Arndt-Jovin, Donna J.

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Valley, Christopher C."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Steinkamp, Mara P."],["dc.contributor.author","Chizhik, Alexey I."],["dc.contributor.author","Karedla, Narain V. R."],["dc.contributor.author","Hlavacek, William S."],["dc.contributor.author","Wilson, Bridget S."],["dc.contributor.author","Lidke, Keith A."],["dc.contributor.author","Lidke, Diane S."],["dc.date.accessioned","2018-11-07T10:01:57Z"],["dc.date.available","2018-11-07T10:01:57Z"],["dc.date.issued","2015"],["dc.format.extent","351A"],["dc.identifier.isi","000362849400177"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38135"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.conference","59th Annual Meeting of the Biophysical-Society"],["dc.relation.eventlocation","Baltimore, MD"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Inside-Out Signaling of Oncogenic EGFR Mutants Promotes Ligand-Independent Dimerization"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","619"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","626"],["dc.bibliographiccitation.volume","170"],["dc.contributor.author","Lidke, Diane S."],["dc.contributor.author","Lidke, Keith A."],["dc.contributor.author","Rieger, Bernd"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.date.accessioned","2021-06-01T10:51:14Z"],["dc.date.available","2021-06-01T10:51:14Z"],["dc.date.issued","2005"],["dc.description.abstract","ErbB1 receptors situated on cellular filopodia undergo systematic retrograde transport after binding of the epidermal growth factor (EGF) and activation of the receptor tyrosine kinase. Specific inhibitors of the erbB1 receptor tyrosine kinase as well as cytochalasin D, a disruptor of the actin cytoskeleton, abolish transport but not free diffusion of the receptor–ligand complex. Diffusion constants and transport rates were determined with single molecule sensitivity by tracking receptors labeled with EGF conjugated to fluorescent quantum dots. Retrograde transport precedes receptor endocytosis, which occurs at the base of the filopodia. Initiation of transport requires the interaction and concerted activation of at least two liganded receptors and proceeds at a constant rate mediated by association with actin. These findings suggest a mechanism by which filopodia detect the presence and concentration of effector molecules far from the cell body and mediate cellular responses via directed transport of activated receptors."],["dc.identifier.doi","10.1083/jcb.200503140"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86938"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","Reaching out for signals"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4087"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","4099"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Valley, Christopher C."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Karedla, Narain V. R."],["dc.contributor.author","Steinkamp, Mara P."],["dc.contributor.author","Chizhik, Alexey I."],["dc.contributor.author","Hlavacek, William S."],["dc.contributor.author","Wilson, Bridget S."],["dc.contributor.author","Lidke, Keith A."],["dc.contributor.author","Lidke, Diane S."],["dc.date.accessioned","2018-11-07T09:49:02Z"],["dc.date.available","2018-11-07T09:49:02Z"],["dc.date.issued","2015"],["dc.description.abstract","Mutations within the epidermal growth factor receptor (EGFR/erbB1/Her1) are often associated with tumorigenesis. In particular, a number of EGFR mutants that demonstrate ligand-independent signaling are common in non-small cell lung cancer (NSCLC), including kinase domain mutations L858R (also called L834R) and exon 19 deletions (e.g., Delta L747-P753insS), which collectively make up nearly 90% of mutations in NSCLC. The molecular mechanisms by which these mutations confer constitutive activity remain unresolved. Using multiple subdiffraction-limit imaging modalities, we reveal the altered receptor structure and interaction kinetics of NSCLC-associated EGFR mutants. We applied two-color single quantum dot tracking to quantify receptor dimerization kinetics on living cells and show that, in contrast to wild-type EGFR, mutants are capable of forming stable, ligand-independent dimers. Two-color superresolution localization microscopy confirmed ligand-independent aggregation of EGFR mutants. Live-cell Forster resonance energy transfer measurements revealed that the L858R kinase mutation alters ectodomain structure such that unliganded mutant EGFR adopts an extended, dimerization-competent conformation. Finally, mutation of the putative dimerization arm confirmed a critical role for ectodomain engagement in ligand-independent signaling. These data support a model in which dysregulated activity of NSCLC-associated kinase mutants is driven by coordinated interactions involving both the kinase and extracellular domains that lead to enhanced dimerization."],["dc.identifier.doi","10.1091/mbc.E15-05-0269"],["dc.identifier.isi","000366324900022"],["dc.identifier.pmid","26337388"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35430"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Enhanced dimerization drives ligand-independent activity of mutant epidermal growth factor receptor in lung cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Lidke, Diane S."],["dc.contributor.author","Chizhik, Alexey I."],["dc.contributor.author","Karedla, Narain V. R."],["dc.contributor.author","Jovin, Thomas M."],["dc.date.accessioned","2018-11-07T09:44:57Z"],["dc.date.available","2018-11-07T09:44:57Z"],["dc.date.issued","2014"],["dc.format.extent","237A"],["dc.identifier.isi","000337000401317"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34509"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.conference","58th Annual Meeting of the Biophysical-Society"],["dc.relation.eventlocation","San Francisco, CA"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Flim-FRET, a Structural Tool for ErbB Receptor Studies in the Living Cell"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]