like 6 interacting protein 1 (Arl6ip1) is a novel addicsin-associated partner that indirectly promotes EAAC1-mediated glutamate transport activity in a protein kinase C activity-dependent manner. Like addicsin, Arl6ip1 is expressed in numerous tissues and proved likely to be co-localized with addicsin in certain neurons in the matured brain. Arl6ip1 was not translocated from the subcellular compartments under any of the test conditions and had no association with any molecules on the plasma membrane. Immunoprecipitation assay demonstrated that Arl6ip1 bound directly to addicsin and that the hydrophobic region located at amino acids 103-117 of addicsin was crucial to the formation of the Arl6ip1-addicsin heterodimer and addicsin homodimer. Glutamate transport assay revealed that increasing the expression of Arl6ip1 in C6BU-1 cells markedly enhanced Na ؉ -dependent EAAC1-mediated glutamate transport activity in the presence of 100 nM phorbol 12-myristate 13-acetate. Under these conditions, kinetic analyses demonstrated that EAAC1 altered glutamate transport activity by increasing its glutamate affinity but not its maximal velocity. Meanwhile, increasing expression of addicsin Y110A/L112A mutant lacking binding ability for Arl6ip1 showed no enhancement of EAAC1-mediated glutamate transport activity, regardless of phorbol 12-myristate 13-acetate activation, suggesting that association between addicsin and Arl6ip1 causes altered EAAC1-mediated glutamate transport activity. Our findings suggest that Arl6ip1 is a novel addicsin-associated partner that promotes EAAC1-mediated glutamate transport activity by decreasing the number of addicsin molecules available for interaction with EAAC1.

show abstract

“…In chemical synapses, PRA1 associates with Piccolo, a zinc finger protein of the presynaptic cytoskeletal matrix, suggesting a function in synaptic vesicle trafficking (Fenster et al, 2000). PRA1 also interacts with other prenylated small GTPases, such as the mouse Ha-Ras, N-Ras, TC21, and RhoA, as well as with the v-SNARE protein VAMP2 (Martincic et al, 1997;Figueroa et al, 2001), and it plays a role as modulator of the neural Glu transporter excitatory amino acid carrier 1 (Akiduki et al, 2007). Because of its capacity to interact with GTPases and SNARE proteins, PRA1 might connect these two large groups of proteins to efficiently control vesicle docking and fusion events.…”

mentioning

confidence: 99%

ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

View full text Add to dashboard Cite

Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis (Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/ prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.

show abstract

Neural localization of addicsin in mouse brain

Cited by 12 publications

References 13 publications

Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin

Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin

Modulation of the Neural Glutamate Transporter EAAC1 by the Addicsin-interacting Protein ARL6IP1

ThePRA1Gene Family in Arabidopsis

Contact Info

Product

Resources

About