scholarly journals Regulation of ciliary membrane protein trafficking and signalling by kinesin motor proteins

FEBS Journal ◽  
2018 ◽  
Vol 285 (24) ◽  
pp. 4535-4564 ◽  
Author(s):  
Stine Kjær Morthorst ◽  
Søren Tvorup Christensen ◽  
Lotte Bang Pedersen
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Motor Proteins ◽  
Kinesin Motor ◽  
Ciliary Membrane ◽  
Membrane Protein Trafficking ◽  
Kinesin Motor Proteins

scholarly journals Uni-directional ciliary membrane protein trafficking by a cytoplasmic retrograde IFT motor and ciliary ectosome shedding

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Muqing Cao ◽  
Jue Ning ◽  
Carmen I Hernandez-Lara ◽  
Olivier Belzile ◽  
Qian Wang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Protein Trafficking ◽  
Protein Composition ◽  
Cytoplasmic Dynein ◽  
Cytoplasmic Microtubule ◽  
Dynamic Regulation ◽  
Ciliary Membrane ◽  
Membrane Protein Trafficking

The role of the primary cilium in key signaling pathways depends on dynamic regulation of ciliary membrane protein composition, yet we know little about the motors or membrane events that regulate ciliary membrane protein trafficking in existing organelles. Recently, we showed that cilium-generated signaling in Chlamydomonas induced rapid, anterograde IFT-independent, cytoplasmic microtubule-dependent redistribution of the membrane polypeptide, SAG1-C65, from the plasma membrane to the periciliary region and the ciliary membrane. Here, we report that the retrograde IFT motor, cytoplasmic dynein 1b, is required in the cytoplasm for this rapid redistribution. Furthermore, signaling-induced trafficking of SAG1-C65 into cilia is unidirectional and the entire complement of cellular SAG1-C65 is shed during signaling and can be recovered in the form of ciliary ectosomes that retain signal-inducing activity. Thus, during signaling, cells regulate ciliary membrane protein composition through cytoplasmic action of the retrograde IFT motor and shedding of ciliary ectosomes.

scholarly journals A rapid and affordable screening platform for membrane protein trafficking

BMC Biology ◽  
2015 ◽  
Vol 13 (1) ◽  
Author(s):  
Joshua C. Snyder ◽  
Thomas F. Pack ◽  
Lauren K. Rochelle ◽  
Subhasish K. Chakraborty ◽  
Ming Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking ◽  
Screening Platform

Ethanol and Membrane Protein Trafficking: Diverse Mechanisms of Ethanol Action

2002 ◽  
Vol 26 (2) ◽  
pp. 287-293 ◽  
Author(s):  
Laura E. Nagy ◽  
M. Raj Lakshman ◽  
Carol A. Casey ◽  
Cynthia F. Bearer
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking

scholarly journals Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane

2012 ◽  
Vol 23 (15) ◽  
pp. 2917-2929 ◽  
Author(s):  
Emily Deutsch ◽  
Aubrey V. Weigel ◽  
Elizabeth J. Akin ◽  
Phil Fox ◽  
Gentry Hansen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Ion Channel ◽  
Protein Trafficking ◽  
Hippocampal Neurons ◽  
Surface Membrane ◽  
Cell Types ◽  
Homogeneous Surface ◽  
Hek Cells ◽  
Membrane Protein Trafficking

Voltage-gated K+ (Kv) channels regulate membrane potential in many cell types. Although the channel surface density and location must be well controlled, little is known about Kv channel delivery and retrieval on the cell surface. The Kv2.1 channel localizes to micron-sized clusters in neurons and transfected human embryonic kidney (HEK) cells, where it is nonconducting. Because Kv2.1 is postulated to be involved in soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion, we examined the hypothesis that these surface clusters are specialized platforms involved in membrane protein trafficking. Total internal reflection–based fluorescence recovery after photobleaching studies and quantum dot imaging of single Kv2.1 channels revealed that Kv2.1-containing vesicles deliver cargo at the Kv2.1 surface clusters in both transfected HEK cells and hippocampal neurons. More than 85% of cytoplasmic and recycling Kv2.1 channels was delivered to the cell surface at the cluster perimeter in both cell types. At least 85% of recycling Kv1.4, which, unlike Kv2.1, has a homogeneous surface distribution, is also delivered here. Actin depolymerization resulted in Kv2.1 exocytosis at cluster-free surface membrane. These results indicate that one nonconducting function of Kv2.1 is to form microdomains involved in membrane protein trafficking. This study is the first to identify stable cell surface platforms involved in ion channel trafficking.

scholarly journals Fluorogenic Probing of Membrane Protein Trafficking

2018 ◽  
Vol 29 (6) ◽  
pp. 1823-1828 ◽  
Author(s):  
Chenge Li ◽  
Aurélien Mourton ◽  
Marie-Aude Plamont ◽  
Vanessa Rodrigues ◽  
Isabelle Aujard ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking

Controlling kinesin motor proteins in nanoengineered systems through a metal-binding on/off switch

2008 ◽  
Vol 101 (3) ◽  
pp. 478-486 ◽  
Author(s):  
Adrienne C. Greene ◽  
Amanda M. Trent ◽  
George D. Bachand
Keyword(s):  
Metal Binding ◽  
Motor Proteins ◽  
Kinesin Motor ◽  
Kinesin Motor Proteins
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