Faculty Opinions recommendation of Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex.

2005 ◽  
Author(s):  
Vance Lemmon
Keyword(s):  
Exocyst Complex ◽  
Ral Gtpases

scholarly journals Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex

2005 ◽  
Vol 171 (5) ◽  
pp. 857-869 ◽  
Author(s):  
Giovanna Lalli ◽  
Alan Hall
Keyword(s):  
Phospholipase D ◽  
Cortical Neurons ◽  
Sympathetic Neurons ◽  
Protein A ◽  
Small Gtpase ◽  
Neuronal Morphology ◽  
Kinase C ◽  
Exocyst Complex ◽  
Ral Gtpases ◽  
Neuronal Connections

Neurite branching is essential for the establishment of appropriate neuronal connections during development and regeneration. We identify the small GTPase Ral as a mediator of neurite branching. Active Ral promotes neurite branching in cortical and sympathetic neurons, whereas Ral inhibition decreases laminin-induced branching. In addition, depletion of endogenous Ral by RNA interference decreases branching in cortical neurons. The two Ral isoforms, RalA and -B, promote branching through distinct pathways, involving the exocyst complex and phospholipase D, respectively. Finally, Ral-dependent branching is mediated by protein kinase C–dependent phosphorylation of 43-kD growth-associated protein, a crucial molecule involved in pathfinding, plasticity, and regeneration. These findings highlight an important role for Ral in the regulation of neuronal morphology.

764: Differential Expression of RAL GTPases and their Effectors in Bladder Cancer

2007 ◽  
Vol 177 (4S) ◽  
pp. 256-256
Author(s):  
Steven Smith ◽  
Gary Oxford ◽  
Dan Theodorescu
Keyword(s):  
Bladder Cancer ◽  
Differential Expression ◽  
Ral Gtpases

scholarly journals Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana

2013 ◽  
Vol 24 (4) ◽  
pp. 510-520 ◽  
Author(s):  
Matyáš Fendrych ◽  
Lukáš Synek ◽  
Tamara Pečenková ◽  
Edita Janková Drdová ◽  
Juraj Sekereš ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Fluorescent Protein ◽  
Complex Dynamics ◽  
Active Regions ◽  
Snare Complex ◽  
Epifluorescence Microscopy ◽  
Rab Gtpases ◽  
Exocyst Complex ◽  
Protein Receptor ◽  
Outer Domain

The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the plasma membrane, exemplified by the outer domain of Arabidopsis root epidermal cells. Using variable-angle epifluorescence microscopy, we visualized the dynamics of exocyst subunits at this domain. The subunits colocalized in defined foci at the plasma membrane, distinct from endocytic sites. Exocyst foci were independent of cytoskeleton, although prolonged actin disruption led to changes in exocyst localization. Exocyst foci partially overlapped with vesicles visualized by VAMP721 v-SNARE, but the majority of the foci represent sites without vesicles, as indicated by electron microscopy and drug treatments, supporting the concept of the exocyst functioning as a dynamic particle. We observed a decrease of SEC6–green fluorescent protein foci in an exo70A1 exocyst mutant. Finally, we documented decreased VAMP721 trafficking to the plasma membrane in exo70A1 and exo84b mutants. Our data support the concept that the exocyst-complex subunits dynamically dock and undock at the plasma membrane to create sites primed for vesicle tethering.

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