scholarly journals The Role of Motor Clustering in Kinesin-Driven Vesicle Transport

2021 ◽  
Vol 120 (3) ◽  
pp. 164a
Author(s):  
Rui Jiang ◽  
Qingzhou Feng ◽  
You Jung Kang ◽  
William O. Hancock
Keyword(s):  
2020 ◽  
Author(s):  
Tatiana A. Kazakova ◽  
Oleg N. Suchalko ◽  
Alexey D. Ivanov ◽  
Anna V. Alova ◽  
George V. Maksimov

AbstractThe redistribution of vesicles containing serotonin in leech neurons was studied using the fluorescent, scanning ion-conductance, and laser phase microscopy methods. During acetylcholine receptor (AChR) activation in Retzius neurons, the changes of Ca2+ desorption, cellular stiffness and the cell optical phase difference (OPD) were established. It was found that the amplitude of OPD changes in the near-membrane area (membrane and near-membrane of the cytoplasm layers) increases upon AChR activation and this is, possibly, associated with the neurons vesicle redistribution. The decrease in the cell stiffness upon AChR activation suggests the crucial role of cytoskeleton for vesicle transport and release. Ca2+ rise in the cytoplasm during AChR activation may regulate the mitochondrial recruitment to regions with high energy demand for vesicle trafficking.


2001 ◽  
Vol 114 (11) ◽  
pp. 2199-2204 ◽  
Author(s):  
Tineke Voorn-Brouwer ◽  
Astrid Kragt ◽  
Henk F. Tabak ◽  
Ben Distel

The classic model for peroxisome biogenesis states that new peroxisomes arise by the fission of pre-existing ones and that peroxisomal matrix and membrane proteins are recruited directly from the cytosol. Recent studies challenge this model and suggest that some peroxisomal membrane proteins might traffic via the endoplasmic reticulum to peroxisomes. We have studied the trafficking in human fibroblasts of three peroxisomal membrane proteins, Pex2p, Pex3p and Pex16p, all of which have been suggested to transit the endoplasmic reticulum before arriving in peroxisomes. Here, we show that targeting of these peroxisomal membrane proteins is not affected by inhibitors of COPI and COPII that block vesicle transport in the early secretory pathway. Moreover, we have obtained no evidence for the presence of these peroxisomal membrane proteins in compartments other than peroxisomes and demonstrate that COPI and COPII inhibitors do not affect peroxisome morphology or integrity. Together, these data fail to provide any evidence for a role of the endoplasmic reticulum in peroxisome biogenesis.


2001 ◽  
Vol 152 (4) ◽  
pp. 843-850 ◽  
Author(s):  
Philippe Bahadoran ◽  
Edith Aberdam ◽  
Frédéric Mantoux ◽  
Roser Buscà ◽  
Karine Bille ◽  
...  

Normal pigmentation depends on the uniform distribution of melanin-containing vesicles, the melanosomes, in the epidermis. Griscelli syndrome (GS) is a rare autosomal recessive disease, characterized by an immune deficiency and a partial albinism that has been ascribed to an abnormal melanosome distribution. GS maps to 15q21 and was first associated with mutations in the myosin-V gene. However, it was demonstrated recently that GS can also be caused by a mutation in the Rab27a gene. These observations prompted us to investigate the role of Rab27a in melanosome transport. Using immunofluorescence and immunoelectron microscopy studies, we show that in normal melanocytes Rab27a colocalizes with melanosomes. In melanocytes isolated from a patient with GS, we show an abnormal melanosome distribution and a lack of Rab27a expression. Finally, reexpression of Rab27a in GS melanocytes restored melanosome transport to dendrite tips, leading to a phenotypic reversion of the diseased cells. These results identify Rab27a as a key component of vesicle transport machinery in melanocytes.


1997 ◽  
Vol 15 (2) ◽  
pp. 126
Author(s):  
Y. Funasaka ◽  
K. Araki ◽  
A.K. Chakraborty ◽  
A. Ito ◽  
E. Nishioka ◽  
...  

1993 ◽  
Vol 28 (9) ◽  
pp. 833-838 ◽  
Author(s):  
M. Hoshino ◽  
T. Ohiwa ◽  
T. Hayakawa ◽  
Y. Kamiya ◽  
A. Tanaka ◽  
...  

2008 ◽  
Vol 81 ◽  
pp. 93-94
Author(s):  
J. N. Larocca ◽  
G. Almazan ◽  
A. G. Rodriguez-Gabin
Keyword(s):  

1998 ◽  
Vol 78 (4) ◽  
pp. 1109-1129 ◽  
Author(s):  
SARAH F. HAMM-ALVAREZ ◽  
MICHAEL P. SHEETZ

Hamm-Alvarez, Sarah F., and Michael P. Sheetz. Microtubule-Dependent Vesicle Transport: Modulation of Channel and Transporter Activity in Liver and Kidney. Physiol. Rev. 78: 1109–1129, 1998. — Microtubule-based vesicle transport driven by kinesin and cytoplasmic dynein motor proteins facilitates several membrane-trafficking steps including elements of endocytosis and exocytosis in many different cell types. Most early studies on the role of microtubule-dependent vesicle transport in membrane trafficking focused either on neurons or on simple cell lines. More recently, other work has considered the role of microtubule-based vesicle transport in other physiological systems, including kidney and liver. Investigation of the role of microtubule-based vesicle transport in membrane trafficking in cells of the kidney and liver suggests a major role for microtubule-based vesicle transport in the rapid and directed movement of ion channels and transporters to and from the apical plasma membranes, events essential for kidney and liver function and homeostasis. This review discusses the evidence supporting a role for microtubule-based vesicle transport and the motor proteins, kinesin and cytoplasmic dynein, in different aspects of membrane trafficking in cells of the kidney and liver, with emphasis on those functions such as maintenance of ion channel and transporter composition in apical membranes that are specialized functions of these organs. Evidence that defects in microtubule-based transport contribute to diseases of the kidney and liver is also discussed.


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