uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Mover is a homomeric phospho-protein present on synaptic vesicles
Show others and affiliations
2013 (English)In: PLoS ONE, ISSN 1932-6203, Vol. 8, no 5, e63474- p.Article in journal (Refereed) Published
Abstract [en]

With remarkably few exceptions, the molecules mediating synaptic vesicle exocytosis at active zones are structurally and functionally conserved between vertebrates and invertebrates. Mover was found in a yeast-2-hybrid assay using the vertebrate-specific active zone scaffolding protein bassoon as a bait. Peptides of Mover have been reported in proteomics screens for self-interacting proteins, phosphorylated proteins, and synaptic vesicle proteins, respectively. Here, we tested the predictions arising from these screens. Using flotation assays, carbonate stripping of peripheral membrane proteins, mass spectrometry, immunogold labelling of purified synaptic vesicles, and immuno-organelle isolation, we found that Mover is indeed a peripheral synaptic vesicle membrane protein. In addition, by generating an antibody against phosphorylated Mover and Western blot analysis of fractionated rat brain, we found that Mover is a bona fide phospho-protein. The localization of Mover to synaptic vesicles is phosphorylation dependent; treatment with a phosphatase caused Mover to dissociate from synaptic vesicles. A yeast-2-hybrid screen, co-immunoprecipitation and cell-based optical assays of homomerization revealed that Mover undergoes homophilic interaction, and regions within both the N- and C- terminus of the protein are required for this interaction. Deleting a region required for homomeric interaction abolished presynaptic targeting of recombinant Mover in cultured neurons. Together, these data prove that Mover is associated with synaptic vesicles, and implicate phosphorylation and multimerization in targeting of Mover to synaptic vesicles and presynaptic sites.

Place, publisher, year, edition, pages
2013. Vol. 8, no 5, e63474- p.
National Category
Cell Biology
URN: urn:nbn:se:uu:diva-224163DOI: 10.1371/journal.pone.0063474PubMedID: 23723986OAI: oai:DiVA.org:uu-224163DiVA: diva2:715598
Available from: 2014-05-05 Created: 2014-05-05 Last updated: 2014-09-18Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Hoeber, Jan
In the same journal
Cell Biology

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 162 hits
ReferencesLink to record
Permanent link

Direct link