Biomedical subjects

Tatsuo Suzuki

Publications and source records attributed to Tatsuo Suzuki.

At least 19 recordsLinked to original sources

PubMed2006

Characterization of mRNA species that are associated with postsynaptic density fraction by gene chip microarray analysis.

We previously reported the partial identification by random sequencing of mRNA species that are associated with the postsynaptic density (PSD) fraction prepared from the rat forebrain [Tian et al., 1999. Mol. Brain Res. 72, 147-157]. We report here further characterization by gene chip analysis of the PSD fraction-associated mRNAs, which were prepared in the presence of RNase inhibitor. We found that mRNAs encoding various postsynaptic proteins, such as channels, receptors for neurotransmitters and neuromodulators, proteins involved in signaling, scaffold and adaptor proteins and cytoskeletal proteins, were highly concentrated in the PSD fraction, whereas those encoding housekeeping proteins, such as enzymes in the glycolytic pathway, were not. We extracted approximately 1900 mRNA species that were highly concentrated in the PSD fraction. mRNAs related to certain neuronal diseases were also enriched in the PSD fraction. We also constructed a cDNA library using the PSD fraction-associated mRNAs as templates, and identified 1152 randomly selected clones by sequencing. Our data suggested that the PSD fraction-associated mRNAs are a very useful resource, in which a number of as yet uncharacterized mRNAs are concentrated. Identification and functional characterization of them are essential for complete understanding of synaptic function.

Animals↗

PubMed2006

Mechanisms for association of Ca2+/calmodulin-dependent protein kinase II with lipid rafts.

Localization of CaMKIIalpha in lipid rafts was demonstrated in both cultured neurons and mammalian cells transfected with plasmid with an insert of CaMKIIalpha cDNA by using sucrose gradient centrifugation and the sensitivity to a cholesterol-extractor, methyl-beta-cyclodextrin. CaMKIIalpha was targeted to lipid rafts possibly through protein-protein interactions via at least three domains (a.a. 261-309, 371-420, and 421-478). The multimeric structure of the full-length molecule also appeared to contribute to efficient lipid raft-targeting. Acylation of CaMKIIalpha did not appear to be a mechanism for the targeting.

Animals↗

PubMed2006

Protective effect of a protein-bound polysaccharide, PSK, on CLP-induced sepsis in mice transplanted orthotopically with colon tumor.

We investigated the effects of a protein-bound polysaccharide, PSK, on the resistance of tumor-bearing mice against sepsis induced by cecal ligation and puncture (CLP). (a) In BALB/c mice that had received intracecal transplantation of colon 26 (C26) tumor, CLP with a 21-gauge needle significantly shortened the survival time, compared with that of non-tumor-bearing mice. Oral administration of PSK to such mice resulted in a significant prolongation of the survival time and increase of the survival rates. The effects were dependent on the timing of PSK administration and the dose. (b) CLP significantly increased the IL-10 level in serum, the IL-10 gene expression by spleen cells, the number of IL-10-producing CD4-positive T cells, and the productivity of IL-10 by spleen of tumor-bearing mice compared with that of non-tumor-bearing mice. PSK administration to such mice suppressed the increase. Further, PSK prevented the reduction of gene expression of IFN-gamma and the number of IFN-gamma-producing CD4-positive T cells and IFN-gamma productivity by spleen cells of tumor-bearing CLP-treated mice. (c) Treatment with anti-IFN-gamma monoclonal antibody before CLP significantly reduced the effects of PSK. These findings suggest that the protective effect of PSK on the CLP-induced sepsis in mice transplanted orthotopically with C26 tumor is possibly mediated by suppression of IL-10 and promotion of IFN-gamma.

Animals↗

PubMed2006

Interaction of LDL receptor-related protein 4 (LRP4) with postsynaptic scaffold proteins via its C-terminal PDZ domain-binding motif, and its regulation by Ca/calmodulin-dependent protein kinase II.

We cloned here a full-length cDNA of Dem26[Tian et al. (1999)Mol. Brain Res., 72, 147-157], a member of the low-density lipoprotein (LDL) receptor gene family from the rat brain. We originally named the corresponding protein synaptic LDL receptor-related protein (synLRP) [Tian et al. (2002) Soc. Neurosci. Abstr., 28, 405] and have renamed it LRP4 to accord it systematic nomenclature (GenBank(TM) accession no. AB073317). LRP4 protein interacted with postsynaptic scaffold proteins such as postsynaptic density (PSD)-95 via its C-terminal tail sequence, and associated with N-methyl-D-aspartate (NMDA)-type glutamate receptor subunit. The mRNA of LRP4 was localized to dendrites, as well as somas, of neuronal cells, and the full-length protein of 250 kDa was highly concentrated in the brain and localized to various subcellular compartments in the brain, including synaptic fractions. Immunocytochemical study using cultured cortical neurons suggested surface localization in the neuronal cells both in somas and dendrites. Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) phosphorylated the C-terminal cytoplasmic region of LRP4 at Ser1887 and Ser1900, and the phosphorylation at the latter site suppressed the interaction of the protein with PSD-95 and synapse-associated protein 97 (SAP97). These findings suggest a postsynaptic role for LRP4, a putative endocytic multiligand receptor, and a mechanism in which CaMKII regulates PDZ-dependent protein-protein interactions and receptor dynamics.

Animals↗

PubMed2006

[Experimental chemotherapy against human esophageal carcinoma xenografts with TS-1, cisplatin and docetaxel].

Three strains of human esophageal carcinoma xenografts established in our institution were tested against combination chemotherapy in vivo and in vitro. TS-1 plus cisplatin (CDDP) was shown to be an effective combination against two carcinoma strains of moderately-differentiated type. Determination of the thymidylate synthase (TS) demonstrated a higher inhibition of the enzyme by adding CDDP to 5-FU, suggesting biochemical modulation. The remaining strain of poorly-differentiated type was resistant to the combination and an attempt was made to add docetaxel (DTX) to show that the three-drug combination was effective against the strain. Combination chemotherapy including TS-1 and CDDP thus appears to be useful treatment choice for esophageal carcinoma.

Animals↗

PubMed2005

Involvement of the virulence gene products of Yersinia enterocolitica in the immune response of infected mice.

The virulence of Yersinia enterocolitica is known to be highly dependent on its virulence plasmid. However, it remains unclear whether the virulence plasmid is engaged also in the induction of cell-mediated immunity that is essential for protective immunity in the host. In this study, we have compared the induction of type 1 helper T cell immunity against Y. enterocolitica using a virulent strain (P+) harboring the pYV plasmid and an avirulent strain (P-) harboring no pYV. Spleen cells from both groups of mice immunized with 1/10 LD50 of P+ strain and those with 1/10 LD50 of P- strain produced a high level of gamma interferon (IFN-gamma) upon stimulation with heat-killed bacteria, and CD4+ T cells were exclusively responsible for IFN-gamma production. When crude Yersinia outer proteins (Yops) were used for antigenic stimulation, IFN-gamma response of immune spleen cells against crude Yops was observed only in mice immunized with P+ strain. Flowcytometric analysis revealed a significant level of increase in IFN-gamma-producing CD8+ T cells as well as the increase in IFN-gamma-producing CD4+ T cells against crude Yops. These results suggest that the virulence plasmid of Y. enterocolitica is involved in the induction of Th1-type of possibly protective T cells in infected mice.

Animals↗

PubMed2005

p55 protein is a member of PSD scaffold proteins in the rat brain and interacts with various PSD proteins.

p55 is a membrane-associated guanylate kinase (MAGuK) family member that consists of a single PDZ followed by SH3, HOOK and guanylate kinase (GuK or GK) domains. We investigated rat p55 (r-p55) in the brain. r-p55 mRNA was expressed widely in various tissues and in various regions of the brain. r-p55 protein was also expressed widely in various rat tissues, including brain and erythrocytes. The protein was enriched in the synaptic plasma membrane and postsynaptic density (PSD) fractions of the forebrain. An immunocytochemical study using cultured cortical neurons suggested postsynaptic localization of r-p55 protein. Pull-down assay showed that r-p55 protein interacted with r-p55 itself and various PSD proteins, such as PSD-95, SAP97, GKAP, CASK, GRIP, neuroligin, cadherin, tubulin, actin, alpha-internexin, neurofilament-L and Ca(2+)/calmodulin-dependent protein kinase II, through its PDZ, SH3, HOOK or GK domains. The interaction with PSD-95 was found to occur between the PDZ domains of PSD-95 and the HOOK and GK domains of r-p55 protein. These findings, together with the presence of r-p55 puncta in a period of early synaptogenesis, suggest that r-p55 protein functions as one of postsynaptic scaffold component in an early stage of synaptogenesis in the brain. r-p55 protein may form a basic structure, which interlinks diverse functional molecules of the PSD necessary for postsynaptic signaling and synaptic adhesion.

Amino Acid Sequence↗

PubMed2005

Oral administration of bovine colostrum stimulates intestinal intraepithelial lymphocytes to polarize Th1-type in mice.

Th1 stimulus for Th2-skewed immune response during infancy is important for reduction of incidence of allergic diseases. We examined effects of oral administration of bovine colostrum on local immunity in intestine in adult mice. C57BL/6 mice were orally given bovine colostrum or control milk for 1, 3 or 6 months and intestinal microflora, fecal IgA, and lymphocyte population of gut-associated lymphoid tissues and their abilities of cytokine production were examined. Although the cell populations of intestinal intraepithelial lymphocytes (i-IEL) were not remarkably changed, the T cells in i-IEL were polarized to Th1 type after oral administration of bovine colostrum. Intestinal microflora and IgA levels in feces were not changed by oral administration of bovine colostrum. These results suggest that colostrum stimulates directly to i-IEL to polarize Th1 type, which may protect from infectious diseases and allergic diseases mediated by Th2 type responses.

Administration, Oral↗

PubMed2005

Nonpathogenic Escherichia coli strain Nissle1917 prevents murine acute and chronic colitis.

BACKGROUND: Nonpathogenic Escherichia coli strain Nissle1917 has been used as a probiotics in human inflammatory bowel disease; however, there are few reports examining its therapeutic effect on animal colitis models, and its therapeutic mechanisms remain unknown. The aim of this study was to elucidate the therapeutic effect and mechanism of Nissle1917 using murine acute and chronic colitis models. METHODS: Two models were used. (1) Acute model: colitis was induced by administration of 1.3% dextran sodium sulfate for 7 days. Nissle1917 or phosphate-buffered saline were orally administered for 10 days. Mice were killed at day 10, and the colonic lesions were assessed macro- and microscopically. (2) Chronic model: IL-10 mice were treated with Nissle1917 or phosphate-buffered saline for 8 weeks. After 8 weeks of treatment, mice were killed to assess the colonic lesions macro- and microscopically. In the acute dextran sodium sulfate colitis model, viable, heat-killed, or genomic DNA of Nissle1917 was orally administered for 10 days, and the therapeutic effect was assessed. RESULTS: In the acute model, Nissle1917 ameliorated body weight loss, disease activity index, and macro- and microscopic damage. In the chronic model, it also suppressed the mucosal inflammatory findings and histologic damages. Moreover, heat-killed Nissle1917 or its genomic DNA alone also ameliorated the acute DSS colitis and viable bacteria macro- and microscopically. CONCLUSIONS: Nonpathogenic E. coli strain Nissle1917 prevents both acute and chronic colitis, and its anti-inflammatory effect is exhibited not only by viable bacteria but also by heat-killed bacteria or its DNA.

Acute Disease↗

PubMed2005

A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins.

We cloned from the rat brain a novel gene, tanc (GenBank Accession No. AB098072), which encoded a protein containing three tetratricopeptide repeats (TPRs), ten ankyrin repeats and a coiled-coil region, and is possibly a rat homolog of Drosophila rolling pebbles (rols). The tanc gene was expressed widely in the adult rat brain. Subcellular distribution, immunohistochemical study of the brain and immunocytochemical studies of cultured neuronal cells indicated the postsynaptic localization of TANC protein of 200 kDa. Pull-down experiments showed that TANC protein bound PSD-95, SAP97, and Homer via its C-terminal PDZ-binding motif, -ESNV, and fodrin via both its ankyrin repeats and the TPRs together with the coiled-coil domain. TANC also bound the alpha subunit of Ca2+/calmodulin-dependent protein kinase II. An immunoprecipitation study showed TANC association with various postsynaptic proteins, including guanylate kinase-associated protein (GKAP), alpha-internexin, and N-methyl-D-aspartate (NMDA)-type glutamate receptor 2B and AMPA-type glutamate receptor (GluR1) subunits. These results suggest that TANC protein may work as a postsynaptic scaffold component by forming a multiprotein complex with various postsynaptic density proteins.

Age Factors↗

PubMed2005

BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N-terminal myristoylation and palmitoylation, and interacts with alpha, but not beta, subunit of Ca/calmodulin-dependent protein kinase II.

We cloned a rat BAALC 1-6-8 isoform cDNA (GenBank Accession No. AB073318) that encoded a 22-kDa protein, and identified endogenous BAALC 1-6-8 protein in the brain. The gene was expressed widely in the frontal part of the brain, and the protein was localized to the synaptic sites and was increased in parallel with synaptogenesis. The protein interacted with the alpha, but not beta, subunit of Ca(2+)/calmodulin-dependent protein kinase II (CaMKIIalpha). The interaction occurred between the N-terminal 35-amino-acid region of BAALC 1-6-8 protein and the C-terminal end of the regulatory domain of CaMKIIalpha, which contains alpha isoform-specific sequence. Thus, the interaction may be CaMKIIalpha-specific. We also found that BAALC 1-6-8 protein, as well as CaMKIIalpha, was localized to lipid rafts and that both myristoylation and palmitoylation of BAALC 1-6-8 N-terminal portion were required for targeting of the protein into lipid rafts. These findings suggest that BAALC 1-6-8 protein play a synaptic role at the postsynaptic lipid raft possibly through interaction with CaMKIIalpha.

Alternative Splicing↗

PubMed2005

Conventional HPLC method used for simultaneous determination of the seven HIV protease inhibitors and nonnucleoside reverse transcription inhibitor efavirenz in human plasma.

We developed a simple HPLC method for the simultaneous quantitative determination of seven HIV protease inhibitors: amprenavir (APV), atazanavir (ATV), indinavir (IDV), lopinavir (LPV), nelfinavir (NFV), ritonavir (RTV), saquinavir (SQV), and a nonnucleoside reverse transcription inhibitor, efavirenz (EFV). This method involves a rapid liquid-liquid drug extraction from plasma, the use of an isocratic elution on a reversed-phase C18 column, and an ultraviolet detection at a single wavelength (205 nm). The mobile phase consisted of 39% 50 mM phosphate buffer (pH 5.9), 22% methanol and 39% acetonitrile. Forty-eight samples could be measured in one day since the runtime of one sample is 30 min. The assay has been validated over a concentration range of 0.05 to 12.20 microg/ml for APV, 0.09 to 12.05 microg/ml for ATV, 0.05 to 12.01 microg/ml for IDV, 0.12 to 12.36 microg/ml for LPV, 0.18 to 12.20 microg/ml for NFV, 0.12 to 12.33 microg/ml for RTV, 0.12 to 12.06 microg/ml for SQV, and 0.05 to 12.17 microg/ml for EFV. Calibration curves were linear in the described concentration ranges. The average accuracy ranged from 97.2 to 106.8%. Both the interday and intraday coefficients of variation for all drugs tested were less than 8.5%. This method provides a simple, accurate, and precise method for the therapeutic drug monitoring of the seven protease inhibitors and EFV in clinical routine use.

Alkynes↗

PubMed2005

Mucosal immunity of nasopharynx: an experimental study in TCR-transgenic (OVA23-3) mice.

The ideal vaccine therapy has been warranted for activation of the mucosal immune response in the upper respiratory tract against various types of microbial infection. However, the precise study in regard to the mucosal route of vaccine administration and its mechanism of action remains to be further investigated. Therefore, to better understand the exact mechanism of nasopharyngeal mucosal immunology, from T-cell aspects, the antigen-specific antibody response was investigated in T cell receptor transgenic (OVA23-3) mice (Tg-mice) and wild type BALB/c mice, in comparison, which were stimulated with repeated nasal antigen challenges of ovalbumin (OVA) together with cholera toxin (CT) or OVA alone. OVA-specific IgA and IgG antibodies were not detected in nasal washings of BALB/c mice when these mice were intranasally stimulated with OVA alone. But they were detected in those of BALB/c mice stimulated with OVA and CT, as we have already reported. Interestingly, OVA-specific IgA and IgG antibodies were significantly higher in nasal washings of Tg-mice stimulated with OVA and CT or OVA alone rather than those of BALB/c mice stimulated with OVA and CT. In line with data of the antibody response, OVA-specific IgA and IgG antibody-producing cells significantly increased in number in nasal passage (NP), nasopharyngeal-associated lymphoreticular tissue (NALT), cervical lymph node (CLN), and spleen (SP) of these mice. In nasal washings of Tg-mice, interferon (IFN)-gamma and interleukin (IL)-4 was detected even with a small amount of antigen. To see the cytokine profile of NALT, NP, CLN, and SP of these mice, various cytokine concentrations were measured in supernatants of these cells cultured in vitro with OVA. As a result, IFN-gamma was detected at significantly higher levels in culture supernatants of lymphocytes sampled from NP, CLN, SP as well as NALT of mice having increased antibody titers in nasal washings. On the other hand, Th2 type cytokines such as IL-4, IL-6 and IL-13 were efficiently detected in culture supernatants of NP, CLN, and SP cells from Tg-mice mice, but not in those from NALT cells of those mice. All these data taken together indicate that helper T cells recruited into nasal mucosa and locally activated in an antigen-specific fashion, as well as NALT T cells, are essential for mounting local antigen-specific antibody responses.

Animals↗

PubMed2004

NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity.

Targeting of neuronal nitric-oxide synthase (nNOS) to appropriate sites in a cell is mediated by interactions with its PDZ domain and plays an important role in specifying the sites of reaction of nitric oxide (NO) in the central nervous system. Here we report the identification and characterization of a novel nNOS-interacting DHHC domain-containing protein with dendritic mRNA (NIDD) (GenBank accession number AB098078), which increases nNOS enzyme activity by targeting the nNOS to the synaptic plasma membrane in a PDZ domain-dependent manner. The deduced NIDD protein consisted of 392 amino acid residues and possessed five transmembrane segments, a zinc finger DHHC domain, and a PDZ-binding motif (-EDIV) at its C-terminal tail. In vitro pull-down assays suggested that the C-terminal tail region of NIDD specifically interacted with the PDZ domain of nNOS. The PDZ dependence was confirmed by an experiment using a deletion mutant, and the interaction was further confirmed by co-sedimentation assays using COS-7 cells transfected with NIDD and nNOS. Both NIDD and nNOS were enriched in synaptosome and synaptic plasma membrane fractions and were present in the lipid raft and postsynaptic density fractions in the rat brain. Co-localization of these proteins was also observed by double staining of the proteins in cultured cortical neurons. Thus, NIDD and nNOS were co-localized in the brain, although the colocalizing regions were restricted, as indicated by the distribution of their mRNA expression. Most important, co-transfection of NIDD and nNOS increased NO-producing nNOS activity. These results suggested that NIDD plays an important role in the regulation of the NO signaling pathway at postsynaptic sites through targeting of nNOS to the postsynaptic membrane.

Amino Acid Sequence↗

PubMed2004

Brain-specific potential guanine nucleotide exchange factor for Arf, synArfGEF (Po), is localized to postsynaptic density.

We cloned from a rat brain cDNA library a novel cDNA and named it a potential synaptic guanine nucleotide exchange factor (GEF) for Arf (synArfGEF (Po)) (GenBank Accession no. AB057643) based on its domain structure and localization. The cloned gene was 7410 bases long with a 3585-bp coding sequence encoding a protein of 1194 amino acids. The deduced protein contained a coiled-coil structure in the N-terminal portion followed by Sec7 and Plekstrin homology (PH) domains. Thus, the protein was a member of the Sec7 family of proteins, GEFs. Conservation of the ADP-ribosylation factor (Arf)-binding sequence suggested that the protein was a GEF for Arf. The gene was expressed specifically in the brain, where it exhibited region-specific expression. The protein was highly enriched in the postsynaptic density (PSD) fraction prepared from the rat forebrain. Uniquely, the protein interacted with PSD-95, SAP97 and Homer/Vesl 1/PSD-Zip45 via its C-terminal PDZ-binding motif and co-localized with these proteins in cultured cortical neurons. These results supported its localization in the PSD. The postsynaptic localization was also supported by immunohistochemical examination of the rat brain. The mRNA for the synArfGEF was also localized to dendrites, as well as somas, of neuronal cells. Thus, both the mRNA and the protein were localized in the postsynaptic compartments. These results suggest a postsynaptic role of synArfGEF in the brain.

ADP-Ribosylation Factors↗

PubMed2004

[Identification of novel PSD proteins and their possible functions].

There are a number of mRNA species localizing to dendrites of neuronal cells, and a postsynaptic local translation system may allow local and rapid synthesis of key postsynaptic proteins required for expression of synaptic plasticity. Most mRNAs localizing in the postsynaptic region may be translated into postsynaptic proteins, localizing in the postsynaptic subcompartments, such as PSD, the synaptic plasma membrane (SPM), or the cytoplasmic region of the spines or dendrites. However, there appears to be a number of dendritic mRNAs (Dems) and postsynaptic proteins still to be found. Recently, we developed a method to identify a large number of mRNA species associated with PSD fraction (Tian et al (1999) Mol Brain Res, 72: 147-157). During the identification process of these mRNAs, we cloned several full-length cDNAs, such as a synaptic short form LDL receptor-related protein (ssLRP) (Tian et al (2002) Soc Neurosci Abst, 28: 405), synaptic ubiquitin-specific protease (synUSP), TANC (a protein containing tetratricopeptide repeat [TPR], ankyrin repeat, and coiled-coil domain) (Suzuki et al (2003) Soc Neurosci Abst, 29), and so forth. In situ hybridization and immunochemical studies confirmed dendritic localization of mRNAs for these proteins in dendrites, and the localization of these proteins in postsynaptic regions, respectively. Some proteins contained signals for targeting the PSD and interacted with various PSD proteins. We present properties and possible physiological functions of these proteins and report the recent progress in our project to identify a large number of postsynaptic proteins based on the identification of dendritically localizing mRNAs.

Guanine Nucleotide Exchange Factors↗

PubMed2003

Localization of translational components at the ultramicroscopic level at postsynaptic sites of the rat brain.

We investigated the localization of components of translational machinery and their regulators in the postsynaptic region. We examined several components, especially those involved in translational regulation: components of (1) MAPK-Mnk-eIF4E, (2) PI3-kinase-PDK-Akt/PKB-FRAP/mTOR-PHAS/4EBP, (3) p70S6K-S6 ribosomal protein and (4) eEF2 kinase/CaMKIII-eEF2 pathways. Western blotting detected all the components examined in the synaptic fractions, and their differential localization to the synaptic subcompartments: initiation or elongation factors, except for eIF5, were detected predominantly in the dendritic lipid raft fraction, which contained ER marker proteins. In contrast, most of their regulatory kinases were distributed to both the postsynaptic density (PSD) and the dendritic lipid raft fractions, or enriched in the former fraction. Localization of eIF4E at synaptic sites was further examined immunohistochemically at the electron microscopic level. The eIF-4E-immunoreactivity was localized to the postsynaptic sites, especially to the microvesicle-like structures underneath the postsynaptic membrane in the spine, some of which were localized in close proximity to PSD. These results suggest that the postsynaptic local translational system, in at least four major regulatory pathways, is similar to those in the perinuclear one, and that it takes place, at least partly, immediately beneath the postsynaptic membrane. The results also suggest the presence of ER-associated type of translational machinery at the postsynaptic sites.

Animals↗

PubMed2003

Huntingtin-interacting protein-1-related protein of rat (rHIP1R) is localized in the postsynaptic regions.

We cloned a rHIP1R (GenBank Accession No., AB005052) encoding a Sla2/huntingtin-interacting protein (HIP1) family protein from a rat brain cDNA library. Localization of rHIP1R was investigated in the rat brain using an antibody specific to the HIP1R antibody. The rHIP1R protein was enriched in the synaptic plasma membrane fraction along with huntingtin, a synaptic protein and a causal protein for Huntington's disease. The electron microscopic examination revealed that HIP1R was localized at postsynaptic spines. Localization of HIP1R in the small vesicular structures in the spine, possible sites of vesicular transport of synaptic proteins, together with the structure-based analysis, suggested a role of HIP1R for vesicle trafficking through interaction with F-actin and working together with huntingtin and HIP1 at the synaptic sites.

Adaptor Proteins, Signal Transducing↗