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Institute: search.filters.UBSInstitut.Institut für Zellbiologie und ImmunologieAuthor: search.filters.author.Eisler, Stephan A.

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    ItemOpen Access
    Golgi screen identifies the RhoGEF Solo as a novel regulator of RhoB and endocytic transport
    (2023) Lungu, Cristiana; Meyer, Florian; Hörning, Marcel; Steudle, Jasmin; Braun, Anja; Noll, Bettina; Benz, David; Fränkle, Felix; Schmid, Simone; Eisler, Stephan A.; Olayioye, Monilola A.
    The control of intracellular membrane trafficking by Rho GTPases is central to cellular homeostasis. How specific guanine nucleotide exchange factors and GTPase‐activating proteins locally balance GTPase activation in this process is nevertheless largely unclear. By performing a microscopy‐based RNAi screen, we here identify the RhoGEF protein Solo as a functional counterplayer of DLC3, a RhoGAP protein with established roles in membrane trafficking. Biochemical, imaging and optogenetics assays further uncover Solo as a novel regulator of endosomal RhoB. Remarkably, we find that Solo and DLC3 control not only the activity, but also total protein levels of RhoB in an antagonistic manner. Together, the results of our study uncover the first functionally connected RhoGAP‐RhoGEF pair at endomembranes, placing Solo and DLC3 at the core of endocytic trafficking.
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    Protein kinase D promotes activity‐dependent AMPA receptor endocytosis in hippocampal neurons
    (2021) Oueslati Morales, Carlos O.; Ignácz, Attila; Bencsik, Norbert; Sziber, Zsofia; Rátkai, Anikó Erika; Lieb, Wolfgang S.; Eisler, Stephan A.; Szűcs, Attila; Schlett, Katalin; Hausser, Angelika
    α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionic acid (AMPA) type glutamate receptors (AMPARs) mediate the majority of fast excitatory neurotransmission in the brain. The continuous trafficking of AMPARs into and out of synapses is a core feature of synaptic plasticity, which is considered as the cellular basis of learning and memory. The molecular mechanisms underlying the postsynaptic AMPAR trafficking, however, are still not fully understood. In this work, we demonstrate that the protein kinase D (PKD) family promotes basal and activity‐induced AMPAR endocytosis in primary hippocampal neurons. Pharmacological inhibition of PKD increased synaptic levels of GluA1‐containing AMPARs, slowed down their endocytic trafficking and increased neuronal network activity. By contrast, ectopic expression of constitutive active PKD decreased the synaptic level of AMPARs, while increasing their colocalization with early endosomes. Our results thus establish an important role for PKD in the regulation of postsynaptic AMPAR trafficking during synaptic plasticity.