<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Grossman GH</submitter><funding>NEI NIH HHS</funding><pagination>129-39</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3936680</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>30(4)</volume><pubmed_abstract>Dynamin proteins are involved in vesicle generation, providing mechanical force to excise newly formed vesicles from membranes of cellular compartments. In the brain, dynamin-1, dynamin-2, and dynamin-3 have been well studied; however, their function in the retina remains elusive. A retina-specific splice variant of dynamin-1 interacts with the photoreceptor-specific protein Tubby-like protein 1 (Tulp1), which when mutated causes an early onset form of autosomal recessive retinitis pigmentosa. Here, we investigated the role of the dynamins in the retina, using immunohistochemistry to localize dynamin-1, dynamin-2, and dynamin-3 and immunoprecipitation followed by mass spectrometry to explore dynamin-1 interacting proteins in mouse retina. Dynamin-2 is primarily confined to the inner segmen</pubmed_abstract><journal>Visual neuroscience</journal><pubmed_title>Protein partners of dynamin-1 in the retina.</pubmed_title><pmcid>PMC3936680</pmcid><funding_grant_id>R01 EY016072</funding_grant_id><funding_grant_id>NIH EY15638</funding_grant_id><pubmed_authors>Grossman GH</pubmed_authors><pubmed_authors>Hagstrom SA</pubmed_authors><pubmed_authors>Ebke LA</pubmed_authors><pubmed_authors>Crabb JW</pubmed_authors><pubmed_authors>Beight CD</pubmed_authors><pubmed_authors>Jang GF</pubmed_authors></additional><is_claimable>false</is_claimable><name>Protein partners of dynamin-1 in the retina.</name><description>Dynamin proteins are involved in vesicle generation, providing mechanical force to excise newly formed vesicles from membranes of cellular compartments. In the brain, dynamin-1, dynamin-2, and dynamin-3 have been well studied; however, their function in the retina remains elusive. A retina-specific splice variant of dynamin-1 interacts with the photoreceptor-specific protein Tubby-like protein 1 (Tulp1), which when mutated causes an early onset form of autosomal recessive retinitis pigmentosa. Here, we investigated the role of the dynamins in the retina, using immunohistochemistry to localize dynamin-1, dynamin-2, and dynamin-3 and immunoprecipitation followed by mass spectrometry to explore dynamin-1 interacting proteins in mouse retina. Dynamin-2 is primarily confined to the inner segmen</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Jul</publication><modification>2026-05-01T02:13:47.917Z</modification><creation>2026-04-07T16:33:55.603Z</creation></dates><accession>S-EPMC3936680</accession><cross_references><pubmed>23746204</pubmed><doi>10.1017/s0952523813000138</doi><doi>10.1017/S0952523813000138</doi></cross_references></HashMap>