Axonal Protein
Recently Published Documents


TOTAL DOCUMENTS

48
(FIVE YEARS 9)

H-INDEX

19
(FIVE YEARS 5)

Neuron ◽  
2020 ◽  
Vol 106 (2) ◽  
pp. 354
Author(s):  
Jone López-Erauskin ◽  
Takahiro Tadokoro ◽  
Michael W. Baughn ◽  
Brian Myers ◽  
Melissa McAlonis-Downes ◽  
...  

Neuron ◽  
2018 ◽  
Vol 100 (4) ◽  
pp. 816-830.e7 ◽  
Author(s):  
Jone López-Erauskin ◽  
Takahiro Tadokoro ◽  
Michael W. Baughn ◽  
Brian Myers ◽  
Melissa McAlonis-Downes ◽  
...  

2018 ◽  
Author(s):  
Li-An Chu ◽  
Chieh-Han Lu ◽  
Shun-Min Yang ◽  
Kuan-Lin Feng ◽  
Yen-Ting Liu ◽  
...  

AbstractLong-term memory (LTM) formation requires learning-induced protein synthesis in specific neurons and synapses within a neural circuit. Precisely how neural activity allocates new proteins to specific synaptic ensembles, however, remains unknown. We developed a deep-tissue super-resolution imaging tool suitable for single-molecule localization in intact adult Drosophila brain, and focused on the axonal protein allocation in mushroom body (MB), a central neuronal structure involved in olfactory memory formation. We found that insufficient training suppresses LTM formation by inducing the synthesis of vesicular monoamine transporter (VMAT) proteins within a dorsal paired medial (DPM) neuron, which innervates all axonal lobes of the MB. Surprisingly, using our localization microscopy, we found that these learning-induced proteins are distributed only in a subset of DPM axons in specific sectors along the MB lobes. This neural architecture suggests that sector-specific modulation of neural activity from MB neurons gates consolidation of early transient memory into LTM.


2018 ◽  
Vol 10 (1) ◽  
Author(s):  
Madhurima Chatterjee ◽  
Marta Del Campo ◽  
Tjado H. J. Morrema ◽  
Matthijs de Waal ◽  
Wiesje M. van der Flier ◽  
...  

Science ◽  
2018 ◽  
Vol 360 (6394) ◽  
pp. 1242-1246 ◽  
Author(s):  
Elizabeth H. Kellogg ◽  
Nisreen M. A. Hejab ◽  
Simon Poepsel ◽  
Kenneth H. Downing ◽  
Frank DiMaio ◽  
...  

Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into fibrils implicated in Alzheimer’s disease. It is unclear which tau residues are crucial for tau-MT interactions, where tau binds on MTs, and how it stabilizes them. We used cryo–electron microscopy to visualize different tau constructs on MTs and computational approaches to generate atomic models of tau-tubulin interactions. The conserved tubulin-binding repeats within tau adopt similar extended structures along the crest of the protofilament, stabilizing the interface between tubulin dimers. Our structures explain the effect of phosphorylation on MT affinity and lead to a model of tau repeats binding in tandem along protofilaments, tethering together tubulin dimers and stabilizing polymerization interfaces.


2016 ◽  
Vol 11 (9) ◽  
pp. 1365 ◽  
Author(s):  
JefferyL Twiss ◽  
AshleyL Kalinski ◽  
Rahul Sachdeva ◽  
JohnD Houle

2016 ◽  
Vol 2016 ◽  
pp. 1-13 ◽  
Author(s):  
Gunja K. Pathak ◽  
Hannah Ornstein ◽  
Helim Aranda-Espinoza ◽  
Amy J. Karlsson ◽  
Sameer B. Shah

Axons in the peripheral nervous system respond to injury by activating retrograde injury signaling (RIS) pathways, which promote local axonal protein synthesis (LPS) and neuronal regeneration. RIS is also initiated following injury of neurons in the central nervous system (CNS). However, regulation of the localization of axonal mRNA required for LPS is not well understood. We used a hippocampal explant system to probe the regulation of axonal levels of RIS-associated transcripts following axonal injury. Axonal levels of importinβ1 and RanBP1 were elevated biphasically at 1 and 24 hrs after axotomy. Transcript levels forβ-actin, a prototypic axonally synthesized protein, were similarly elevated. Our data suggest differential regulation of axonal transcripts. At 1 hr after injury, deployment of actinomycin revealed that RanBP1, but not importinβ1, requires de novo mRNA synthesis. At 24 hrs after injury, use of importazole revealed that the second wave of increased axonal mRNA levels required importinβ-mediated nuclear import. We also observed increased importinβ1 axonal protein levels at 1 and 6 hrs after injury. RanBP1 levels and vimentin levels fluctuated but were unchanged at 3 and 6 hrs after injury. This study revealed temporally complex regulation of axonal transcript levels, and it has implications for understanding neuronal response to injury in the CNS.


Sign in / Sign up

Export Citation Format

Share Document