Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Nanoscopic spine localization of Norbin, an mGluR5 accessory protein
KTH, Skolan för teknikvetenskap (SCI), Tillämpad fysik. KTH, Centra, Science for Life Laboratory, SciLifeLab.
Vise andre og tillknytning
2014 (engelsk)Inngår i: BMC neuroscience (Online), ISSN 1471-2202, E-ISSN 1471-2202, Vol. 15, s. 45-Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Background: Norbin is a neuron-specific, cytosolic protein that interacts with the metabotropic glutamate receptor 5 (mGluR5) and has a profound impact on mGluR5 signaling. Yet, little is known about its synaptic distribution. Results: Here we have analyzed the spatial relationship between Norbin, postsynaptic density protein 95 (PSD-95), actin and mGluR5 in spines using super-resolution microscopy. Norbin was found to have a high degree of colocalization with actin and a lower degree of colocalization with PSD-95. Co-immunoprecipitation studies confirmed that interaction occurs between Norbin and actin, but not between Norbin and PSD-95. Norbin was also found to have a high degree of colocalization with the perisynaptically located mGluR5. Findings based on structured illumination microscopy (3D-SIM) of exogenous expressed Norbin-GFP were confirmed by stimulated emission depletion microscopy (STED) of immunolabeled endogenous Norbin. Conclusions: Norbin associates with actin rather than with PSD-95 in dendritic spines. Results regarding protein localization and colocalization performed with conventional confocal microscopy must be interpreted with great caution. The now available super-resolution microscopy techniques provide more accurate information about sub-cellular protein localization than previously was possible.

sted, utgiver, år, opplag, sider
BioMed Central, 2014. Vol. 15, s. 45-
Emneord [en]
Super-resolution microscopy, Colocalization, Norbin, Dendritic spines
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-145606DOI: 10.1186/1471-2202-15-45ISI: 000334951100001Scopus ID: 2-s2.0-84897525805OAI: oai:DiVA.org:kth-145606DiVA, id: diva2:719205
Forskningsfinansiär
Swedish Research CouncilScience for Life Laboratory - a national resource center for high-throughput molecular bioscience
Merknad

QC 20140523

Tilgjengelig fra: 2014-05-23 Laget: 2014-05-23 Sist oppdatert: 2018-01-11bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstScopus

Personposter BETA

Brismar, Hjalmar

Søk i DiVA

Av forfatter/redaktør
Reuss, MatthiasBrismar, Hjalmar
Av organisasjonen
I samme tidsskrift
BMC neuroscience (Online)

Søk utenfor DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric

doi
urn-nbn
Totalt: 210 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf