Cellular and Molecular Neurobiology<\/p>\n
Author:<\/strong> Maria Bel\u00e9n Montiel | Email:<\/strong> mariabelenmontiel@gmail.com<\/p>\n Maria Bel\u00e9n Montiel 1\u00b0<\/sup>, Nicol\u00e1s Matias Rosas 1\u00b0<\/sup>, Beata Fuchsova 1\u00b0<\/sup><\/p>\n 1\u00b0 Instituto de Investigaciones Biotecnol\u00f3gicas, Escuela de Bio y Nanotecnolog\u00edas (EByN), Universidad Nacional de San Mart\u00edn (UNSAM) \u0096 Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas (CONICET), San Mart\u00edn, Buenos Aires, Argentina<\/p>\n Gpm6a is a neuronal membrane glycoprotein that functions in the processes of neuronal Author: Montiel Maria Bel\u00e9n | email: mariabelenmontiel@gmail.com | Cellular and Molecular Neurobiology<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[34],"tags":[18],"class_list":["post-1896","post","type-post","status-publish","format-standard","hentry","category-session-2","tag-cellular-and-molecular-neurobiology"],"_links":{"self":[{"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/posts\/1896","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/comments?post=1896"}],"version-history":[{"count":1,"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/posts\/1896\/revisions"}],"predecessor-version":[{"id":2046,"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/posts\/1896\/revisions\/2046"}],"wp:attachment":[{"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/media?parent=1896"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/categories?post=1896"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/csan2023.saneurociencias.org.ar\/index.php\/wp-json\/wp\/v2\/tags?post=1896"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}
\n
\ndevelopment and its overexpression leads to the extensive formation of filopodia. Previously,
\nwe showed that Gpm6a lacking C- but not N-terminal cytoplasmic tail fails to induce
\nfilopodium formation and we identified K250, K255, and E258 within the C-terminus as the key
\nfunctional residues in this process. We observed that Gpm6a lacking C-terminus and the point
\nmutation E258A, display high accumulation in the cytosol suggesting that cell surface
\ntrafficking is affected. Since different types of membrane outgrowth, filopodia formation
\nincluding, require polarized membrane transport we hypothesized that the incapacity of the
\nmutant Gpm6a to induce filopodium formation could be linked to the disrupted trafficking of
\nmutant Gpm6a.
\nHere, we show using confocal microscopy that the mutant forms of Gpm6a that fail to
\ninduce filopodia formation display preferential localization to the Lamp1-positive structures.
\nOur colocalization assays show that the wt Gpm6a and all studied mutant proteins clearly
\nprogress from the plasma membrane to Lamp1-containing late endosomal\/ lysosomal structures
\nbut the Gpm6a ?C-EGFP and E258-EGFP mutations result in increased accumulation of
\nGpm6a in these compartments. At the same time, the overexpression of E258-EGFP leads to
\ndecreased neuronal arborization as assessed by Sholl analysis and differences in the
\ncolocalization of Gpm6a with Rab 11.<\/p>\n","protected":false},"excerpt":{"rendered":"