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Interplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43.

Gauthier-Kemper A, Igaev M, Sündermann F, Janning D, Brühmann J, Moschner K, Reyher HJ, Junge W, Glebov K, Walter J, Bakota L, Brandt R - Mol. Biol. Cell (2014)

Bottom Line: Plasma membrane association decreased the diffusion constant fourfold in neuritic shafts.Simulations confirmed that a combination of diffusion, dynamic plasma membrane interaction and active transport of a small fraction of GAP43 suffices for efficient sorting to growth cones.Our data demonstrate a complex interplay between phosphorylation and lipidation in mediating the localization of GAP43 in neuronal cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurobiology, University of Osnabrück, 49076 Osnabrück, Germany.

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Retention of GAP43 constructs differs in the cell body, the process shaft, and the tip of processes. Top, schematic representation of the position of photoactivation in neuronally differentiated PC12 cells. Bottom, fractions of fluorescence as indicator for the retention at the respective position. Note that retention correlates with the ability of the GAP43 constructs to interact with the plasma membrane except at the process tip. Mean ± SEM, n = 10–39.
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Figure 5: Retention of GAP43 constructs differs in the cell body, the process shaft, and the tip of processes. Top, schematic representation of the position of photoactivation in neuronally differentiated PC12 cells. Bottom, fractions of fluorescence as indicator for the retention at the respective position. Note that retention correlates with the ability of the GAP43 constructs to interact with the plasma membrane except at the process tip. Mean ± SEM, n = 10–39.

Mentions: Regulation of protein mobility by dynamic plasma membrane association may also contribute to the anchorage of proteins in specific compartments of a neuron, such as the growth cone. To test this hypothesis, we determined the retention of GAP43, the different phosphomutants, and the two reference proteins in the cell body, the process shaft, and the tip of processes using spatially restricted photoactivation experiments (Figure 5, top). Retention was quantified by determining the fraction of the fluorescent protein population in the activated segment 10 s after photoactivation (see Materials and Methods).


Interplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43.

Gauthier-Kemper A, Igaev M, Sündermann F, Janning D, Brühmann J, Moschner K, Reyher HJ, Junge W, Glebov K, Walter J, Bakota L, Brandt R - Mol. Biol. Cell (2014)

Retention of GAP43 constructs differs in the cell body, the process shaft, and the tip of processes. Top, schematic representation of the position of photoactivation in neuronally differentiated PC12 cells. Bottom, fractions of fluorescence as indicator for the retention at the respective position. Note that retention correlates with the ability of the GAP43 constructs to interact with the plasma membrane except at the process tip. Mean ± SEM, n = 10–39.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4214776&req=5

Figure 5: Retention of GAP43 constructs differs in the cell body, the process shaft, and the tip of processes. Top, schematic representation of the position of photoactivation in neuronally differentiated PC12 cells. Bottom, fractions of fluorescence as indicator for the retention at the respective position. Note that retention correlates with the ability of the GAP43 constructs to interact with the plasma membrane except at the process tip. Mean ± SEM, n = 10–39.
Mentions: Regulation of protein mobility by dynamic plasma membrane association may also contribute to the anchorage of proteins in specific compartments of a neuron, such as the growth cone. To test this hypothesis, we determined the retention of GAP43, the different phosphomutants, and the two reference proteins in the cell body, the process shaft, and the tip of processes using spatially restricted photoactivation experiments (Figure 5, top). Retention was quantified by determining the fraction of the fluorescent protein population in the activated segment 10 s after photoactivation (see Materials and Methods).

Bottom Line: Plasma membrane association decreased the diffusion constant fourfold in neuritic shafts.Simulations confirmed that a combination of diffusion, dynamic plasma membrane interaction and active transport of a small fraction of GAP43 suffices for efficient sorting to growth cones.Our data demonstrate a complex interplay between phosphorylation and lipidation in mediating the localization of GAP43 in neuronal cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurobiology, University of Osnabrück, 49076 Osnabrück, Germany.

Show MeSH
Related in: MedlinePlus