Mover is a homomeric phospho-protein present on synaptic vesicles.

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...

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Autores principales:	Saheeb Ahmed, Nina Wittenmayer, Thomas Kremer, Jan Hoeber, Asha Kiran Akula, Henning Urlaub, Markus Islinger, Joachim Kirsch, Camin Dean, Thomas Dresbach
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7731ba30286e4d8585a237756518208c
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spelling	oai:doaj.org-article:7731ba30286e4d8585a237756518208c2021-11-18T07:44:11ZMover is a homomeric phospho-protein present on synaptic vesicles.1932-620310.1371/journal.pone.0063474https://doaj.org/article/7731ba30286e4d8585a237756518208c2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23723986/?tool=EBIhttps://doaj.org/toc/1932-6203With 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.Saheeb AhmedNina WittenmayerThomas KremerJan HoeberAsha Kiran AkulaHenning UrlaubMarkus IslingerJoachim KirschCamin DeanThomas DresbachPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e63474 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Saheeb Ahmed Nina Wittenmayer Thomas Kremer Jan Hoeber Asha Kiran Akula Henning Urlaub Markus Islinger Joachim Kirsch Camin Dean Thomas Dresbach Mover is a homomeric phospho-protein present on synaptic vesicles.
description	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.
format	article
author	Saheeb Ahmed Nina Wittenmayer Thomas Kremer Jan Hoeber Asha Kiran Akula Henning Urlaub Markus Islinger Joachim Kirsch Camin Dean Thomas Dresbach
author_facet	Saheeb Ahmed Nina Wittenmayer Thomas Kremer Jan Hoeber Asha Kiran Akula Henning Urlaub Markus Islinger Joachim Kirsch Camin Dean Thomas Dresbach
author_sort	Saheeb Ahmed
title	Mover is a homomeric phospho-protein present on synaptic vesicles.
title_short	Mover is a homomeric phospho-protein present on synaptic vesicles.
title_full	Mover is a homomeric phospho-protein present on synaptic vesicles.
title_fullStr	Mover is a homomeric phospho-protein present on synaptic vesicles.
title_full_unstemmed	Mover is a homomeric phospho-protein present on synaptic vesicles.
title_sort	mover is a homomeric phospho-protein present on synaptic vesicles.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/7731ba30286e4d8585a237756518208c
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Mover is a homomeric phospho-protein present on synaptic vesicles.

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