Publication:
Labeling carboxyl groups of surface-exposed proteins provides an orthogonal approach for cell surface isolation

dc.contributor.coauthorTan, Edwin
dc.contributor.coauthorMitchison, Timothy
dc.contributor.departmentDepartment of Molecular Biology and Genetics
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.departmentKUTTAM (Koç University Research Center for Translational Medicine)
dc.contributor.kuauthorKüçük, Nazlı Ezgi Özkan
dc.contributor.kuauthorŞanal, Erdem
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.contributor.schoolcollegeinstituteResearch Center
dc.date.accessioned2024-11-09T23:48:02Z
dc.date.issued2018
dc.description.abstractQuantitative profiling of cell surface proteins is critically important for the understanding of cell-cell communication, signaling, tissue development, and homeostasis. Traditional proteomics methods are challenging for cell surface proteins due to their hydrophobic nature and low abundance, necessitating alternative methods to efficiently identify and quantify this protein group. Here we established carboxyl reactive biotinylation for selective and efficient biotinylation and isolation of surface-exposed proteins of living cells. We assessed the efficiency of carboxyl-reactive biotinylation for plasma membrane proteins by comparing it with a well-established protocol, amine-reactive biotinylation, using SILAC (stable isotope labeling in cell culture). Our results show that carboxyl-reactive biotinylation of cell surface proteins is both more selective and more efficient than amine-reactive biotinylation. We conclude that it is a useful approach, which is partially orthogonal to amine-reactive biotinylation, allowing us to cast a wider net for a comprehensive profiling of cell surface proteins.
dc.description.indexedbyWOS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue5
dc.description.openaccessNO
dc.description.sponsoredbyTubitakEuN/A
dc.description.sponsorshipEMBO (European Molecular Biology Organization) Installation Grant
dc.description.sponsorshipBAGEP
dc.description.sponsorshipNIH [3R01GM23928-31S1] We thank Busra Akarlar for her assistance in the mass spectrometry analysis, Nazan Saner and Aydanur Senturk for editing the manuscript, and Ozge Karayel for suggestions. N.O. is funded by EMBO (European Molecular Biology Organization) Installation Grant and BAGEP (Young Scientist Awards Program). T.M. is funded by NIH grant number 3R01GM23928-31S1.
dc.description.volume17
dc.identifier.doi10.1021/acs.jproteome.7b00825
dc.identifier.eissn1535-3907
dc.identifier.issn1535-3893
dc.identifier.scopus2-s2.0-85046161807
dc.identifier.urihttps://doi.org/10.1021/acs.jproteome.7b00825
dc.identifier.urihttps://hdl.handle.net/20.500.14288/14224
dc.identifier.wos431726700004
dc.keywordsCell surface
dc.keywordsBiotinylation
dc.keywordsPlasma membrane
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal Of Proteome Research
dc.subjectBiochemical research methods
dc.titleLabeling carboxyl groups of surface-exposed proteins provides an orthogonal approach for cell surface isolation
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.kuauthorKüçük, Nazlı Ezgi Özkan
local.contributor.kuauthorŞanal, Erdem
local.contributor.kuauthorÖzlü, Nurhan
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