SCAMP5 Plays a Critical Role in Synaptic Vesicle Endocytosis during High Neuronal Activity

Zhao, Haixia; Kim, Yoonju; Park, Joo Hyun; Park, Daehun; Lee, Sang-Eun; Chang, Iree; Chang, Sunghoe

doi:10.1523/jneurosci.2156-14.2014

Cited by 33 publications

(42 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4. Seven pathways had experimentally validated relationships with autism, including the Wnt signaling pathway, cell cycle, p53 signaling pathway, MAPK signaling pathway, glioma signaling pathway, endocytosis, and neurotrophin signaling pathway40414243. In addition, two pathways (i.e., adherens junction and TGF-beta signaling pathway) were confirmed by computational methods44.…”

Section: Resultsmentioning

confidence: 96%

“…During endocytosis, the SCAMP5 gene is essential when the neuronal activity is high, where it might control the recycling of synaptic vesicles, and thus it could maintain sufficient endocytosis during intense neuronal activity. Thus, the knockdown of SCAMP5 would have negative effects on neuronal functions and lead to synaptic dysfunction43. Moreover, brain-derived neurotrophic factor (BDNF) in the neurotrophin signaling pathway plays vital roles in neurodevelopmental and neurodegenerative diseases52.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Knowledge-Guided Bioinformatics Model for Identifying Autism Spectrum Disorder Diagnostic MicroRNA Biomarkers

Shen

Lin

Sun

et al. 2016

Sci Rep

View full text Add to dashboard Cite

Autism spectrum disorder (ASD) is a severe neurodevelopmental disease with a high incidence and effective biomarkers are urgently needed for its diagnosis. A few previous studies have reported the detection of miRNA biomarkers for autism diagnosis, especially those based on bioinformatics approaches. In this study, we developed a knowledge-guided bioinformatics model for identifying autism miRNA biomarkers. We downloaded gene expression microarray data from the GEO Database and extracted genes with expression levels that differed in ASD and the controls. We then constructed an autism-specific miRNA–mRNA network and inferred candidate autism biomarker miRNAs based on their regulatory modes and functions. We defined a novel parameter called the autism gene percentage as autism-specific knowledge to further facilitate the identification of autism-specific biomarker miRNAs. Finally, 11 miRNAs were screened as putative autism biomarkers, where eight miRNAs (72.7%) were significantly dysregulated in ASD samples according to previous reports. Functional enrichment results indicated that the targets of the identified miRNAs were enriched in autism-associated pathways, such as Wnt signaling (in KEGG and IPA), cell cycle (in KEGG), and glioblastoma multiforme signaling (in IPA), thereby supporting the predictive power of our model.

show abstract

Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

Knowledge-Guided Bioinformatics Model for Identifying Autism Spectrum Disorder Diagnostic MicroRNA Biomarkers

Shen

Lin

Sun

et al. 2016

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Endocytosis during stimulation was derived by subtracting the vGluT1‐pH fluorescence in the absence of Baf from that in the presence of Baf after the subtraction of the spontaneous release (ΔF endo = ΔF exo ‐ΔF exo‐endo ), as indicated previously (Zhao et al . ). The rate of exocytosis and endocytosis during stimulation were obtained from the linear fits to the data.…”

Section: Methodsmentioning

confidence: 97%

Brefeldin A sensitive mechanisms contribute to endocytotic membrane retrieval and vesicle recycling in cerebellar granule cells

Rampérez

Sánchez‐Prieto

Torres

2017

Journal of Neurochemistry

View full text Add to dashboard Cite

The recycling of synaptic vesicle (SV) proteins and transmitter release occur at multiple sites along the axon. These processes are sensitive to inhibition of the small GTP binding protein ARF1, which regulates the adaptor protein 1 and 3 complex (AP-1/AP-3). As the axon matures, SV recycling becomes restricted to the presynaptic bouton, and its machinery undergoes a complex process of maturation. We used the styryl dye FM1-43 to highlight differences in the efficiency of membrane recycling at different sites in cerebellar granule cells cultured for 7 days in vitro. We used Brefeldin A (BFA) to inhibit AP-1/AP-3-mediated recycling and to test the contribution of this pathway to the heterogeneity of the responses when these cells are strongly stimulated. Combining imaging techniques and ultrastructural analyses, we found a significant decrease in the density of functional boutons and an increase in the presence of endosome-like structures within the boutons of cells incubated with BFA prior to FM1-43 loading. Such effects were not observed when BFA was added 5 min after the end of the loading step, when endocytosis was almost fully completed. In this situation, vesicles were found closer to the active zone (AZ) in boutons exposed to BFA. Together, these data suggest that the AP-1/AP-3 pathway contributes to SV recycling, affecting different steps in all boutons but not equally, and thus being partly responsible for the heterogeneity of the different recycling efficiencies. Cover Image for this issue: doi. 10.1111/jnc.13801.

show abstract

“…nArgBP2 KD was carried out by expressing shRNA duplexes through a pSIREN-DNR-DsRed vector. Primary rat hippocampal or cortical neurons derived from E18 Sprague-Dawley fetal rats were prepared as described previously (53). Images were analyzed using MetaMorph software and ImageJ.…”

Section: Methodsmentioning

confidence: 99%

nArgBP2 regulates excitatory synapse formation by controlling dendritic spine morphology

Lee

Kim

Han

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Neural Abelson-related gene-binding protein 2 (nArgBP2) was originally identified as a protein that directly interacts with synapseassociated protein 90/postsynaptic density protein 95-associated protein 3 (SAPAP3), a postsynaptic scaffolding protein critical for the assembly of glutamatergic synapses. Although genetic deletion of nArgBP2 in mice leads to manic/bipolar-like behaviors resembling many aspects of symptoms in patients with bipolar disorder, the actual function of nArgBP2 at the synapse is completely unknown. Here, we found that the knockdown (KD) of nArgBP2 by specific small hairpin RNAs (shRNAs) resulted in a dramatic change in dendritic spine morphology. Reintroducing shRNA-resistant nArgBP2 reversed these defects. In particular, nArgBP2 KD impaired spinesynapse formation such that excitatory synapses terminated mostly at dendritic shafts instead of spine heads in spiny neurons, although inhibitory synapse formation was not affected. nArgBP2 KD further caused a marked increase of actin cytoskeleton dynamics in spines, which was associated with increased Wiskott-Aldrich syndrome protein-family verprolin homologous protein 1 (WAVE1)/p21-activated kinase (PAK) phosphorylation and reduced activity of cofilin. These effects of nArgBP2 KD in spines were rescued by inhibiting PAK or activating cofilin combined with sequestration of WAVE. Together, our results suggest that nArgBP2 functions to regulate spine morphogenesis and subsequent spine-synapse formation at glutamatergic synapses. They also raise the possibility that the aberrant regulation of synaptic actin filaments caused by reduced nArgBP2 expression may contribute to the manifestation of the synaptic dysfunction observed in manic/bipolar disorder. nArgBP2 | dendritic spines | excitatory synapse | actin | bipolar disorder T he postsynaptic enriched adaptor protein neural Abelsonrelated gene-binding protein 2 (nArgBP2), a neural-specific splice variant of the ubiquitous ArgBP2, was originally identified as a binding partner of synapse-associated protein 90/postsynaptic density protein 95-associated protein 3 (SAPAP3) (1). It belongs to a family of adaptor proteins that are involved in the regulation of cell adhesion, actin cytoskeleton organization, and growth factor receptor signaling (2). This protein family is characterized by a sorbin homology (SoHo) domain in the NH 2 -terminal region and three Src homology 3 (SH3) domains in the COOH-terminal region (3). Although the SoHo domain remains poorly characterized, the SH3 domains bind signaling protein kinases, the ubiquitin ligase, and protein involved in the regulation of focal adhesions and adhering junctions (1, 4-6). The NH 2 -terminal region of nArgBP2, which contains the SoHo domain, interacts with spectrin, whereas the COOH-terminal SH3 domains bind dynamin, synaptojanin, Wiskott-Aldrich syndrome protein-family verprolin homologous protein (WAVE) isoforms, and WAVE regulatory proteins (3), all of which participate in the regulation of the actin cytoskeleton. We also found that the down-re...

show abstract

SCAMP5 Plays a Critical Role in Synaptic Vesicle Endocytosis during High Neuronal Activity

Cited by 33 publications

References 41 publications

Knowledge-Guided Bioinformatics Model for Identifying Autism Spectrum Disorder Diagnostic MicroRNA Biomarkers

Knowledge-Guided Bioinformatics Model for Identifying Autism Spectrum Disorder Diagnostic MicroRNA Biomarkers

Brefeldin A sensitive mechanisms contribute to endocytotic membrane retrieval and vesicle recycling in cerebellar granule cells

nArgBP2 regulates excitatory synapse formation by controlling dendritic spine morphology

Contact Info

Product

Resources

About