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Molecular Control of Organelle Shape and Identity in the Endomembrane System

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (25 September 2018)

Special Issue Editor

Special Issue Information

Dear Colleagues,

One striking observation in eukaryotic cells is that, over time, their organelles maintain a remarkably constant size and shape despite high levels of biochemical activity. In the early secretory pathway for example, proteins synthesised in the endoplasmic reticulum (ER) but which are destined for secretion, are constantly packaged into membrane transport carriers that leave the ER and are directed towards the Golgi complex. The fact that the ER maintains its overall size, shape and volume tells us that this organelle must receive—from the Golgi complex—an equivalent amount of membrane per unit time. Indeed, if all the organelles in the endomembrane system are to retain their functionality, such counter-balancing of membrane flow must exist between all compartments that communicate with each other. This control of membrane identity and function is likely to be regulated through a variety of factors, including the activity of proteins and lipids resident in each compartment, as well as through long range signalling events across the cell, and linkage to the cytoskeleton. What is also clear is that perturbation of transport pathways between organelles, manifested in a number of diseases, results in aberrant organelle function and morphology. In this Special Issue entitled "Molecular Control of Organelle Shape and Identity in the Endomembrane System", we are seeking novel research or review articles highlighting the variety of machinery and regulatory mechanisms used in membrane traffic, with specific regard to how membrane flux is controlled and how it determines the identity and function of organelles. Additionally relevant is how dysfunctional trafficking events has implications in disease. We look forward to receiving your contributions to this exciting Special Issue.

Prof. Dr. Jeremy C. Simpson
Guest Editor

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Keywords

  • membrane traffic
  • secretory pathway
  • endocytic pathway
  • organelle identity
  • coat proteins
  • small GTPases
  • lipids and phosphoinositides
  • endoplasmic reticulum
  • Golgi complex
  • endosomal system
  • cytoskeleton
  • signalling pathways
  • disease, infection and membrane traffic

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Published Papers (1 paper)

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Research

19 pages, 7500 KiB  
Article
VEGF Triggers the Activation of Cofilin and the Arp2/3 Complex within the Growth Cone
by Matthias Schlau, Daniel Terheyden-Keighley, Verena Theis, Hans Georg Mannherz and Carsten Theiss
Int. J. Mol. Sci. 2018, 19(2), 384; https://doi.org/10.3390/ijms19020384 - 27 Jan 2018
Cited by 13 | Viewed by 4924
Abstract
A crucial neuronal structure for the development and regeneration of neuronal networks is the axonal growth cone. Affected by different guidance cues, it grows in a predetermined direction to reach its final destination. One of those cues is the vascular endothelial growth factor [...] Read more.
A crucial neuronal structure for the development and regeneration of neuronal networks is the axonal growth cone. Affected by different guidance cues, it grows in a predetermined direction to reach its final destination. One of those cues is the vascular endothelial growth factor (VEGF), which was identified as a positive effector for growth cone movement. These positive effects are mainly mediated by a reorganization of the actin network. This study shows that VEGF triggers a tight colocalization of cofilin and the Arp2/3 complex to the actin cytoskeleton within chicken dorsal root ganglia (DRG). Live cell imaging after microinjection of GFP (green fluorescent protein)-cofilin and RFP (red fluorescent protein)-LifeAct revealed that both labeled proteins rapidly redistributed within growth cones, and showed a congruent distribution pattern after VEGF supplementation. Disruption of signaling upstream of cofilin via blocking LIM-kinase (LIMK) activity resulted in growth cones displaying regressive growth behavior. Microinjection of GFP-p16b (a subunit of the Arp2/3 complex) and RFP-LifeAct revealed that both proteins redistributed into lamellipodia of the growth cone within minutes after VEGF stimulation. Disruption of the signaling to the Arp2/3 complex in the presence of VEGF by inhibition of N-WASP (neuronal Wiskott–Aldrich–Scott protein) caused retraction of growth cones. Hence, cofilin and the Arp2/3 complex appear to be downstream effector proteins of VEGF signaling to the actin cytoskeleton of DRG growth cones. Our data suggest that VEGF simultaneously affects different pathways for signaling to the actin cytoskeleton, since activation of cofilin occurs via inhibition of LIMK, whereas activation of Arp2/3 is achieved by stimulation of N-WASP. Full article
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