scholarly journals A novel HSP90 chaperone complex regulates intracellular vesicle transport

2008 ◽  
Vol 121 (5) ◽  
pp. 717-723 ◽  
Author(s):  
G. P. Lotz ◽  
A. Brychzy ◽  
S. Heinz ◽  
W. M. J. Obermann
Keyword(s):  
Vesicle Transport ◽  
Intracellular Vesicle ◽  
Hsp90 Chaperone ◽  
Chaperone Complex ◽  
Intracellular Vesicle Transport

Distinct intracellular vesicle transport mechanisms are selectively modified by spastin and spastin mutations

2010 ◽  
Vol 226 (2) ◽  
pp. 362-368 ◽  
Author(s):  
Julia C. Fuerst ◽  
Andreas W. Henkel ◽  
Armin Stroebel ◽  
Oliver Welzel ◽  
Teja W. Groemer ◽  
...  
Keyword(s):  
Vesicle Transport ◽  
Transport Mechanisms ◽  
Intracellular Vesicle ◽  
Intracellular Vesicle Transport

Actin sequestering protein, profilin, regulates intracellular vesicle transport in Leishmania

2020 ◽  
Vol 238 ◽  
pp. 111280 ◽  
Author(s):  
Bindu Ambaru ◽  
Anupriya Gopalsamy ◽  
T.V.Satish Tammana ◽  
Hosahalli S. Subramanya ◽  
Chhitar M. Gupta
Keyword(s):  
Vesicle Transport ◽  
Intracellular Vesicle ◽  
Intracellular Vesicle Transport

VISUALIZING THE UPTAKE AND INTRACELLULAR VESICLE TRANSPORT OF CARBON NANOTUBES TOWARD THE PERINUCLEAR REGION INSIDE CELLS

NANO ◽  
2014 ◽  
Vol 09 (01) ◽  
pp. 1450001 ◽  
Author(s):  
JUN LI ◽  
BIN KANG ◽  
SHUQUAN CHANG ◽  
YAODONG DAI
Keyword(s):  
Carbon Nanotubes ◽  
Living Cells ◽  
Vesicle Transport ◽  
Endocytic Pathway ◽  
Perinuclear Region ◽  
Microtubule Organizing Center ◽  
Ph Change ◽  
Intracellular Vesicle ◽  
Early Endosomes ◽  
Intracellular Vesicle Transport

We directly visualized the uptake and intracellular vesicle transport of shortened single walled carbon nanotubes in living cells through a dual-labeling system. With a stable labeling of fluorescein isothiocyanate and a pH-sensitive stacking of doxorubicin on carbon nanotubes, the location of internalized nanotubes inside the cell and the microenvironment especially the pH change of the nanotube-embedded vesicles could be monitored at the same time. Results showed that after internalization through endocytic pathway, carbon nanotubes tended to transport from the early endosomes to later acidic lysosomes and these vesicles moved along the microtubule track toward a perinuclear region where is a microtubule-organizing center. These results might provide a novel understanding for the intracellular interaction of carbon nanotubes and living cells.

scholarly journals The Hsp90 Chaperone Complex Regulates GDI-dependent Rab Recycling

2006 ◽  
Vol 17 (8) ◽  
pp. 3494-3507 ◽  
Author(s):  
Christine Y. Chen ◽  
William E. Balch
Keyword(s):  
Rab Gtpase ◽  
Rab Gtpases ◽  
Coding System ◽  
Golgi Transport ◽  
Guanine Nucleotide Dissociation Inhibitor ◽  
Hsp90 Activity ◽  
Hsp90 Chaperone ◽  
Chaperone Complex ◽  
Hsp 90 ◽  
Synaptic Vesicle Fusion

Rab GTPase regulated hubs provide a framework for an integrated coding system, the membrome network, that controls the dynamics of the specialized exocytic and endocytic membrane architectures found in eukaryotic cells. Herein, we report that Rab recycling in the early exocytic pathways involves the heat-shock protein (Hsp)90 chaperone system. We find that Hsp90 forms a complex with guanine nucleotide dissociation inhibitor (GDI) to direct recycling of the client substrate Rab1 required for endoplasmic reticulum (ER)-to-Golgi transport. ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol. Hsp90 activity is required to form a functional GDI complex to retrieve Rab1 from the membrane. Moreover, we find that Hsp90 is essential for Rab1-dependent Golgi assembly. The observation that the highly divergent Rab GTPases Rab1 involved in ER-to-Golgi transport and Rab3A involved in synaptic vesicle fusion require Hsp90 for retrieval from membranes lead us to now propose that the Hsp90 chaperone system may function as a general regulator for Rab GTPase recycling in exocytic and endocytic trafficking pathways involved in cell signaling and proliferation.

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