Soykan, Tolga

[["dc.bibliographiccitation.firstpage","321"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","446"],["dc.contributor.author","Poulopoulos, Alexandros"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Tuffy, Liam P."],["dc.contributor.author","Hammer, Matthieu"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:48:25Z"],["dc.date.available","2017-09-07T11:48:25Z"],["dc.date.issued","2012"],["dc.description.abstract","Neuroligins are postsynaptic adhesion proteins involved in the establishment of functional synapses in the central nervous system. In rodents, four genes give rise to neuroligins that function at distinct synapses, with corresponding neurotransmitter and subtype specificities. In the present study, we examined the interactions between the different neuroligins by isolating endogenous oligomeric complexes using in situ cross-linking on primary neurons. Examining hippocampal, striatal, cerebellar and spinal cord cultures, we found that neuroligins form constitutive dimers, including homomers and, most notably, neuroligin 1/3 heteromers. Additionally, we found that neuroligin monomers are specifically retained in the secretory pathway through a cellular quality control mechanism that involves the neuroligin transmembrane domain, ensuring that dimerization occurs prior to cell surface trafficking. Lastly, we identified differences in the dimerization capacity of autism-associated neuroligin mutants, and found that neuroligin 3 R471C mutants can form heterodimers with neuroligin 1. The pervasive nature of neuroligin dimerization indicates that the unit of neuroligin function is the dimer, and raises intriguing possibilities of distinct heterodimer functions, and of interactions between native and mutant neuroligins contributing to disease phenotypes."],["dc.identifier.doi","10.1042/BJ20120808"],["dc.identifier.gro","3142468"],["dc.identifier.isi","000308767500016"],["dc.identifier.pmid","22671294"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8618"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0264-6021"],["dc.title","Homodimerization and isoform-specific heterodimerization of neuroligins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2113"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","2133"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Schneeberger, Daniela"],["dc.contributor.author","Tria, Giancarlo"],["dc.contributor.author","Buechner, Claudia"],["dc.contributor.author","Bader, Nicole"],["dc.contributor.author","Svergun, Dmitri"],["dc.contributor.author","Tessmer, Ingrid"],["dc.contributor.author","Poulopoulos, Alexandros"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.contributor.author","Schindelin, Hermann"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:45:30Z"],["dc.date.available","2017-09-07T11:45:30Z"],["dc.date.issued","2014"],["dc.description.abstract","The formation of neuronal synapses and the dynamic regulation of their efficacy depend on the assembly of the postsynaptic neuro transmitter receptor apparatus. Receptor recruitment to inhibitory GABAergic and glycinergic synapses is controlled by the scaffold protein gephyrin and the adaptor protein collybistin. We derived new insights into the structure of collybistin and used these to design biochemical, cell biological, and genetic analyses of collybistin function. Our data define a collybistin-based protein interaction network that controls the gephyrin content of inhibitory postsynapses. Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides. This function of collybistin is regulated by binding of the adhesion protein neuroligin-2, which stabilizes the open/active conformation of collybistin at the postsynaptic plasma membrane by competing with an intramolecular interaction in collybistin that favors the closed/inactive conformation. By linking trans-synaptic neuroligin-dependent adhesion and phosphoinositide signaling with gephyrin recruitment, the collybistin-based regulatory switch mechanism represents an integrating regulatory node in the formation and function of inhibitory postsynapses."],["dc.identifier.doi","10.15252/embj.201488143"],["dc.identifier.gro","3142051"],["dc.identifier.isi","000342503000012"],["dc.identifier.pmid","25082542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4000"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","A conformational switch in collybistin determines the differentiation of inhibitory postsynapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3053"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","3058"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Hoon, Mrinalini"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Falkenburger, Björn"],["dc.contributor.author","Hammer, Matthieu"],["dc.contributor.author","Patrizi, Annarita"],["dc.contributor.author","Schmidt, Karl-Friedrich"],["dc.contributor.author","Sassoè-Pognetto, Marco"],["dc.contributor.author","Löwel, Siegrid"],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.date.accessioned","2017-09-07T11:44:21Z"],["dc.date.available","2017-09-07T11:44:21Z"],["dc.date.issued","2011"],["dc.description.abstract","Neuroligins (NL1-NL4) are postsynaptic adhesion proteins that control the maturation and function of synapses in the central nervous system (CNS). Loss-of-function mutations in NL4 are linked to rare forms of monogenic heritable autism, but its localization and function are unknown. Using the retina as a model system, we show that NL4 is preferentially localized to glycinergic postsynapses and that the loss of NL4 is accompanied by a reduced number of glycine receptors mediating fast glycinergic transmission. Accordingly, NL4-deficient ganglion cells exhibit slower glycinergic miniature postsynaptic currents and subtle alterations in their stimuluscoding efficacy, and inhibition within the NL4-deficient retinal network is altered as assessed by electroretinogram recordings. These data indicate that NL4 shapes network activity and information processing in the retina by modulating glycinergic inhibition. Importantly, NL4 is also targeted to inhibitory synapses in other areas of the CNS, such as the thalamus, colliculi, brainstem, and spinal cord, and forms complexes with the inhibitory postsynapse proteins gephyrin and collybistin in vivo, indicating that NL4 is an important component of glycinergic postsynapses."],["dc.identifier.doi","10.1073/pnas.1006946108"],["dc.identifier.gro","3142775"],["dc.identifier.isi","000287377000078"],["dc.identifier.pmid","21282647"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/216"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Neuroligin-4 is localized to glycinergic postsynapses and regulates inhibition in the retina"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]