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Pluripotency transcription factor Sox2 is strongly adsorbed by heparin but requires a protein transduction domain for cell internalization

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dc.contributor.authorAlbayrak, CEM
dc.contributor.authorYang, William C.
dc.contributor.authorSwartz, James R.
dc.contributor.institutionauthorALBAYRAK, CEM
dc.date.accessioned2021-05-17T20:59:09Z
dc.date.available2021-05-17T20:59:09Z
dc.date.issued2013-02-01T00:00:00Z
dc.description.abstractThe binding of protein transduction domain (PTD)-conjugated proteins to heparan sulfate is an important step in cellular internalization of macromolecules. Here, we studied the pluripotency transcription factor Sox2, with or without the nonaarginine (R9) PTD. Unexpectedly, we observed that Sox2 is strongly adsorbed by heparin and by the fibroblasts without the R9 PTD. However, only the R9Sox2 fusion protein is internalized by the cells. These results collectively show that binding to heparan sulfate is not sufficient for cellular uptake, thereby supporting a recent hypothesis that other proteins play a role in cell internalization of PTD-conjugated proteins. (C) 2012 Elsevier Inc. All rights reserved.
dc.identifier.citationAlbayrak C., Yang W. C. , Swartz J. R. , -Pluripotency transcription factor Sox2 is strongly adsorbed by heparin but requires a protein transduction domain for cell internalization-, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, cilt.431, sa.3, ss.641-645, 2013
dc.identifier.doi10.1016/j.bbrc.2012.11.016
dc.identifier.pubmed23318174
dc.identifier.scopus84873705208
dc.identifier.urihttp://hdl.handle.net/20.500.12645/28882
dc.identifier.wosWOS:000315842800047
dc.titlePluripotency transcription factor Sox2 is strongly adsorbed by heparin but requires a protein transduction domain for cell internalization
dc.typeArticle
dspace.entity.typePublication
local.avesis.id4b277e53-fdcc-47a3-8d07-7bcdfa3f622b
local.indexed.atPubMed
local.indexed.atWOS
local.indexed.atScopus
local.publication.isinternational1
relation.isAuthorOfPublicationced2804c-b9e5-4f25-9926-74404ade4f49
relation.isAuthorOfPublication.latestForDiscoveryced2804c-b9e5-4f25-9926-74404ade4f49

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