Diversifying the secretory routes in neurons

Valenzuela, Juan Pablo; Perez, Franck

doi:10.3389/fnins.2015.00358

Cited by 40 publications

(31 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Calnexin exhibits a peri-nuclear labeling pattern with colocalization with membrane labels -this represents a previously known sub-population of Calnexin proteins that are post-translationally modified with a palmitoyl group inside the ER and localize to contact sites of the ER with the nucleus 34 . Additionally, the Golgi apparatus, colabeled with anti-giantin and our lipid stain, is visible primarily in neuronal somas, in accordance with previous studies 35 (Fig. 3b, right).…”

Section: Immunohistochemistry-compatible Mexmsupporting

confidence: 92%

Expansion Microscopy of Lipid Membranes

Karagiannis

Kang

Shin

et al. 2019

Preprint

View full text Add to dashboard Cite

Lipids are fundamental building blocks of cells and their organelles, yet nanoscale resolution imaging of lipids has been largely limited to electron microscopy techniques. We introduce and validate a chemical tag that enables lipid membranes to be imaged optically at nanoscale resolution via a lipid-optimized form of expansion microscopy, which we call membrane expansion microscopy (mExM). mExM, via a novel post-expansion antibody labeling protocol, enables protein-lipid relationships to be imaged in organelles such as mitochondria, the endoplasmic reticulum, the nuclear membrane, and the Golgi apparatus. mExM may be of use in a variety of biological contexts, including the study of cell-cell interactions, intracellular transport, and neural connectomics. MainExpansion microscopy (ExM) physically magnifies biological specimens by covalently anchoring biomolecules or labels to a swellable polymer network (typically sodium polyacrylate) synthesized in situ throughout the specimen 1-4 . Following tissue softening and solvent exchange, the hydrogel-specimen composite expands isotropically, typically to a physical magnification of ~4.5x in linear dimension. The net result is that biomolecules or labels that are initially localized within the diffraction limit of a traditional optical microscope can now be separated in space to distances far enough that they can be resolved on ordinary microscopes. Expansion microscopy protocols 5 for the visualization of proteins 3,6,7 and nucleic acids 4 are in increasingly widespread use, raising the question of whether other biological molecule classes, such as lipids, can also be visualized by ExM. We here report an expansion microscopy-compatible lipid stain, as well as a

show abstract

Section: Immunohistochemistry-compatible Mexmsupporting

confidence: 92%

Expansion Microscopy of Lipid Membranes

Karagiannis

Kang

Shin

et al. 2019

Preprint

View full text Add to dashboard Cite

show abstract

“…Synaptopodin puncta in both spines and dendrite shafts were stably anchored at the same locations and sometimes oscillated within areas of 1-2 µm. These data rule out the possibility that clusters of synaptopodin (and thus the SA) might be actively transported via long-distance microtubule-dependent, active transport as it is known for many other membrane organelles (Ayloo et al, 2017;Valenzuela and Perez, 2015;van Spronsen et al, 2013).…”

Section: Synaptopodin Clusters Show No Processive Trafficking and Aresupporting

confidence: 58%

Characterization of neuronal synaptopodin reveals a myosin V-dependent mechanism of synaptopodin clustering at the post-synaptic sites

González-Gallego¹,

Konietzny²,

Pérez-Álvarez³

et al. 2019

Preprint

View full text Add to dashboard Cite

STATEMENTHere we demonstrate that the spine apparatus is assembled locally in dendrites. This process, which relies on the presence of synaptopodin and F-actin, is disrupted by interfering with myosin-V activity. ABSTRACTThe spine apparatus (SA) is an endoplasmic reticulum-related organelle which is present in a subset of dendritic spines in cortical and pyramidal neurons. The synaptopodin protein localizes between the stacks of the spine apparatus and is essential for the formation of this unique organelle. Although several studies have demonstrated the significance of the SA and synaptopodin in calcium homeostasis and plasticity of dendritic spines, it is still unclear what factors contribute to its stability at the synapse and whether the SA is locally formed or it is actively delivered to the spines. In this study we show that synaptopodin clusters are stable at their locations. We found no evidence of active microtubule-based transport for synaptopodin. Instead new clusters were emerging in the spines, which we interpret as the SA being assembled on-site.Furthermore, using super-resolution microscopy we show a tight association of synaptopodin with actin filaments. We identify the actin-based motor proteins myosin V and VI as novel interaction partners of synaptopodin and demonstrate that myosin V is important for the formation and/or maintenance of the SA.

show abstract

“…A range of neuronal transmembrane proteins, including AMPARs, NMDARs and GABA B Rs, can be translated using both somatic and dendritically localised ribosome patterned rough ER. They then traffic from the ER using dendritic ER exit sites and utilise the somatic Golgi or dendritic Golgi outposts for mature glycosylation [48, [58][59][60][61][62]. Importantly, all of the secretory pathway machinery appears to be present in neurites as iGluRs can mature in isolated dendrites [63].…”

Section: Local Dendritic Translation and Secretory Pathway Traffickingmentioning

confidence: 99%

Exciting Times: New Advances Towards Understanding the Regulation and Roles of Kainate Receptors

et al. 2017

View full text Add to dashboard Cite

Kainate receptors (KARs) are glutamate-gated ion channels that play fundamental roles in regulating neuronal excitability and network function in the brain. After being cloned in the 1990s, important progress has been made in understanding the mechanisms controlling the molecular and cellular properties of KARs, and the nature and extent of their regulation of wider neuronal activity. However, there have been significant recent advances towards understanding KAR trafficking through the secretory pathway, their precise synaptic positioning, and their roles in synaptic plasticity and disease. Here we provide an overview highlighting these new findings about the mechanisms controlling KARs and how KARs, in turn, regulate other proteins and pathways to influence synaptic function.

show abstract

Diversifying the secretory routes in neurons

Cited by 40 publications

References 62 publications

Expansion Microscopy of Lipid Membranes

Expansion Microscopy of Lipid Membranes

Characterization of neuronal synaptopodin reveals a myosin V-dependent mechanism of synaptopodin clustering at the post-synaptic sites

Exciting Times: New Advances Towards Understanding the Regulation and Roles of Kainate Receptors

Contact Info

Product

Resources

About