Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin

The Inhibitor of Apoptosis Protein survivin (svn) is upregulated in nearly all types of cancer and represents a promising therapeutic target. Localization to specific subcellular compartments and interactions with various binding partners allow survivin to play diverse roles in apoptosis resistance...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Sheila Figel, Meaghan Birkemeier, Sanam Sahjram Dharma, Tara Barone, Emma Steinmetz, Michael Ciesielski, Robert Fenstermaker
Formato: article
Lenguaje:EN
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://doaj.org/article/7384950b302c4a2e83e8329711c4cf61
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:7384950b302c4a2e83e8329711c4cf61
record_format dspace
spelling oai:doaj.org-article:7384950b302c4a2e83e8329711c4cf612021-11-22T04:27:26ZWild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin2405-580810.1016/j.bbrep.2021.101174https://doaj.org/article/7384950b302c4a2e83e8329711c4cf612021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2405580821002685https://doaj.org/toc/2405-5808The Inhibitor of Apoptosis Protein survivin (svn) is upregulated in nearly all types of cancer and represents a promising therapeutic target. Localization to specific subcellular compartments and interactions with various binding partners allow survivin to play diverse roles in apoptosis resistance and mitosis. Survivin has recently been found in two extracellular compartments: the outer plasma membrane and secreted exosomes. In addition to svn-wt, splice variants svn-dEX3 and svn-2B are also overexpressed in human tumors. Here we show that, similarly to svn-wt, svn-dEX3 and svn-2B can be displayed on the outer plasma membrane, and secreted in exosomes. Additionally, we have identified a novel interaction of all three forms of survivin with secreted tubulin.Sheila FigelMeaghan BirkemeierSanam Sahjram DharmaTara BaroneEmma SteinmetzMichael CiesielskiRobert FenstermakerElsevierarticleSurvivinSurvivin-2BSurvivin-dEX3ExosomePlasma membraneTubulinBiology (General)QH301-705.5BiochemistryQD415-436ENBiochemistry and Biophysics Reports, Vol 28, Iss , Pp 101174- (2021)
institution DOAJ
collection DOAJ
language EN
topic Survivin
Survivin-2B
Survivin-dEX3
Exosome
Plasma membrane
Tubulin
Biology (General)
QH301-705.5
Biochemistry
QD415-436
spellingShingle Survivin
Survivin-2B
Survivin-dEX3
Exosome
Plasma membrane
Tubulin
Biology (General)
QH301-705.5
Biochemistry
QD415-436
Sheila Figel
Meaghan Birkemeier
Sanam Sahjram Dharma
Tara Barone
Emma Steinmetz
Michael Ciesielski
Robert Fenstermaker
Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
description The Inhibitor of Apoptosis Protein survivin (svn) is upregulated in nearly all types of cancer and represents a promising therapeutic target. Localization to specific subcellular compartments and interactions with various binding partners allow survivin to play diverse roles in apoptosis resistance and mitosis. Survivin has recently been found in two extracellular compartments: the outer plasma membrane and secreted exosomes. In addition to svn-wt, splice variants svn-dEX3 and svn-2B are also overexpressed in human tumors. Here we show that, similarly to svn-wt, svn-dEX3 and svn-2B can be displayed on the outer plasma membrane, and secreted in exosomes. Additionally, we have identified a novel interaction of all three forms of survivin with secreted tubulin.
format article
author Sheila Figel
Meaghan Birkemeier
Sanam Sahjram Dharma
Tara Barone
Emma Steinmetz
Michael Ciesielski
Robert Fenstermaker
author_facet Sheila Figel
Meaghan Birkemeier
Sanam Sahjram Dharma
Tara Barone
Emma Steinmetz
Michael Ciesielski
Robert Fenstermaker
author_sort Sheila Figel
title Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
title_short Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
title_full Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
title_fullStr Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
title_full_unstemmed Wild type, dEX3 and 2B survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
title_sort wild type, dex3 and 2b survivin isoforms localize to the tumor cell plasma membrane, are secreted in exosomes, and interact with extracellular tubulin
publisher Elsevier
publishDate 2021
url https://doaj.org/article/7384950b302c4a2e83e8329711c4cf61
work_keys_str_mv AT sheilafigel wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
AT meaghanbirkemeier wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
AT sanamsahjramdharma wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
AT tarabarone wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
AT emmasteinmetz wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
AT michaelciesielski wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
AT robertfenstermaker wildtypedex3and2bsurvivinisoformslocalizetothetumorcellplasmamembranearesecretedinexosomesandinteractwithextracellulartubulin
_version_ 1718418167630397440