Role of Doc2α in dense-core vesicle exocytosis in PC12 cells revealed by live cell imaging

2011 ◽  
Vol 71 ◽  
pp. e213
Author(s):  
Takashi Tsuboi ◽  
Yasunori Mori ◽  
Hideki Matsui ◽  
Ryo Aoki ◽  
Manami Oya ◽  
...  
2010 ◽  
pp. no-no ◽  
Author(s):  
Mai Sato ◽  
Yasunori Mori ◽  
Takahide Matsui ◽  
Ryo Aoki ◽  
Manami Oya ◽  
...  

2018 ◽  
Vol 217 (6) ◽  
pp. 2047-2058 ◽  
Author(s):  
Chi-Lun Chang ◽  
Yu-Ju Chen ◽  
Carlo Giovanni Quintanilla ◽  
Ting-Sung Hsieh ◽  
Jen Liou

The endoplasmic reticulum (ER) Ca2+ sensor STIM1 forms oligomers and translocates to ER–plasma membrane (PM) junctions to activate store-operated Ca2+ entry (SOCE) after ER Ca2+ depletion. STIM1 also interacts with EB1 and dynamically tracks microtubule (MT) plus ends. Nevertheless, the role of STIM1–EB1 interaction in regulating SOCE remains unresolved. Using live-cell imaging combined with a synthetic construct approach, we found that EB1 binding constitutes a trapping mechanism restricting STIM1 targeting to ER–PM junctions. We further showed that STIM1 oligomers retain EB1 binding ability in ER Ca2+-depleted cells. By trapping STIM1 molecules at dynamic contacts between the ER and MT plus ends, EB1 binding delayed STIM1 translocation to ER–PM junctions during ER Ca2+ depletion and prevented excess SOCE and ER Ca2+ overload. Our study suggests that STIM1–EB1 interaction shapes the kinetics and amplitude of local SOCE in cellular regions with growing MTs and contributes to spatiotemporal regulation of Ca2+ signaling crucial for cellular functions and homeostasis.


10.1038/nn869 ◽  
2002 ◽  
Vol 5 (7) ◽  
pp. 649-656 ◽  
Author(s):  
Ok-Ho Shin ◽  
Josep Rizo ◽  
Thomas C. Südhof

2009 ◽  
Vol 37 (5) ◽  
pp. 1056-1060 ◽  
Author(s):  
Marek Cebecauer ◽  
Dylan M. Owen ◽  
Anna Markiewicz ◽  
Anthony I. Magee

Multimolecular assemblies on the plasma membrane exhibit dynamic nature and are often generated during the activation of eukaryotic cells. The role of lipids and their physical properties in helping to control the existence of these structures is discussed. Technological improvements for live cell imaging of membrane components are also reviewed.


2007 ◽  
Vol 85 (12) ◽  
pp. 2640-2647 ◽  
Author(s):  
Kenneth R. Myers ◽  
Kevin W.-H. Lo ◽  
R. John Lye ◽  
John M. Kogoy ◽  
Violetta Soura ◽  
...  

2005 ◽  
Vol 168 (5) ◽  
pp. 697-703 ◽  
Author(s):  
Yan He ◽  
Franto Francis ◽  
Kenneth A. Myers ◽  
Wenqian Yu ◽  
Mark M. Black ◽  
...  

Recent studies have shown that the transport of microtubules (MTs) and neurofilaments (NFs) within the axon is rapid, infrequent, asynchronous, and bidirectional. Here, we used RNA interference to investigate the role of cytoplasmic dynein in powering these transport events. To reveal transport of MTs and NFs, we expressed EGFP-tagged tubulin or NF proteins in cultured rat sympathetic neurons and performed live-cell imaging of the fluorescent cytoskeletal elements in photobleached regions of the axon. The occurrence of anterograde MT and retrograde NF movements was significantly diminished in neurons that had been depleted of dynein heavy chain, whereas the occurrence of retrograde MT and anterograde NF movements was unaffected. These results support a cargo model for NF transport and a sliding filament model for MT transport.


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